A Novel Adenosine Kinase from <i<Bombyx mori</i<: Enzymatic Activity, Structure, and Biological Function

Adenosine kinase (ADK) is the first enzyme in the adenosine remediation pathway that catalyzes adenosine phosphorylation into adenosine monophosphate, thus regulating adenosine homeostasis in cells. To obtain new insights into ADK from <i<Bombyx mori</i< (BmADK), we obtained recombinant...
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Autor*in:	Kai Song [verfasserIn] Yu Li [verfasserIn] Huawei He [verfasserIn] Lina Liu [verfasserIn] Ping Zhao [verfasserIn] Qingyou Xia [verfasserIn] Yejing Wang [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2019

Schlagwörter:	adenosine kinase enzymatic activity structure

Übergeordnetes Werk:	In: International Journal of Molecular Sciences - MDPI AG, 2003, 20(2019), 15, p 3732
Übergeordnetes Werk:	volume:20 ; year:2019 ; number:15, p 3732

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/ijms20153732

Katalog-ID:	DOAJ005509335

Internformat


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520			\|a Adenosine kinase (ADK) is the first enzyme in the adenosine remediation pathway that catalyzes adenosine phosphorylation into adenosine monophosphate, thus regulating adenosine homeostasis in cells. To obtain new insights into ADK from <i<Bombyx mori</i< (BmADK), we obtained recombinant BmADK, and analyzed its activity, structure, and function. Gel-filtration showed BmADK was a monomer with molecular weight of approximately 38 kDa. Circular dichroism spectra indicated BmADK had 36.8% α-helix and 29.9% β-strand structures, respectively. The structure of BmADK was stable in pH 5.0−11.0, and not affected under 30 °C. The melting temperature and the enthalpy and entropy changes in the thermal transition of BmADK were 46.51 ± 0.50 °C, 253.43 ± 0.20 KJ/mol, and 0.79 ± 0.01 KJ/(mol·K), respectively. Site-directed mutagenesis demonstrated G68, S201, E229, and D303 were key amino acids for BmADK structure and activity. In particular, S201A mutation significantly increased the α-helix content of BmADK and its activity. BmADK was located in the cytoplasm and highly expressed in the silk gland during the pre-pupal stage. RNA interference revealed the downregulation of <i<BmADK</i< decreased <i<ATG-8</i<, <i<Caspase-9</i<, <i<Ec-R</i<, <i<E74A</i<, and <i<Br-C</i< expression, indicating it was likely involved in 20E signaling, apoptosis, and autophagy to regulate silk gland degeneration and silkworm metamorphosis. Our study greatly expanded the knowledge on the activity, structure, and role of ADK.
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700	0		\|a Yejing Wang \|e verfasserin \|4 aut
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Indexfelder

author_variant	k s ks y l yl h h hh l l ll p z pz q x qx y w yw
matchkey_str	article:14220067:2019----::nvldnsnknsfoiobxoiezmtcciiytutr
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allfields	10.3390/ijms20153732 doi (DE-627)DOAJ005509335 (DE-599)DOAJf36ebc69d4fd4efa912951426acf11ad DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Kai Song verfasserin aut A Novel Adenosine Kinase from <i<Bombyx mori</i<: Enzymatic Activity, Structure, and Biological Function 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Adenosine kinase (ADK) is the first enzyme in the adenosine remediation pathway that catalyzes adenosine phosphorylation into adenosine monophosphate, thus regulating adenosine homeostasis in cells. To obtain new insights into ADK from <i<Bombyx mori</i< (BmADK), we obtained recombinant BmADK, and analyzed its activity, structure, and function. Gel-filtration showed BmADK was a monomer with molecular weight of approximately 38 kDa. Circular dichroism spectra indicated BmADK had 36.8% α-helix and 29.9% β-strand structures, respectively. The structure of BmADK was stable in pH 5.0−11.0, and not affected under 30 °C. The melting temperature and the enthalpy and entropy changes in the thermal transition of BmADK were 46.51 ± 0.50 °C, 253.43 ± 0.20 KJ/mol, and 0.79 ± 0.01 KJ/(mol·K), respectively. Site-directed mutagenesis demonstrated G68, S201, E229, and D303 were key amino acids for BmADK structure and activity. In particular, S201A mutation significantly increased the α-helix content of BmADK and its activity. BmADK was located in the cytoplasm and highly expressed in the silk gland during the pre-pupal stage. RNA interference revealed the downregulation of <i<BmADK</i< decreased <i<ATG-8</i<, <i<Caspase-9</i<, <i<Ec-R</i<, <i<E74A</i<, and <i<Br-C</i< expression, indicating it was likely involved in 20E signaling, apoptosis, and autophagy to regulate silk gland degeneration and silkworm metamorphosis. Our study greatly expanded the knowledge on the activity, structure, and role of ADK. adenosine kinase <i<Bombyx mori</i< enzymatic activity structure Biology (General) Chemistry Yu Li verfasserin aut Huawei He verfasserin aut Lina Liu verfasserin aut Ping Zhao verfasserin aut Qingyou Xia verfasserin aut Yejing Wang verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 20(2019), 15, p 3732 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:20 year:2019 number:15, p 3732 https://doi.org/10.3390/ijms20153732 kostenfrei https://doaj.org/article/f36ebc69d4fd4efa912951426acf11ad kostenfrei https://www.mdpi.com/1422-0067/20/15/3732 kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 20 2019 15, p 3732
spelling	10.3390/ijms20153732 doi (DE-627)DOAJ005509335 (DE-599)DOAJf36ebc69d4fd4efa912951426acf11ad DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Kai Song verfasserin aut A Novel Adenosine Kinase from <i<Bombyx mori</i<: Enzymatic Activity, Structure, and Biological Function 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Adenosine kinase (ADK) is the first enzyme in the adenosine remediation pathway that catalyzes adenosine phosphorylation into adenosine monophosphate, thus regulating adenosine homeostasis in cells. To obtain new insights into ADK from <i<Bombyx mori</i< (BmADK), we obtained recombinant BmADK, and analyzed its activity, structure, and function. Gel-filtration showed BmADK was a monomer with molecular weight of approximately 38 kDa. Circular dichroism spectra indicated BmADK had 36.8% α-helix and 29.9% β-strand structures, respectively. The structure of BmADK was stable in pH 5.0−11.0, and not affected under 30 °C. The melting temperature and the enthalpy and entropy changes in the thermal transition of BmADK were 46.51 ± 0.50 °C, 253.43 ± 0.20 KJ/mol, and 0.79 ± 0.01 KJ/(mol·K), respectively. Site-directed mutagenesis demonstrated G68, S201, E229, and D303 were key amino acids for BmADK structure and activity. In particular, S201A mutation significantly increased the α-helix content of BmADK and its activity. BmADK was located in the cytoplasm and highly expressed in the silk gland during the pre-pupal stage. RNA interference revealed the downregulation of <i<BmADK</i< decreased <i<ATG-8</i<, <i<Caspase-9</i<, <i<Ec-R</i<, <i<E74A</i<, and <i<Br-C</i< expression, indicating it was likely involved in 20E signaling, apoptosis, and autophagy to regulate silk gland degeneration and silkworm metamorphosis. Our study greatly expanded the knowledge on the activity, structure, and role of ADK. adenosine kinase <i<Bombyx mori</i< enzymatic activity structure Biology (General) Chemistry Yu Li verfasserin aut Huawei He verfasserin aut Lina Liu verfasserin aut Ping Zhao verfasserin aut Qingyou Xia verfasserin aut Yejing Wang verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 20(2019), 15, p 3732 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:20 year:2019 number:15, p 3732 https://doi.org/10.3390/ijms20153732 kostenfrei https://doaj.org/article/f36ebc69d4fd4efa912951426acf11ad kostenfrei https://www.mdpi.com/1422-0067/20/15/3732 kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 20 2019 15, p 3732
allfields_unstemmed	10.3390/ijms20153732 doi (DE-627)DOAJ005509335 (DE-599)DOAJf36ebc69d4fd4efa912951426acf11ad DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Kai Song verfasserin aut A Novel Adenosine Kinase from <i<Bombyx mori</i<: Enzymatic Activity, Structure, and Biological Function 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Adenosine kinase (ADK) is the first enzyme in the adenosine remediation pathway that catalyzes adenosine phosphorylation into adenosine monophosphate, thus regulating adenosine homeostasis in cells. To obtain new insights into ADK from <i<Bombyx mori</i< (BmADK), we obtained recombinant BmADK, and analyzed its activity, structure, and function. Gel-filtration showed BmADK was a monomer with molecular weight of approximately 38 kDa. Circular dichroism spectra indicated BmADK had 36.8% α-helix and 29.9% β-strand structures, respectively. The structure of BmADK was stable in pH 5.0−11.0, and not affected under 30 °C. The melting temperature and the enthalpy and entropy changes in the thermal transition of BmADK were 46.51 ± 0.50 °C, 253.43 ± 0.20 KJ/mol, and 0.79 ± 0.01 KJ/(mol·K), respectively. Site-directed mutagenesis demonstrated G68, S201, E229, and D303 were key amino acids for BmADK structure and activity. In particular, S201A mutation significantly increased the α-helix content of BmADK and its activity. BmADK was located in the cytoplasm and highly expressed in the silk gland during the pre-pupal stage. RNA interference revealed the downregulation of <i<BmADK</i< decreased <i<ATG-8</i<, <i<Caspase-9</i<, <i<Ec-R</i<, <i<E74A</i<, and <i<Br-C</i< expression, indicating it was likely involved in 20E signaling, apoptosis, and autophagy to regulate silk gland degeneration and silkworm metamorphosis. Our study greatly expanded the knowledge on the activity, structure, and role of ADK. adenosine kinase <i<Bombyx mori</i< enzymatic activity structure Biology (General) Chemistry Yu Li verfasserin aut Huawei He verfasserin aut Lina Liu verfasserin aut Ping Zhao verfasserin aut Qingyou Xia verfasserin aut Yejing Wang verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 20(2019), 15, p 3732 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:20 year:2019 number:15, p 3732 https://doi.org/10.3390/ijms20153732 kostenfrei https://doaj.org/article/f36ebc69d4fd4efa912951426acf11ad kostenfrei https://www.mdpi.com/1422-0067/20/15/3732 kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 20 2019 15, p 3732
allfieldsGer	10.3390/ijms20153732 doi (DE-627)DOAJ005509335 (DE-599)DOAJf36ebc69d4fd4efa912951426acf11ad DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Kai Song verfasserin aut A Novel Adenosine Kinase from <i<Bombyx mori</i<: Enzymatic Activity, Structure, and Biological Function 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Adenosine kinase (ADK) is the first enzyme in the adenosine remediation pathway that catalyzes adenosine phosphorylation into adenosine monophosphate, thus regulating adenosine homeostasis in cells. To obtain new insights into ADK from <i<Bombyx mori</i< (BmADK), we obtained recombinant BmADK, and analyzed its activity, structure, and function. Gel-filtration showed BmADK was a monomer with molecular weight of approximately 38 kDa. Circular dichroism spectra indicated BmADK had 36.8% α-helix and 29.9% β-strand structures, respectively. The structure of BmADK was stable in pH 5.0−11.0, and not affected under 30 °C. The melting temperature and the enthalpy and entropy changes in the thermal transition of BmADK were 46.51 ± 0.50 °C, 253.43 ± 0.20 KJ/mol, and 0.79 ± 0.01 KJ/(mol·K), respectively. Site-directed mutagenesis demonstrated G68, S201, E229, and D303 were key amino acids for BmADK structure and activity. In particular, S201A mutation significantly increased the α-helix content of BmADK and its activity. BmADK was located in the cytoplasm and highly expressed in the silk gland during the pre-pupal stage. RNA interference revealed the downregulation of <i<BmADK</i< decreased <i<ATG-8</i<, <i<Caspase-9</i<, <i<Ec-R</i<, <i<E74A</i<, and <i<Br-C</i< expression, indicating it was likely involved in 20E signaling, apoptosis, and autophagy to regulate silk gland degeneration and silkworm metamorphosis. Our study greatly expanded the knowledge on the activity, structure, and role of ADK. adenosine kinase <i<Bombyx mori</i< enzymatic activity structure Biology (General) Chemistry Yu Li verfasserin aut Huawei He verfasserin aut Lina Liu verfasserin aut Ping Zhao verfasserin aut Qingyou Xia verfasserin aut Yejing Wang verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 20(2019), 15, p 3732 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:20 year:2019 number:15, p 3732 https://doi.org/10.3390/ijms20153732 kostenfrei https://doaj.org/article/f36ebc69d4fd4efa912951426acf11ad kostenfrei https://www.mdpi.com/1422-0067/20/15/3732 kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 20 2019 15, p 3732
allfieldsSound	10.3390/ijms20153732 doi (DE-627)DOAJ005509335 (DE-599)DOAJf36ebc69d4fd4efa912951426acf11ad DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Kai Song verfasserin aut A Novel Adenosine Kinase from <i<Bombyx mori</i<: Enzymatic Activity, Structure, and Biological Function 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Adenosine kinase (ADK) is the first enzyme in the adenosine remediation pathway that catalyzes adenosine phosphorylation into adenosine monophosphate, thus regulating adenosine homeostasis in cells. To obtain new insights into ADK from <i<Bombyx mori</i< (BmADK), we obtained recombinant BmADK, and analyzed its activity, structure, and function. Gel-filtration showed BmADK was a monomer with molecular weight of approximately 38 kDa. Circular dichroism spectra indicated BmADK had 36.8% α-helix and 29.9% β-strand structures, respectively. The structure of BmADK was stable in pH 5.0−11.0, and not affected under 30 °C. The melting temperature and the enthalpy and entropy changes in the thermal transition of BmADK were 46.51 ± 0.50 °C, 253.43 ± 0.20 KJ/mol, and 0.79 ± 0.01 KJ/(mol·K), respectively. Site-directed mutagenesis demonstrated G68, S201, E229, and D303 were key amino acids for BmADK structure and activity. In particular, S201A mutation significantly increased the α-helix content of BmADK and its activity. BmADK was located in the cytoplasm and highly expressed in the silk gland during the pre-pupal stage. RNA interference revealed the downregulation of <i<BmADK</i< decreased <i<ATG-8</i<, <i<Caspase-9</i<, <i<Ec-R</i<, <i<E74A</i<, and <i<Br-C</i< expression, indicating it was likely involved in 20E signaling, apoptosis, and autophagy to regulate silk gland degeneration and silkworm metamorphosis. Our study greatly expanded the knowledge on the activity, structure, and role of ADK. adenosine kinase <i<Bombyx mori</i< enzymatic activity structure Biology (General) Chemistry Yu Li verfasserin aut Huawei He verfasserin aut Lina Liu verfasserin aut Ping Zhao verfasserin aut Qingyou Xia verfasserin aut Yejing Wang verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 20(2019), 15, p 3732 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:20 year:2019 number:15, p 3732 https://doi.org/10.3390/ijms20153732 kostenfrei https://doaj.org/article/f36ebc69d4fd4efa912951426acf11ad kostenfrei https://www.mdpi.com/1422-0067/20/15/3732 kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 20 2019 15, p 3732
language	English
source	In International Journal of Molecular Sciences 20(2019), 15, p 3732 volume:20 year:2019 number:15, p 3732
sourceStr	In International Journal of Molecular Sciences 20(2019), 15, p 3732 volume:20 year:2019 number:15, p 3732
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	adenosine kinase <i<Bombyx mori</i< enzymatic activity structure Biology (General) Chemistry
isfreeaccess_bool	true
container_title	International Journal of Molecular Sciences
authorswithroles_txt_mv	Kai Song @@aut@@ Yu Li @@aut@@ Huawei He @@aut@@ Lina Liu @@aut@@ Ping Zhao @@aut@@ Qingyou Xia @@aut@@ Yejing Wang @@aut@@
publishDateDaySort_date	2019-01-01T00:00:00Z
hierarchy_top_id	316340715
id	DOAJ005509335
language_de	englisch
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callnumber-first	Q - Science
author	Kai Song
spellingShingle	Kai Song misc QH301-705.5 misc QD1-999 misc adenosine kinase misc <i<Bombyx mori</i< misc enzymatic activity misc structure misc Biology (General) misc Chemistry A Novel Adenosine Kinase from <i<Bombyx mori</i<: Enzymatic Activity, Structure, and Biological Function
authorStr	Kai Song
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topic_title	QH301-705.5 QD1-999 A Novel Adenosine Kinase from <i<Bombyx mori</i<: Enzymatic Activity, Structure, and Biological Function adenosine kinase <i<Bombyx mori</i< enzymatic activity structure
topic	misc QH301-705.5 misc QD1-999 misc adenosine kinase misc <i<Bombyx mori</i< misc enzymatic activity misc structure misc Biology (General) misc Chemistry
topic_unstemmed	misc QH301-705.5 misc QD1-999 misc adenosine kinase misc <i<Bombyx mori</i< misc enzymatic activity misc structure misc Biology (General) misc Chemistry
topic_browse	misc QH301-705.5 misc QD1-999 misc adenosine kinase misc <i<Bombyx mori</i< misc enzymatic activity misc structure misc Biology (General) misc Chemistry
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title	A Novel Adenosine Kinase from <i<Bombyx mori</i<: Enzymatic Activity, Structure, and Biological Function
ctrlnum	(DE-627)DOAJ005509335 (DE-599)DOAJf36ebc69d4fd4efa912951426acf11ad
title_full	A Novel Adenosine Kinase from <i<Bombyx mori</i<: Enzymatic Activity, Structure, and Biological Function
author_sort	Kai Song
journal	International Journal of Molecular Sciences
journalStr	International Journal of Molecular Sciences
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author_browse	Kai Song Yu Li Huawei He Lina Liu Ping Zhao Qingyou Xia Yejing Wang
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author-letter	Kai Song
doi_str_mv	10.3390/ijms20153732
author2-role	verfasserin
title_sort	novel adenosine kinase from <i<bombyx mori</i<: enzymatic activity, structure, and biological function
callnumber	QH301-705.5
title_auth	A Novel Adenosine Kinase from <i<Bombyx mori</i<: Enzymatic Activity, Structure, and Biological Function
abstract	Adenosine kinase (ADK) is the first enzyme in the adenosine remediation pathway that catalyzes adenosine phosphorylation into adenosine monophosphate, thus regulating adenosine homeostasis in cells. To obtain new insights into ADK from <i<Bombyx mori</i< (BmADK), we obtained recombinant BmADK, and analyzed its activity, structure, and function. Gel-filtration showed BmADK was a monomer with molecular weight of approximately 38 kDa. Circular dichroism spectra indicated BmADK had 36.8% α-helix and 29.9% β-strand structures, respectively. The structure of BmADK was stable in pH 5.0−11.0, and not affected under 30 °C. The melting temperature and the enthalpy and entropy changes in the thermal transition of BmADK were 46.51 ± 0.50 °C, 253.43 ± 0.20 KJ/mol, and 0.79 ± 0.01 KJ/(mol·K), respectively. Site-directed mutagenesis demonstrated G68, S201, E229, and D303 were key amino acids for BmADK structure and activity. In particular, S201A mutation significantly increased the α-helix content of BmADK and its activity. BmADK was located in the cytoplasm and highly expressed in the silk gland during the pre-pupal stage. RNA interference revealed the downregulation of <i<BmADK</i< decreased <i<ATG-8</i<, <i<Caspase-9</i<, <i<Ec-R</i<, <i<E74A</i<, and <i<Br-C</i< expression, indicating it was likely involved in 20E signaling, apoptosis, and autophagy to regulate silk gland degeneration and silkworm metamorphosis. Our study greatly expanded the knowledge on the activity, structure, and role of ADK.
abstractGer	Adenosine kinase (ADK) is the first enzyme in the adenosine remediation pathway that catalyzes adenosine phosphorylation into adenosine monophosphate, thus regulating adenosine homeostasis in cells. To obtain new insights into ADK from <i<Bombyx mori</i< (BmADK), we obtained recombinant BmADK, and analyzed its activity, structure, and function. Gel-filtration showed BmADK was a monomer with molecular weight of approximately 38 kDa. Circular dichroism spectra indicated BmADK had 36.8% α-helix and 29.9% β-strand structures, respectively. The structure of BmADK was stable in pH 5.0−11.0, and not affected under 30 °C. The melting temperature and the enthalpy and entropy changes in the thermal transition of BmADK were 46.51 ± 0.50 °C, 253.43 ± 0.20 KJ/mol, and 0.79 ± 0.01 KJ/(mol·K), respectively. Site-directed mutagenesis demonstrated G68, S201, E229, and D303 were key amino acids for BmADK structure and activity. In particular, S201A mutation significantly increased the α-helix content of BmADK and its activity. BmADK was located in the cytoplasm and highly expressed in the silk gland during the pre-pupal stage. RNA interference revealed the downregulation of <i<BmADK</i< decreased <i<ATG-8</i<, <i<Caspase-9</i<, <i<Ec-R</i<, <i<E74A</i<, and <i<Br-C</i< expression, indicating it was likely involved in 20E signaling, apoptosis, and autophagy to regulate silk gland degeneration and silkworm metamorphosis. Our study greatly expanded the knowledge on the activity, structure, and role of ADK.
abstract_unstemmed	Adenosine kinase (ADK) is the first enzyme in the adenosine remediation pathway that catalyzes adenosine phosphorylation into adenosine monophosphate, thus regulating adenosine homeostasis in cells. To obtain new insights into ADK from <i<Bombyx mori</i< (BmADK), we obtained recombinant BmADK, and analyzed its activity, structure, and function. Gel-filtration showed BmADK was a monomer with molecular weight of approximately 38 kDa. Circular dichroism spectra indicated BmADK had 36.8% α-helix and 29.9% β-strand structures, respectively. The structure of BmADK was stable in pH 5.0−11.0, and not affected under 30 °C. The melting temperature and the enthalpy and entropy changes in the thermal transition of BmADK were 46.51 ± 0.50 °C, 253.43 ± 0.20 KJ/mol, and 0.79 ± 0.01 KJ/(mol·K), respectively. Site-directed mutagenesis demonstrated G68, S201, E229, and D303 were key amino acids for BmADK structure and activity. In particular, S201A mutation significantly increased the α-helix content of BmADK and its activity. BmADK was located in the cytoplasm and highly expressed in the silk gland during the pre-pupal stage. RNA interference revealed the downregulation of <i<BmADK</i< decreased <i<ATG-8</i<, <i<Caspase-9</i<, <i<Ec-R</i<, <i<E74A</i<, and <i<Br-C</i< expression, indicating it was likely involved in 20E signaling, apoptosis, and autophagy to regulate silk gland degeneration and silkworm metamorphosis. Our study greatly expanded the knowledge on the activity, structure, and role of ADK.
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container_issue	15, p 3732
title_short	A Novel Adenosine Kinase from <i<Bombyx mori</i<: Enzymatic Activity, Structure, and Biological Function
url	https://doi.org/10.3390/ijms20153732 https://doaj.org/article/f36ebc69d4fd4efa912951426acf11ad https://www.mdpi.com/1422-0067/20/15/3732 https://doaj.org/toc/1422-0067
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up_date	2024-07-03T15:27:21.235Z
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