Literature DB >> 12435492

Microbial aldo-keto reductases.

Elizabeth M Ellis1.   

Abstract

The aldo-keto reductases (AKR) are a superfamily of enzymes with diverse functions in the reduction of aldehydes and ketones. AKR enzymes are found in a wide range of microorganisms, and many open reading frames encoding related putative enzymes have been identified through genome sequencing projects. Established microbial members of the superfamily include the xylose reductases, 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases. The AKR enzymes share a common (alpha/beta)(8) structure, and conserved catalytic mechanism, although there is considerable variation in the substrate-binding pocket. The physiological function of many of these enzymes is unknown, but a variety of methods including gene disruptions, heterologous expression systems and expression profiling are being employed to deduce the roles of these enzymes in cell metabolism. Several microbial AKR are already being exploited in biotransformation reactions and there is potential for other novel members of this important superfamily to be identified, studied and utilized in this way.

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Year:  2002        PMID: 12435492     DOI: 10.1111/j.1574-6968.2002.tb11425.x

Source DB:  PubMed          Journal:  FEMS Microbiol Lett        ISSN: 0378-1097            Impact factor:   2.742


  20 in total

1.  Production and characterization of a thermostable alcohol dehydrogenase that belongs to the aldo-keto reductase superfamily.

Authors:  Ronnie Machielsen; Agustinus R Uria; Servé W M Kengen; John van der Oost
Journal:  Appl Environ Microbiol       Date:  2006-01       Impact factor: 4.792

2.  Selective enzymatic reduction of aldehydes.

Authors:  Guido Sello; Fulvia Orsini; Silvana Bernasconi; Patrizia Di Gennaro
Journal:  Molecules       Date:  2006-05-12       Impact factor: 4.411

Review 3.  The aldo-keto reductase superfamily and its role in drug metabolism and detoxification.

Authors:  Oleg A Barski; Srinivas M Tipparaju; Aruni Bhatnagar
Journal:  Drug Metab Rev       Date:  2008       Impact factor: 4.518

4.  Investigation of the role of a conserved glycine motif in the Saccharomyces cerevisiae xylose reductase.

Authors:  Byron C H Chu; Hung Lee
Journal:  Curr Microbiol       Date:  2006-06-26       Impact factor: 2.188

5.  Crystallographic analysis of a novel aldo-keto reductase from Thermotoga maritima in complex with NADP⁺.

Authors:  Hai Hou; Ruiying Li; Xiaoyan Wang; Zhen Yuan; Xuemeng Liu; Zhenmin Chen; Xiaoling Xu
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2015-06-27       Impact factor: 1.056

6.  Novel Aldo-Keto Reductases for the Biocatalytic Conversion of 3-Hydroxybutanal to 1,3-Butanediol: Structural and Biochemical Studies.

Authors:  Taeho Kim; Robert Flick; Joseph Brunzelle; Alex Singer; Elena Evdokimova; Greg Brown; Jeong Chan Joo; George A Minasov; Wayne F Anderson; Radhakrishnan Mahadevan; Alexei Savchenko; Alexander F Yakunin
Journal:  Appl Environ Microbiol       Date:  2017-03-17       Impact factor: 4.792

7.  Probing the substrate binding site of Candida tenuis xylose reductase (AKR2B5) with site-directed mutagenesis.

Authors:  Regina Kratzer; Stefan Leitgeb; David K Wilson; Bernd Nidetzky
Journal:  Biochem J       Date:  2006-01-01       Impact factor: 3.857

8.  Cloning of a novel aldo-keto reductase gene from Klebsiella sp. strain F51-1-2 and its functional expression in Escherichia coli.

Authors:  Hong Jiang; Chao Yang; Hong Qu; Zheng Liu; Q S Fu; Chuanling Qiao
Journal:  Appl Environ Microbiol       Date:  2007-06-15       Impact factor: 4.792

9.  Conversion of methylglyoxal to acetol by Escherichia coli aldo-keto reductases.

Authors:  Junsang Ko; Insook Kim; Seokho Yoo; Bumchan Min; Kyungmin Kim; Chankyu Park
Journal:  J Bacteriol       Date:  2005-08       Impact factor: 3.490

10.  Thermostable alcohol dehydrogenase from Thermococcus kodakarensis KOD1 for enantioselective bioconversion of aromatic secondary alcohols.

Authors:  Xi Wu; Chong Zhang; Izumi Orita; Tadayuki Imanaka; Toshiaki Fukui; Xin-Hui Xing
Journal:  Appl Environ Microbiol       Date:  2013-01-25       Impact factor: 4.792

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