Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine
Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxyl...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Yang, Yao [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2010 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer Science+Business Media B.V. 2010 |
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| Übergeordnetes Werk: |
Enthalten in: Biodegradation - Springer Netherlands, 1990, 21(2010), 4 vom: 02. Feb., Seite 593-602 |
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| Übergeordnetes Werk: |
volume:21 ; year:2010 ; number:4 ; day:02 ; month:02 ; pages:593-602 |
| Links: |
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| DOI / URN: |
10.1007/s10532-010-9327-2 |
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OLC2050401442 |
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| 245 | 1 | 0 | |a Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine |
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| 520 | |a Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. | ||
| 650 | 4 | |a Nicotinate dehydrogenase (NaDH) | |
| 650 | 4 | |a Nicotinic acid | |
| 650 | 4 | |a 6-Hydroxynicotinic acid | |
| 650 | 4 | |a 3-Cyanopyridine | |
| 650 | 4 | |a 3-Cyano-6-hydrxoypyridine | |
| 700 | 1 | |a Chen, Ting |4 aut | |
| 700 | 1 | |a Ma, Pengjuan |4 aut | |
| 700 | 1 | |a Shang, Guangdong |4 aut | |
| 700 | 1 | |a Dai, Yijun |4 aut | |
| 700 | 1 | |a Yuan, Sheng |4 aut | |
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10.1007/s10532-010-9327-2 doi (DE-627)OLC2050401442 (DE-He213)s10532-010-9327-2-p DE-627 ger DE-627 rakwb eng 570 610 VZ 12 ssgn Yang, Yao verfasserin aut Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media B.V. 2010 Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. Nicotinate dehydrogenase (NaDH) Nicotinic acid 6-Hydroxynicotinic acid 3-Cyanopyridine 3-Cyano-6-hydrxoypyridine Chen, Ting aut Ma, Pengjuan aut Shang, Guangdong aut Dai, Yijun aut Yuan, Sheng aut Enthalten in Biodegradation Springer Netherlands, 1990 21(2010), 4 vom: 02. Feb., Seite 593-602 (DE-627)130929395 (DE-600)1056014-2 (DE-576)026322242 0923-9820 nnns volume:21 year:2010 number:4 day:02 month:02 pages:593-602 https://doi.org/10.1007/s10532-010-9327-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-UMW SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2016 GBV_ILN_4082 GBV_ILN_4219 AR 21 2010 4 02 02 593-602 |
| spelling |
10.1007/s10532-010-9327-2 doi (DE-627)OLC2050401442 (DE-He213)s10532-010-9327-2-p DE-627 ger DE-627 rakwb eng 570 610 VZ 12 ssgn Yang, Yao verfasserin aut Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media B.V. 2010 Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. Nicotinate dehydrogenase (NaDH) Nicotinic acid 6-Hydroxynicotinic acid 3-Cyanopyridine 3-Cyano-6-hydrxoypyridine Chen, Ting aut Ma, Pengjuan aut Shang, Guangdong aut Dai, Yijun aut Yuan, Sheng aut Enthalten in Biodegradation Springer Netherlands, 1990 21(2010), 4 vom: 02. Feb., Seite 593-602 (DE-627)130929395 (DE-600)1056014-2 (DE-576)026322242 0923-9820 nnns volume:21 year:2010 number:4 day:02 month:02 pages:593-602 https://doi.org/10.1007/s10532-010-9327-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-UMW SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2016 GBV_ILN_4082 GBV_ILN_4219 AR 21 2010 4 02 02 593-602 |
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10.1007/s10532-010-9327-2 doi (DE-627)OLC2050401442 (DE-He213)s10532-010-9327-2-p DE-627 ger DE-627 rakwb eng 570 610 VZ 12 ssgn Yang, Yao verfasserin aut Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media B.V. 2010 Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. Nicotinate dehydrogenase (NaDH) Nicotinic acid 6-Hydroxynicotinic acid 3-Cyanopyridine 3-Cyano-6-hydrxoypyridine Chen, Ting aut Ma, Pengjuan aut Shang, Guangdong aut Dai, Yijun aut Yuan, Sheng aut Enthalten in Biodegradation Springer Netherlands, 1990 21(2010), 4 vom: 02. Feb., Seite 593-602 (DE-627)130929395 (DE-600)1056014-2 (DE-576)026322242 0923-9820 nnns volume:21 year:2010 number:4 day:02 month:02 pages:593-602 https://doi.org/10.1007/s10532-010-9327-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-UMW SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2016 GBV_ILN_4082 GBV_ILN_4219 AR 21 2010 4 02 02 593-602 |
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10.1007/s10532-010-9327-2 doi (DE-627)OLC2050401442 (DE-He213)s10532-010-9327-2-p DE-627 ger DE-627 rakwb eng 570 610 VZ 12 ssgn Yang, Yao verfasserin aut Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media B.V. 2010 Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. Nicotinate dehydrogenase (NaDH) Nicotinic acid 6-Hydroxynicotinic acid 3-Cyanopyridine 3-Cyano-6-hydrxoypyridine Chen, Ting aut Ma, Pengjuan aut Shang, Guangdong aut Dai, Yijun aut Yuan, Sheng aut Enthalten in Biodegradation Springer Netherlands, 1990 21(2010), 4 vom: 02. Feb., Seite 593-602 (DE-627)130929395 (DE-600)1056014-2 (DE-576)026322242 0923-9820 nnns volume:21 year:2010 number:4 day:02 month:02 pages:593-602 https://doi.org/10.1007/s10532-010-9327-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-UMW SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2016 GBV_ILN_4082 GBV_ILN_4219 AR 21 2010 4 02 02 593-602 |
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10.1007/s10532-010-9327-2 doi (DE-627)OLC2050401442 (DE-He213)s10532-010-9327-2-p DE-627 ger DE-627 rakwb eng 570 610 VZ 12 ssgn Yang, Yao verfasserin aut Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media B.V. 2010 Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. Nicotinate dehydrogenase (NaDH) Nicotinic acid 6-Hydroxynicotinic acid 3-Cyanopyridine 3-Cyano-6-hydrxoypyridine Chen, Ting aut Ma, Pengjuan aut Shang, Guangdong aut Dai, Yijun aut Yuan, Sheng aut Enthalten in Biodegradation Springer Netherlands, 1990 21(2010), 4 vom: 02. Feb., Seite 593-602 (DE-627)130929395 (DE-600)1056014-2 (DE-576)026322242 0923-9820 nnns volume:21 year:2010 number:4 day:02 month:02 pages:593-602 https://doi.org/10.1007/s10532-010-9327-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-UMW SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2016 GBV_ILN_4082 GBV_ILN_4219 AR 21 2010 4 02 02 593-602 |
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Enthalten in Biodegradation 21(2010), 4 vom: 02. Feb., Seite 593-602 volume:21 year:2010 number:4 day:02 month:02 pages:593-602 |
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Enthalten in Biodegradation 21(2010), 4 vom: 02. Feb., Seite 593-602 volume:21 year:2010 number:4 day:02 month:02 pages:593-602 |
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Nicotinate dehydrogenase (NaDH) Nicotinic acid 6-Hydroxynicotinic acid 3-Cyanopyridine 3-Cyano-6-hydrxoypyridine |
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The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. 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Yang, Yao |
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Yang, Yao ddc 570 ssgn 12 misc Nicotinate dehydrogenase (NaDH) misc Nicotinic acid misc 6-Hydroxynicotinic acid misc 3-Cyanopyridine misc 3-Cyano-6-hydrxoypyridine Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine |
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570 610 VZ 12 ssgn Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine Nicotinate dehydrogenase (NaDH) Nicotinic acid 6-Hydroxynicotinic acid 3-Cyanopyridine 3-Cyano-6-hydrxoypyridine |
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ddc 570 ssgn 12 misc Nicotinate dehydrogenase (NaDH) misc Nicotinic acid misc 6-Hydroxynicotinic acid misc 3-Cyanopyridine misc 3-Cyano-6-hydrxoypyridine |
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ddc 570 ssgn 12 misc Nicotinate dehydrogenase (NaDH) misc Nicotinic acid misc 6-Hydroxynicotinic acid misc 3-Cyanopyridine misc 3-Cyano-6-hydrxoypyridine |
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Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine |
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Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine |
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Yang, Yao Chen, Ting Ma, Pengjuan Shang, Guangdong Dai, Yijun Yuan, Sheng |
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cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from comamonas testosteroni ja1 that can hydroxylate 3-cyanopyridine |
| title_auth |
Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine |
| abstract |
Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. © Springer Science+Business Media B.V. 2010 |
| abstractGer |
Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. © Springer Science+Business Media B.V. 2010 |
| abstract_unstemmed |
Abstract A nicotinate dehydrogenase (NaDH) gene cluster was cloned from Comamonas testosteroni JA1. The enzyme, termed $ NaDH_{JA1} $, is composed of 21, 82, and 46 kDa subunits, respectivley containing [2Fe2S], Mo(V) and cytochrome c domains. The recombinant $ NaDH_{JA1} $ can catalyze the hydroxylation of nicotinate and 3-cyanopyridine. $ NaDH_{JA1} $ protein exhibits 52.8% identity to the amino acid sequence of $ NaDH_{KT2440} $ from P. putida KT2440. Sequence alignment analysis showed that the [2Fe2S] domain in $ NaDH_{JA1} $ had a type II [2Fe-2S] motif and a type I [2Fe-2S] motif, while the same domain in $ NaDH_{KT2440} $ had only a type II [2Fe-2S] motif. $ NaDH_{KT2440} $ had an additional hypoxanthine dehydrogenase motif that $ NaDH_{JA1} $ does not have. When the small unit of $ NaDH_{JA1} $ was replaced by the small subunit from $ NaDH_{KT2440} $, the hybrid protein was able to catalyze the hydroxylation of nicotinate, but lost the ability to catalyze hydroxylation of 3-cyanopyridine. In contrast, after replacement of the small subunit of $ NaDH_{KT2440} $ with the small subunit from $ NaDH_{JA1} $, the resulting hybrid protein $ NaDH_{JAS+KTL} $ acquired the ability to hydroxylate 3-cyanopyridine. The subunits swap results indicate the [2Fe2S] motif determines the 3-cyanopyridine hydroxylation ability, which is evidently different from the previous belief that the Mo motif determines substrate specificity. © Springer Science+Business Media B.V. 2010 |
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Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine |
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