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PLoS One. 2012;7(5):e36519. doi: 10.1371/journal.pone.0036519. Epub 2012 May 4.

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

Author information

1
State Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China.

Abstract

BACKGROUND:

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.

METHODOLOGY/PRINCIPAL FINDINGS:

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.

CONCLUSIONS/SIGNIFICANCE:

It is proposed that L-iLDH plays an indispensable function in Pseudomonas L-lactate utilization by catalyzing the conversion of L-lactate into pyruvate.

PMID:
22574176
PMCID:
PMC3344892
DOI:
10.1371/journal.pone.0036519
[Indexed for MEDLINE]
Free PMC Article

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