Dataset Information

Relative catalytic efficiencies and transcript levels of three d- and two l-lactate dehydrogenases for optically pure d-lactate production in Sporolactobacillus inulinus.

ABSTRACT: As the optical purity of the lactate monomer is pivotal for polymerization, the production of optically pure d-lactate is of significant importance. Sporolactobacillus inulinus YBS1-5 is a superior optically pure d-lactate-producing bacterium. However, little is known about the relationship between lactate dehydrogenases in S. inulinus YBS1-5 and the optical purity of d-lactate. Three potential d-lactate dehydrogenase (D-LDH1-3)- and two putative l-lactate dehydrogenase (L-LDH1-2)-encoding genes were cloned from the YBS1-5 strain and expressed in Escherichia coli D-LDH1 exhibited the highest catalytic efficiency toward pyruvate, whereas two L-LDHs showed low catalytic efficiency. Different neutralizers significantly affected the optical purity of d-lactate produced by strain YBS1-5 as well as the transcription levels of ldhDs and ldhLs. The high catalytic efficiency of D-LDH1 and elevated ldhD1 mRNA levels suggest that this enzyme is essential for d-lactate synthesis in S. inulinus YBS1-5. The correlation between the optical purity of d-lactate and transcription levels of ldhL1 in the case of different neutralizers indicate that ldhL1 is a key factor affecting the optical purity of d-lactate in S. inulinus YBS1-5.

SUBMITTER: Wu B

PROVIDER: S-EPMC6528580 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature

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Publications

Relative catalytic efficiencies and transcript levels of three d- and two l-lactate dehydrogenases for optically pure d-lactate production in Sporolactobacillus inulinus.

Wu Bin B Yu Qi Q Zheng Shan S Pedroso Marcelo Monteiro MM Guddat Luke W LW He Bingfang B Schenk Gerhard G

MicrobiologyOpen 20180801 5

As the optical purity of the lactate monomer is pivotal for polymerization, the production of optically pure d-lactate is of significant importance. Sporolactobacillus inulinus YBS1-5 is a superior optically pure d-lactate-producing bacterium. However, little is known about the relationship between lactate dehydrogenases in S. inulinus YBS1-5 and the optical purity of d-lactate. Three potential d-lactate dehydrogenase (D-LDH1-3)- and two putative l-lactate dehydrogenase (L-LDH1-2)-encoding genes ...[more]

PMID: 30066438

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Project description:BACKGROUND: The L-lactate and D-lactate dehydrogenases, which are involved in the reduction of pyruvate to L(-)-lactate and D(+)-lactate, belong to evolutionarily unrelated enzyme families. The genes encoding L-LDH have been used as a model for gene duplication due to the multiple paralogs found in eubacteria, archaebacteria, and eukaryotes. Phylogenetic studies have suggested that several gene duplication events led to the main isozymes of this gene family in chordates, but little is known about the evolution of L-Ldh in invertebrates. While most invertebrates preferentially oxidize L-lactic acid, several species of mollusks, a few arthropods and polychaetes were found to have exclusively D-LDH enzymatic activity. Therefore, it has been suggested that L-LDH and D-LDH are mutually exclusive. However, recent characterization of putative mammalian D-LDH with significant similarity to yeast proteins showing D-LDH activity suggests that at least mammals have the two naturally occurring forms of LDH specific to L- and D-lactate. This study describes the phylogenetic relationships of invertebrate L-LDH and D-LDH with special emphasis on crustaceans, and discusses gene duplication events during the evolution of L-Ldh. RESULTS: Our phylogenetic analyses of L-LDH in vertebrates are consistent with the general view that the main isozymes (LDH-A, LDH-B and LDH-C) evolved through a series of gene duplications after the vertebrates diverged from tunicates. We report several gene duplication events in the crustacean, Daphnia pulex, and the leech, Helobdella robusta. Several amino acid sequences with strong similarity to putative mammalian D-LDH and to yeast DLD1 with D-LDH activity were found in both vertebrates and invertebrates. CONCLUSION: The presence of both L-Ldh and D-Ldh genes in several chordates and invertebrates suggests that the two enzymatic forms are not necessarily mutually exclusive. Although, the evolution of L-Ldh has been punctuated by multiple events of gene duplication in both vertebrates and invertebrates, a shared evolutionary history of this gene in the two groups is apparent. Moreover, the high degree of sequence similarity among D-LDH amino acid sequences suggests that they share a common evolutionary history.

Dataset Information

Relative catalytic efficiencies and transcript levels of three d- and two l-lactate dehydrogenases for optically pure d-lactate production in Sporolactobacillus inulinus.

Publications

Relative catalytic efficiencies and transcript levels of three d- and two l-lactate dehydrogenases for optically pure d-lactate production in Sporolactobacillus inulinus.

Similar Datasets

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