Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani
The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Are, Sayanna [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2020transfer abstract |
|---|
| Umfang: |
16 |
|---|
| Übergeordnetes Werk: |
Enthalten in: Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor - Penchovsky, Robert ELSEVIER, 2019, structure, function and interactions, New York, NY [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:152 ; year:2020 ; day:1 ; month:06 ; pages:812-827 ; extent:16 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.ijbiomac.2020.02.257 |
|---|
| Katalog-ID: |
ELV050105167 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | ELV050105167 | ||
| 003 | DE-627 | ||
| 005 | 20230626025824.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 200518s2020 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1016/j.ijbiomac.2020.02.257 |2 doi | |
| 028 | 5 | 2 | |a /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000988.pica |
| 035 | |a (DE-627)ELV050105167 | ||
| 035 | |a (ELSEVIER)S0141-8130(19)37798-0 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 082 | 0 | 4 | |a 570 |a 610 |q VZ |
| 084 | |a 58.30 |2 bkl | ||
| 084 | |a 50.22 |2 bkl | ||
| 084 | |a 44.09 |2 bkl | ||
| 100 | 1 | |a Are, Sayanna |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani |
| 264 | 1 | |c 2020transfer abstract | |
| 300 | |a 16 | ||
| 336 | |a nicht spezifiziert |b zzz |2 rdacontent | ||
| 337 | |a nicht spezifiziert |b z |2 rdamedia | ||
| 338 | |a nicht spezifiziert |b zu |2 rdacarrier | ||
| 520 | |a The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors. | ||
| 520 | |a The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors. | ||
| 700 | 1 | |a Gatreddi, Santhosh |4 oth | |
| 700 | 1 | |a Jakkula, Pranay |4 oth | |
| 700 | 1 | |a Qureshi, Insaf Ahmed |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier |a Penchovsky, Robert ELSEVIER |t Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor |d 2019 |d structure, function and interactions |g New York, NY [u.a.] |w (DE-627)ELV002200198 |
| 773 | 1 | 8 | |g volume:152 |g year:2020 |g day:1 |g month:06 |g pages:812-827 |g extent:16 |
| 856 | 4 | 0 | |u https://doi.org/10.1016/j.ijbiomac.2020.02.257 |3 Volltext |
| 912 | |a GBV_USEFLAG_U | ||
| 912 | |a GBV_ELV | ||
| 912 | |a SYSFLAG_U | ||
| 912 | |a SSG-OLC-PHA | ||
| 936 | b | k | |a 58.30 |j Biotechnologie |q VZ |
| 936 | b | k | |a 50.22 |j Sensorik |q VZ |
| 936 | b | k | |a 44.09 |j Medizintechnik |q VZ |
| 951 | |a AR | ||
| 952 | |d 152 |j 2020 |b 1 |c 0601 |h 812-827 |g 16 | ||
| author_variant |
s a sa |
|---|---|
| matchkey_str |
aresayannagatreddisanthoshjakkulapranayq:2020----:tutrltrbtsnsbtaepcfctoprdxliae |
| hierarchy_sort_str |
2020transfer abstract |
| bklnumber |
58.30 50.22 44.09 |
| publishDate |
2020 |
| allfields |
10.1016/j.ijbiomac.2020.02.257 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000988.pica (DE-627)ELV050105167 (ELSEVIER)S0141-8130(19)37798-0 DE-627 ger DE-627 rakwb eng 570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl Are, Sayanna verfasserin aut Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani 2020transfer abstract 16 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors. The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors. Gatreddi, Santhosh oth Jakkula, Pranay oth Qureshi, Insaf Ahmed oth Enthalten in Elsevier Penchovsky, Robert ELSEVIER Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor 2019 structure, function and interactions New York, NY [u.a.] (DE-627)ELV002200198 volume:152 year:2020 day:1 month:06 pages:812-827 extent:16 https://doi.org/10.1016/j.ijbiomac.2020.02.257 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.30 Biotechnologie VZ 50.22 Sensorik VZ 44.09 Medizintechnik VZ AR 152 2020 1 0601 812-827 16 |
| spelling |
10.1016/j.ijbiomac.2020.02.257 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000988.pica (DE-627)ELV050105167 (ELSEVIER)S0141-8130(19)37798-0 DE-627 ger DE-627 rakwb eng 570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl Are, Sayanna verfasserin aut Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani 2020transfer abstract 16 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors. The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors. Gatreddi, Santhosh oth Jakkula, Pranay oth Qureshi, Insaf Ahmed oth Enthalten in Elsevier Penchovsky, Robert ELSEVIER Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor 2019 structure, function and interactions New York, NY [u.a.] (DE-627)ELV002200198 volume:152 year:2020 day:1 month:06 pages:812-827 extent:16 https://doi.org/10.1016/j.ijbiomac.2020.02.257 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.30 Biotechnologie VZ 50.22 Sensorik VZ 44.09 Medizintechnik VZ AR 152 2020 1 0601 812-827 16 |
| allfields_unstemmed |
10.1016/j.ijbiomac.2020.02.257 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000988.pica (DE-627)ELV050105167 (ELSEVIER)S0141-8130(19)37798-0 DE-627 ger DE-627 rakwb eng 570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl Are, Sayanna verfasserin aut Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani 2020transfer abstract 16 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors. The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors. Gatreddi, Santhosh oth Jakkula, Pranay oth Qureshi, Insaf Ahmed oth Enthalten in Elsevier Penchovsky, Robert ELSEVIER Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor 2019 structure, function and interactions New York, NY [u.a.] (DE-627)ELV002200198 volume:152 year:2020 day:1 month:06 pages:812-827 extent:16 https://doi.org/10.1016/j.ijbiomac.2020.02.257 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.30 Biotechnologie VZ 50.22 Sensorik VZ 44.09 Medizintechnik VZ AR 152 2020 1 0601 812-827 16 |
| allfieldsGer |
10.1016/j.ijbiomac.2020.02.257 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000988.pica (DE-627)ELV050105167 (ELSEVIER)S0141-8130(19)37798-0 DE-627 ger DE-627 rakwb eng 570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl Are, Sayanna verfasserin aut Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani 2020transfer abstract 16 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors. The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors. Gatreddi, Santhosh oth Jakkula, Pranay oth Qureshi, Insaf Ahmed oth Enthalten in Elsevier Penchovsky, Robert ELSEVIER Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor 2019 structure, function and interactions New York, NY [u.a.] (DE-627)ELV002200198 volume:152 year:2020 day:1 month:06 pages:812-827 extent:16 https://doi.org/10.1016/j.ijbiomac.2020.02.257 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.30 Biotechnologie VZ 50.22 Sensorik VZ 44.09 Medizintechnik VZ AR 152 2020 1 0601 812-827 16 |
| allfieldsSound |
10.1016/j.ijbiomac.2020.02.257 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000988.pica (DE-627)ELV050105167 (ELSEVIER)S0141-8130(19)37798-0 DE-627 ger DE-627 rakwb eng 570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl Are, Sayanna verfasserin aut Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani 2020transfer abstract 16 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors. The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors. Gatreddi, Santhosh oth Jakkula, Pranay oth Qureshi, Insaf Ahmed oth Enthalten in Elsevier Penchovsky, Robert ELSEVIER Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor 2019 structure, function and interactions New York, NY [u.a.] (DE-627)ELV002200198 volume:152 year:2020 day:1 month:06 pages:812-827 extent:16 https://doi.org/10.1016/j.ijbiomac.2020.02.257 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.30 Biotechnologie VZ 50.22 Sensorik VZ 44.09 Medizintechnik VZ AR 152 2020 1 0601 812-827 16 |
| language |
English |
| source |
Enthalten in Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor New York, NY [u.a.] volume:152 year:2020 day:1 month:06 pages:812-827 extent:16 |
| sourceStr |
Enthalten in Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor New York, NY [u.a.] volume:152 year:2020 day:1 month:06 pages:812-827 extent:16 |
| format_phy_str_mv |
Article |
| bklname |
Biotechnologie Sensorik Medizintechnik |
| institution |
findex.gbv.de |
| dewey-raw |
570 |
| isfreeaccess_bool |
false |
| container_title |
Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor |
| authorswithroles_txt_mv |
Are, Sayanna @@aut@@ Gatreddi, Santhosh @@oth@@ Jakkula, Pranay @@oth@@ Qureshi, Insaf Ahmed @@oth@@ |
| publishDateDaySort_date |
2020-01-01T00:00:00Z |
| hierarchy_top_id |
ELV002200198 |
| dewey-sort |
3570 |
| id |
ELV050105167 |
| language_de |
englisch |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">ELV050105167</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230626025824.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">200518s2020 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.ijbiomac.2020.02.257</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">/cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000988.pica</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV050105167</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S0141-8130(19)37798-0</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="a">610</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">58.30</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">50.22</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">44.09</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Are, Sayanna</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2020transfer abstract</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">16</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gatreddi, Santhosh</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Jakkula, Pranay</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Qureshi, Insaf Ahmed</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="n">Elsevier</subfield><subfield code="a">Penchovsky, Robert ELSEVIER</subfield><subfield code="t">Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor</subfield><subfield code="d">2019</subfield><subfield code="d">structure, function and interactions</subfield><subfield code="g">New York, NY [u.a.]</subfield><subfield code="w">(DE-627)ELV002200198</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:152</subfield><subfield code="g">year:2020</subfield><subfield code="g">day:1</subfield><subfield code="g">month:06</subfield><subfield code="g">pages:812-827</subfield><subfield code="g">extent:16</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://doi.org/10.1016/j.ijbiomac.2020.02.257</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ELV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">58.30</subfield><subfield code="j">Biotechnologie</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">50.22</subfield><subfield code="j">Sensorik</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">44.09</subfield><subfield code="j">Medizintechnik</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">152</subfield><subfield code="j">2020</subfield><subfield code="b">1</subfield><subfield code="c">0601</subfield><subfield code="h">812-827</subfield><subfield code="g">16</subfield></datafield></record></collection>
|
| author |
Are, Sayanna |
| spellingShingle |
Are, Sayanna ddc 570 bkl 58.30 bkl 50.22 bkl 44.09 Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani |
| authorStr |
Are, Sayanna |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)ELV002200198 |
| format |
electronic Article |
| dewey-ones |
570 - Life sciences; biology 610 - Medicine & health |
| delete_txt_mv |
keep |
| author_role |
aut |
| collection |
elsevier |
| remote_str |
true |
| illustrated |
Not Illustrated |
| topic_title |
570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani |
| topic |
ddc 570 bkl 58.30 bkl 50.22 bkl 44.09 |
| topic_unstemmed |
ddc 570 bkl 58.30 bkl 50.22 bkl 44.09 |
| topic_browse |
ddc 570 bkl 58.30 bkl 50.22 bkl 44.09 |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| author2_variant |
s g sg p j pj i a q ia iaq |
| hierarchy_parent_title |
Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor |
| hierarchy_parent_id |
ELV002200198 |
| dewey-tens |
570 - Life sciences; biology 610 - Medicine & health |
| hierarchy_top_title |
Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)ELV002200198 |
| title |
Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani |
| ctrlnum |
(DE-627)ELV050105167 (ELSEVIER)S0141-8130(19)37798-0 |
| title_full |
Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani |
| author_sort |
Are, Sayanna |
| journal |
Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor |
| journalStr |
Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor |
| lang_code |
eng |
| isOA_bool |
false |
| dewey-hundreds |
500 - Science 600 - Technology |
| recordtype |
marc |
| publishDateSort |
2020 |
| contenttype_str_mv |
zzz |
| container_start_page |
812 |
| author_browse |
Are, Sayanna |
| container_volume |
152 |
| physical |
16 |
| class |
570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl |
| format_se |
Elektronische Aufsätze |
| author-letter |
Are, Sayanna |
| doi_str_mv |
10.1016/j.ijbiomac.2020.02.257 |
| dewey-full |
570 610 |
| title_sort |
structural attributes and substrate specificity of pyridoxal kinase from leishmania donovani |
| title_auth |
Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani |
| abstract |
The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors. |
| abstractGer |
The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors. |
| abstract_unstemmed |
The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors. |
| collection_details |
GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA |
| title_short |
Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani |
| url |
https://doi.org/10.1016/j.ijbiomac.2020.02.257 |
| remote_bool |
true |
| author2 |
Gatreddi, Santhosh Jakkula, Pranay Qureshi, Insaf Ahmed |
| author2Str |
Gatreddi, Santhosh Jakkula, Pranay Qureshi, Insaf Ahmed |
| ppnlink |
ELV002200198 |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth oth oth |
| doi_str |
10.1016/j.ijbiomac.2020.02.257 |
| up_date |
2024-07-06T16:37:29.356Z |
| _version_ |
1803848357624414208 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">ELV050105167</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230626025824.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">200518s2020 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.ijbiomac.2020.02.257</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">/cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000988.pica</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV050105167</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S0141-8130(19)37798-0</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="a">610</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">58.30</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">50.22</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">44.09</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Are, Sayanna</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Structural attributes and substrate specificity of pyridoxal kinase from Leishmania donovani</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2020transfer abstract</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">16</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination, decarboxylation and deamination. In the present study, full-length ORF of PdxK from Leishmania donovani (LdPdxK) was cloned and then purified using affinity chromatography. LdPdxK exists as a homo-dimer in solution and shows more activity at near to physiological pH. Biochemical analysis of LdPdxK with pyridoxal, pyridoxamine, pyridoxine and ginkgotoxin revealed its affinity preference towards different substrates. The secondary structure analysis using circular dichroism spectroscopy showed LdPdxK to be predominantly α-helical in organization which tends to decline at lower and higher pH. Simultaneously, LdPdxK was crystallized and its three-dimensional structure in complex with ADP and different substrates were determined. Crystal structure of LdPdxK delineated that it has a central core of β-sheets surrounded by α-helices with a conserved GTGD ribokinase motif. The structures of LdPdxK disclosed no major structural changes between ADP and ADP- substrate bound structures. In addition, comparative structural analysis highlighted the key differences between the active site pockets of leishmanial and human PdxK, rendering LdPdxK an attractive candidate for the designing of novel and specific inhibitors.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gatreddi, Santhosh</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Jakkula, Pranay</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Qureshi, Insaf Ahmed</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="n">Elsevier</subfield><subfield code="a">Penchovsky, Robert ELSEVIER</subfield><subfield code="t">Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor</subfield><subfield code="d">2019</subfield><subfield code="d">structure, function and interactions</subfield><subfield code="g">New York, NY [u.a.]</subfield><subfield code="w">(DE-627)ELV002200198</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:152</subfield><subfield code="g">year:2020</subfield><subfield code="g">day:1</subfield><subfield code="g">month:06</subfield><subfield code="g">pages:812-827</subfield><subfield code="g">extent:16</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://doi.org/10.1016/j.ijbiomac.2020.02.257</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ELV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">58.30</subfield><subfield code="j">Biotechnologie</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">50.22</subfield><subfield code="j">Sensorik</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">44.09</subfield><subfield code="j">Medizintechnik</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">152</subfield><subfield code="j">2020</subfield><subfield code="b">1</subfield><subfield code="c">0601</subfield><subfield code="h">812-827</subfield><subfield code="g">16</subfield></datafield></record></collection>
|
| score |
7.400342 |