Literature DB >> 20432935

[Kinetic mechanisms of glycerol dehydrogenase and 1,3-propanediol oxidoreductase from Klebsiella pneumoniae].

Hongwen Chen1, Jinfeng Nie, Guo Chen, Baishan Fang.   

Abstract

The kinetic mechanisms of two key enzymes in the biotransformation of glycerol to 1,3-propanediol (1,3-PD) by Klebsiella pneumoniae, glycerol dehydrogenase (GDH) and 1,3-propanediol oxidoreductase (PDOR), was characterized. Kinetics on initial velocity and product inhibition revealed that GDH and PDOR follow an ordered Bi-Bi sequential mechanism. Kinetic models for GDH and PDOR showed that the oxidation reaction catalyzed by GDH was the rate-limiting step in coupled enzymatic reaction when the GDH/PDOR was 1:1, and the NAD+ was the main form of coenzyme in the reaction. Knowledge about the kinetic mechanisms will be helpful to understand how these enzymes is regulated, which will be useful for further enzyme catalysis and metabolic engineering studies.

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Year:  2010        PMID: 20432935

Source DB:  PubMed          Journal:  Sheng Wu Gong Cheng Xue Bao        ISSN: 1000-3061


  3 in total

Review 1.  Key enzymes catalyzing glycerol to 1,3-propanediol.

Authors:  Wei Jiang; Shizhen Wang; Yuanpeng Wang; Baishan Fang
Journal:  Biotechnol Biofuels       Date:  2016-03-10       Impact factor: 6.040

2.  Exploring Lactobacillus reuteri DSM20016 as a biocatalyst for transformation of longer chain 1,2-diols: Limits with microcompartment.

Authors:  Lu Chen; Rajni Hatti-Kaul
Journal:  PLoS One       Date:  2017-09-28       Impact factor: 3.240

3.  Mechanistic study of manganese-substituted glycerol dehydrogenase using a kinetic and thermodynamic analysis.

Authors:  Baishan Fang; Jin Niu; Hong Ren; Yingxia Guo; Shizhen Wang
Journal:  PLoS One       Date:  2014-06-04       Impact factor: 3.240

  3 in total

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