NAD-independent L-lactate dehydrogenase is required for L-lactate utilization in Pseudomonas stutzeri SDM.

PloS One
Chao GaoPing Xu

Abstract

Various Pseudomonas strains can use L-lactate as their sole carbon source for growth. However, the L-lactate-utilizing enzymes in Pseudomonas have never been identified and further studied. An NAD-independent L-lactate dehydrogenase (L-iLDH) was purified from the membrane fraction of Pseudomonas stutzeri SDM. The enzyme catalyzes the oxidation of L-lactate to pyruvate by using FMN as cofactor. After cloning its encoding gene (lldD), L-iLDH was successfully expressed, purified from a recombinant Escherichia coli strain, and characterized. An lldD mutant of P. stutzeri SDM was constructed by gene knockout technology. This mutant was unable to grow on L-lactate, but retained the ability to grow on pyruvate. It is proposed that L-iLDH plays an indispensable function in Pseudomonas L-lactate utilization by catalyzing the conversion of L-lactate into pyruvate.

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Citations

May 3, 2014·Genome Announcements·Yujiao WangPing Xu
Feb 19, 2013·Applied and Environmental Microbiology·Youqiang XuPing Xu
Feb 19, 2013·Bioresource Technology·Chao GaoPing Xu
Aug 14, 2012·Journal of Bacteriology·Chao GaoPing Xu
Apr 12, 2015·Applied and Environmental Microbiology·Binbin ShengPing Xu
Jun 7, 2016·Environmental Microbiology Reports·Yingxin ZhangPing Xu
Jul 27, 2017·Scientific Reports·Sandra BilligFranz-Christoph Bange

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Methods Mentioned

BETA
electrophoresis
PCR

Software Mentioned

CLUSTAL X

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