Heterologous expression and enzymatic identification of two novel soluble pyridine nucleotide transhydrogenases from Acidobacteria bacterium KBS 146 and Nocardia jiangxiensis

Soluble pyridine nucleotide transhydrogenase (STH), catalyzes a reversible hydrogen transfer between NADH and NADPH, is widely utilized in cofactor engineering. In the present study, we expanded the distribution range of STH to more unreported bacteria. Meanwhile, STH was mainly found in α, γ, δ-pro...

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Autores principales:	Zhengyu Cao, Rui Meng, Peng Wang, Guoping Zhu
Formato:	article
Lenguaje:	EN
Publicado:	Taylor & Francis Group 2021
Materias:	soluble pyridine nucleotide transhydrogenase distribution range enzymatic characterization kinetics acidobacteria bacterium nocardia jiangxiensis Biotechnology TP248.13-248.65
Acceso en línea:	https://doaj.org/article/213876396b424b5bbfe437e6504617f1
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spelling	oai:doaj.org-article:213876396b424b5bbfe437e6504617f12021-11-17T14:21:55ZHeterologous expression and enzymatic identification of two novel soluble pyridine nucleotide transhydrogenases from Acidobacteria bacterium KBS 146 and Nocardia jiangxiensis1310-28181314-353010.1080/13102818.2021.1988708https://doaj.org/article/213876396b424b5bbfe437e6504617f12021-01-01T00:00:00Zhttp://dx.doi.org/10.1080/13102818.2021.1988708https://doaj.org/toc/1310-2818https://doaj.org/toc/1314-3530Soluble pyridine nucleotide transhydrogenase (STH), catalyzes a reversible hydrogen transfer between NADH and NADPH, is widely utilized in cofactor engineering. In the present study, we expanded the distribution range of STH to more unreported bacteria. Meanwhile, STH was mainly found in α, γ, δ-proteobacteria, acidobacteria, actinobacteria and planctomycetes. The enzymological properties of two novel STHs from Acidobacteria bacterium KBS 146 (AbSTH) and Nocardia jiangxiensis (NjSTH) were characterized. The optimum temperature and pH of AbSTH and NjSTH were pH 6.2 and 35 °C, pH 5.7 and 50 °C, respectively. When using thio-NAD+ as a hydrogen accepter, the 1/Km and kcat/Km for NADH of AbSTH were 1.8 and 1.7-fold greater than NADPH, whereas the 1/Km and kcat/Km of NjSTH for NADPH were 2.0 and 2.2-fold greater than NADH. The physiological hydrogen donor substrate of AbSTH and NjSTH may be NADH and NADPH, respectively. AbSTH activity was inhibited by ATP and strongly stimulated by ADP and AMP. These results may provide new insights into the physiological roles and cofactor engineering application of STH. Supplemental data for this article is available online at https://doi.org/10.1080/13102818.2021.1988708 .Zhengyu CaoRui MengPeng WangGuoping ZhuTaylor & Francis Grouparticlesoluble pyridine nucleotide transhydrogenasedistribution rangeenzymatic characterizationkinetics acidobacteria bacterium nocardia jiangxiensis BiotechnologyTP248.13-248.65ENBiotechnology & Biotechnological Equipment, Vol 35, Iss 1, Pp 1452-1460 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	soluble pyridine nucleotide transhydrogenase distribution range enzymatic characterization kinetics acidobacteria bacterium nocardia jiangxiensis Biotechnology TP248.13-248.65
spellingShingle	soluble pyridine nucleotide transhydrogenase distribution range enzymatic characterization kinetics acidobacteria bacterium nocardia jiangxiensis Biotechnology TP248.13-248.65 Zhengyu Cao Rui Meng Peng Wang Guoping Zhu Heterologous expression and enzymatic identification of two novel soluble pyridine nucleotide transhydrogenases from Acidobacteria bacterium KBS 146 and Nocardia jiangxiensis
description	Soluble pyridine nucleotide transhydrogenase (STH), catalyzes a reversible hydrogen transfer between NADH and NADPH, is widely utilized in cofactor engineering. In the present study, we expanded the distribution range of STH to more unreported bacteria. Meanwhile, STH was mainly found in α, γ, δ-proteobacteria, acidobacteria, actinobacteria and planctomycetes. The enzymological properties of two novel STHs from Acidobacteria bacterium KBS 146 (AbSTH) and Nocardia jiangxiensis (NjSTH) were characterized. The optimum temperature and pH of AbSTH and NjSTH were pH 6.2 and 35 °C, pH 5.7 and 50 °C, respectively. When using thio-NAD+ as a hydrogen accepter, the 1/Km and kcat/Km for NADH of AbSTH were 1.8 and 1.7-fold greater than NADPH, whereas the 1/Km and kcat/Km of NjSTH for NADPH were 2.0 and 2.2-fold greater than NADH. The physiological hydrogen donor substrate of AbSTH and NjSTH may be NADH and NADPH, respectively. AbSTH activity was inhibited by ATP and strongly stimulated by ADP and AMP. These results may provide new insights into the physiological roles and cofactor engineering application of STH. Supplemental data for this article is available online at https://doi.org/10.1080/13102818.2021.1988708 .
format	article
author	Zhengyu Cao Rui Meng Peng Wang Guoping Zhu
author_facet	Zhengyu Cao Rui Meng Peng Wang Guoping Zhu
author_sort	Zhengyu Cao
title	Heterologous expression and enzymatic identification of two novel soluble pyridine nucleotide transhydrogenases from Acidobacteria bacterium KBS 146 and Nocardia jiangxiensis
title_short	Heterologous expression and enzymatic identification of two novel soluble pyridine nucleotide transhydrogenases from Acidobacteria bacterium KBS 146 and Nocardia jiangxiensis
title_full	Heterologous expression and enzymatic identification of two novel soluble pyridine nucleotide transhydrogenases from Acidobacteria bacterium KBS 146 and Nocardia jiangxiensis
title_fullStr	Heterologous expression and enzymatic identification of two novel soluble pyridine nucleotide transhydrogenases from Acidobacteria bacterium KBS 146 and Nocardia jiangxiensis
title_full_unstemmed	Heterologous expression and enzymatic identification of two novel soluble pyridine nucleotide transhydrogenases from Acidobacteria bacterium KBS 146 and Nocardia jiangxiensis
title_sort	heterologous expression and enzymatic identification of two novel soluble pyridine nucleotide transhydrogenases from acidobacteria bacterium kbs 146 and nocardia jiangxiensis
publisher	Taylor & Francis Group
publishDate	2021
url	https://doaj.org/article/213876396b424b5bbfe437e6504617f1
work_keys_str_mv	AT zhengyucao heterologousexpressionandenzymaticidentificationoftwonovelsolublepyridinenucleotidetranshydrogenasesfromacidobacteriabacteriumkbs146andnocardiajiangxiensis AT ruimeng heterologousexpressionandenzymaticidentificationoftwonovelsolublepyridinenucleotidetranshydrogenasesfromacidobacteriabacteriumkbs146andnocardiajiangxiensis AT pengwang heterologousexpressionandenzymaticidentificationoftwonovelsolublepyridinenucleotidetranshydrogenasesfromacidobacteriabacteriumkbs146andnocardiajiangxiensis AT guopingzhu heterologousexpressionandenzymaticidentificationoftwonovelsolublepyridinenucleotidetranshydrogenasesfromacidobacteriabacteriumkbs146andnocardiajiangxiensis
_version_	1718425468400566272

Heterologous expression and enzymatic identification of two novel soluble pyridine nucleotide transhydrogenases from Acidobacteria bacterium KBS 146 and Nocardia jiangxiensis

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