A Photobacterium sp. α2–6-sialyltransferase (Psp2,6ST) mutant with an increased expression level and improved activities in sialylating Tn antigens
In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Ding, Li [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015transfer abstract |
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| Schlagwörter: |
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| Umfang: |
7 |
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| Übergeordnetes Werk: |
Enthalten in: An analytical model of apparent viscosity in bleeding process - Wang, Xiaochen ELSEVIER, 2021, an international journal, Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:408 ; year:2015 ; day:18 ; month:05 ; pages:127-133 ; extent:7 |
| Links: |
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| DOI / URN: |
10.1016/j.carres.2014.12.007 |
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ELV034838856 |
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| 245 | 1 | 0 | |a A Photobacterium sp. α2–6-sialyltransferase (Psp2,6ST) mutant with an increased expression level and improved activities in sialylating Tn antigens |
| 264 | 1 | |c 2015transfer abstract | |
| 300 | |a 7 | ||
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| 520 | |a In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15–501)-His6 toward α-GalNAc-containing acceptors by 21–115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18–40mgL−1 for the wild-type enzyme to 72–110mgL−1 for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. Mutant A366G performed better than the wild-type Psp2,6ST(15–501)-His6 for synthesizing Neu5Acα2–6GalNAcαOSer/Thr STn antigens. | ||
| 520 | |a In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15–501)-His6 toward α-GalNAc-containing acceptors by 21–115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18–40mgL−1 for the wild-type enzyme to 72–110mgL−1 for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. Mutant A366G performed better than the wild-type Psp2,6ST(15–501)-His6 for synthesizing Neu5Acα2–6GalNAcαOSer/Thr STn antigens. | ||
| 650 | 7 | |a Mutagenesis |2 Elsevier | |
| 650 | 7 | |a Sialyltransferase mutant |2 Elsevier | |
| 650 | 7 | |a STn antigen |2 Elsevier | |
| 650 | 7 | |a Sialyltransferase |2 Elsevier | |
| 650 | 7 | |a Improved protein expression |2 Elsevier | |
| 700 | 1 | |a Zhao, Chao |4 oth | |
| 700 | 1 | |a Qu, Jingyao |4 oth | |
| 700 | 1 | |a Li, Yanhong |4 oth | |
| 700 | 1 | |a Sugiarto, Go |4 oth | |
| 700 | 1 | |a Yu, Hai |4 oth | |
| 700 | 1 | |a Wang, Junru |4 oth | |
| 700 | 1 | |a Chen, Xi |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier Science |a Wang, Xiaochen ELSEVIER |t An analytical model of apparent viscosity in bleeding process |d 2021 |d an international journal |g Amsterdam [u.a.] |w (DE-627)ELV006581838 |
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10.1016/j.carres.2014.12.007 doi GBVA2015020000001.pica (DE-627)ELV034838856 (ELSEVIER)S0008-6215(14)00459-5 DE-627 ger DE-627 rakwb eng 660 660 DE-600 690 VZ 56.45 bkl Ding, Li verfasserin aut A Photobacterium sp. α2–6-sialyltransferase (Psp2,6ST) mutant with an increased expression level and improved activities in sialylating Tn antigens 2015transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15–501)-His6 toward α-GalNAc-containing acceptors by 21–115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18–40mgL−1 for the wild-type enzyme to 72–110mgL−1 for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. Mutant A366G performed better than the wild-type Psp2,6ST(15–501)-His6 for synthesizing Neu5Acα2–6GalNAcαOSer/Thr STn antigens. In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15–501)-His6 toward α-GalNAc-containing acceptors by 21–115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18–40mgL−1 for the wild-type enzyme to 72–110mgL−1 for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. Mutant A366G performed better than the wild-type Psp2,6ST(15–501)-His6 for synthesizing Neu5Acα2–6GalNAcαOSer/Thr STn antigens. Mutagenesis Elsevier Sialyltransferase mutant Elsevier STn antigen Elsevier Sialyltransferase Elsevier Improved protein expression Elsevier Zhao, Chao oth Qu, Jingyao oth Li, Yanhong oth Sugiarto, Go oth Yu, Hai oth Wang, Junru oth Chen, Xi oth Enthalten in Elsevier Science Wang, Xiaochen ELSEVIER An analytical model of apparent viscosity in bleeding process 2021 an international journal Amsterdam [u.a.] (DE-627)ELV006581838 volume:408 year:2015 day:18 month:05 pages:127-133 extent:7 https://doi.org/10.1016/j.carres.2014.12.007 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 56.45 Baustoffkunde VZ AR 408 2015 18 0518 127-133 7 045F 660 |
| spelling |
10.1016/j.carres.2014.12.007 doi GBVA2015020000001.pica (DE-627)ELV034838856 (ELSEVIER)S0008-6215(14)00459-5 DE-627 ger DE-627 rakwb eng 660 660 DE-600 690 VZ 56.45 bkl Ding, Li verfasserin aut A Photobacterium sp. α2–6-sialyltransferase (Psp2,6ST) mutant with an increased expression level and improved activities in sialylating Tn antigens 2015transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15–501)-His6 toward α-GalNAc-containing acceptors by 21–115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18–40mgL−1 for the wild-type enzyme to 72–110mgL−1 for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. Mutant A366G performed better than the wild-type Psp2,6ST(15–501)-His6 for synthesizing Neu5Acα2–6GalNAcαOSer/Thr STn antigens. In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15–501)-His6 toward α-GalNAc-containing acceptors by 21–115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18–40mgL−1 for the wild-type enzyme to 72–110mgL−1 for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. Mutant A366G performed better than the wild-type Psp2,6ST(15–501)-His6 for synthesizing Neu5Acα2–6GalNAcαOSer/Thr STn antigens. Mutagenesis Elsevier Sialyltransferase mutant Elsevier STn antigen Elsevier Sialyltransferase Elsevier Improved protein expression Elsevier Zhao, Chao oth Qu, Jingyao oth Li, Yanhong oth Sugiarto, Go oth Yu, Hai oth Wang, Junru oth Chen, Xi oth Enthalten in Elsevier Science Wang, Xiaochen ELSEVIER An analytical model of apparent viscosity in bleeding process 2021 an international journal Amsterdam [u.a.] (DE-627)ELV006581838 volume:408 year:2015 day:18 month:05 pages:127-133 extent:7 https://doi.org/10.1016/j.carres.2014.12.007 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 56.45 Baustoffkunde VZ AR 408 2015 18 0518 127-133 7 045F 660 |
| allfields_unstemmed |
10.1016/j.carres.2014.12.007 doi GBVA2015020000001.pica (DE-627)ELV034838856 (ELSEVIER)S0008-6215(14)00459-5 DE-627 ger DE-627 rakwb eng 660 660 DE-600 690 VZ 56.45 bkl Ding, Li verfasserin aut A Photobacterium sp. α2–6-sialyltransferase (Psp2,6ST) mutant with an increased expression level and improved activities in sialylating Tn antigens 2015transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15–501)-His6 toward α-GalNAc-containing acceptors by 21–115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18–40mgL−1 for the wild-type enzyme to 72–110mgL−1 for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. Mutant A366G performed better than the wild-type Psp2,6ST(15–501)-His6 for synthesizing Neu5Acα2–6GalNAcαOSer/Thr STn antigens. In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15–501)-His6 toward α-GalNAc-containing acceptors by 21–115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18–40mgL−1 for the wild-type enzyme to 72–110mgL−1 for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. Mutant A366G performed better than the wild-type Psp2,6ST(15–501)-His6 for synthesizing Neu5Acα2–6GalNAcαOSer/Thr STn antigens. Mutagenesis Elsevier Sialyltransferase mutant Elsevier STn antigen Elsevier Sialyltransferase Elsevier Improved protein expression Elsevier Zhao, Chao oth Qu, Jingyao oth Li, Yanhong oth Sugiarto, Go oth Yu, Hai oth Wang, Junru oth Chen, Xi oth Enthalten in Elsevier Science Wang, Xiaochen ELSEVIER An analytical model of apparent viscosity in bleeding process 2021 an international journal Amsterdam [u.a.] (DE-627)ELV006581838 volume:408 year:2015 day:18 month:05 pages:127-133 extent:7 https://doi.org/10.1016/j.carres.2014.12.007 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 56.45 Baustoffkunde VZ AR 408 2015 18 0518 127-133 7 045F 660 |
| allfieldsGer |
10.1016/j.carres.2014.12.007 doi GBVA2015020000001.pica (DE-627)ELV034838856 (ELSEVIER)S0008-6215(14)00459-5 DE-627 ger DE-627 rakwb eng 660 660 DE-600 690 VZ 56.45 bkl Ding, Li verfasserin aut A Photobacterium sp. α2–6-sialyltransferase (Psp2,6ST) mutant with an increased expression level and improved activities in sialylating Tn antigens 2015transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15–501)-His6 toward α-GalNAc-containing acceptors by 21–115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18–40mgL−1 for the wild-type enzyme to 72–110mgL−1 for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. Mutant A366G performed better than the wild-type Psp2,6ST(15–501)-His6 for synthesizing Neu5Acα2–6GalNAcαOSer/Thr STn antigens. In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15–501)-His6 toward α-GalNAc-containing acceptors by 21–115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18–40mgL−1 for the wild-type enzyme to 72–110mgL−1 for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. Mutant A366G performed better than the wild-type Psp2,6ST(15–501)-His6 for synthesizing Neu5Acα2–6GalNAcαOSer/Thr STn antigens. Mutagenesis Elsevier Sialyltransferase mutant Elsevier STn antigen Elsevier Sialyltransferase Elsevier Improved protein expression Elsevier Zhao, Chao oth Qu, Jingyao oth Li, Yanhong oth Sugiarto, Go oth Yu, Hai oth Wang, Junru oth Chen, Xi oth Enthalten in Elsevier Science Wang, Xiaochen ELSEVIER An analytical model of apparent viscosity in bleeding process 2021 an international journal Amsterdam [u.a.] (DE-627)ELV006581838 volume:408 year:2015 day:18 month:05 pages:127-133 extent:7 https://doi.org/10.1016/j.carres.2014.12.007 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 56.45 Baustoffkunde VZ AR 408 2015 18 0518 127-133 7 045F 660 |
| allfieldsSound |
10.1016/j.carres.2014.12.007 doi GBVA2015020000001.pica (DE-627)ELV034838856 (ELSEVIER)S0008-6215(14)00459-5 DE-627 ger DE-627 rakwb eng 660 660 DE-600 690 VZ 56.45 bkl Ding, Li verfasserin aut A Photobacterium sp. α2–6-sialyltransferase (Psp2,6ST) mutant with an increased expression level and improved activities in sialylating Tn antigens 2015transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15–501)-His6 toward α-GalNAc-containing acceptors by 21–115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18–40mgL−1 for the wild-type enzyme to 72–110mgL−1 for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. Mutant A366G performed better than the wild-type Psp2,6ST(15–501)-His6 for synthesizing Neu5Acα2–6GalNAcαOSer/Thr STn antigens. In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15–501)-His6 toward α-GalNAc-containing acceptors by 21–115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18–40mgL−1 for the wild-type enzyme to 72–110mgL−1 for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. Mutant A366G performed better than the wild-type Psp2,6ST(15–501)-His6 for synthesizing Neu5Acα2–6GalNAcαOSer/Thr STn antigens. Mutagenesis Elsevier Sialyltransferase mutant Elsevier STn antigen Elsevier Sialyltransferase Elsevier Improved protein expression Elsevier Zhao, Chao oth Qu, Jingyao oth Li, Yanhong oth Sugiarto, Go oth Yu, Hai oth Wang, Junru oth Chen, Xi oth Enthalten in Elsevier Science Wang, Xiaochen ELSEVIER An analytical model of apparent viscosity in bleeding process 2021 an international journal Amsterdam [u.a.] (DE-627)ELV006581838 volume:408 year:2015 day:18 month:05 pages:127-133 extent:7 https://doi.org/10.1016/j.carres.2014.12.007 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 56.45 Baustoffkunde VZ AR 408 2015 18 0518 127-133 7 045F 660 |
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Enthalten in An analytical model of apparent viscosity in bleeding process Amsterdam [u.a.] volume:408 year:2015 day:18 month:05 pages:127-133 extent:7 |
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An analytical model of apparent viscosity in bleeding process |
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Ding, Li @@aut@@ Zhao, Chao @@oth@@ Qu, Jingyao @@oth@@ Li, Yanhong @@oth@@ Sugiarto, Go @@oth@@ Yu, Hai @@oth@@ Wang, Junru @@oth@@ Chen, Xi @@oth@@ |
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JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15–501)-His6 toward α-GalNAc-containing acceptors by 21–115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18–40mgL−1 for the wild-type enzyme to 72–110mgL−1 for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. 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a photobacterium sp. α2–6-sialyltransferase (psp2,6st) mutant with an increased expression level and improved activities in sialylating tn antigens |
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A Photobacterium sp. α2–6-sialyltransferase (Psp2,6ST) mutant with an increased expression level and improved activities in sialylating Tn antigens |
| abstract |
In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15–501)-His6 toward α-GalNAc-containing acceptors by 21–115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18–40mgL−1 for the wild-type enzyme to 72–110mgL−1 for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. Mutant A366G performed better than the wild-type Psp2,6ST(15–501)-His6 for synthesizing Neu5Acα2–6GalNAcαOSer/Thr STn antigens. |
| abstractGer |
In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15–501)-His6 toward α-GalNAc-containing acceptors by 21–115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18–40mgL−1 for the wild-type enzyme to 72–110mgL−1 for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. Mutant A366G performed better than the wild-type Psp2,6ST(15–501)-His6 for synthesizing Neu5Acα2–6GalNAcαOSer/Thr STn antigens. |
| abstract_unstemmed |
In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2–6-sialyltransferase Psp2,6ST(15–501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15–501)-His6 toward α-GalNAc-containing acceptors by 21–115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18–40mgL−1 for the wild-type enzyme to 72–110mgL−1 for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. Mutant A366G performed better than the wild-type Psp2,6ST(15–501)-His6 for synthesizing Neu5Acα2–6GalNAcαOSer/Thr STn antigens. |
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A Photobacterium sp. α2–6-sialyltransferase (Psp2,6ST) mutant with an increased expression level and improved activities in sialylating Tn antigens |
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