Cloning and characterization of the bifunctional alcohol/acetaldehyde dehydrogenase gene (adhE) in Leuconostoc mesenteroides isolated from kimchi View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2005-04

AUTHORS

Ok Kyung Koo, Do-Won Jeong, Jung Min Lee, Min Jung Kim, Jong-Hoon Lee, Hae Choon Chang, Jeong Hwan Kim, & Hyong Joo Lee

ABSTRACT

A bifunctional alcohol/acetaldehyde dehydrogenase (AdhE) gene (adhE) was cloned from Leuconostoc mesenteroides C7 (LMC7), which is the dominant lactic acid bacterium produced during heterofermentation of kimchi. The nucleotide sequence of the DNA fragment containing putative adhE, which is 2685 bp long and encodes an 886 amino acid polypeptide, exhibits 99% homology with Leu. mesenteroides sp. cremoris. The deduced AdhE comprises two conserved domains: alcohol dehydrogenase (Adh) and acetaldehyde dehydrogenase (Aldh). Moreover, two NAD-binding sites were observed, based on the presence of the GXGXXG motif. A pADHE containing the adhE gene expressed AdhE at the translational level in Escherichia coli BL21, which was at a higher level than in E. coli DH5alpha and E. coli JM109. The AdhE of LMC7 showed Adh and Aldh activities that, when expressed in E. coli. BL21, were 7.5 and 5.7 U mg(-1) , respectively. More... »

PAGES

505-510

Journal

TITLE

Biotechnology Letters

ISSUE

7

VOLUME

27

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s10529-005-2541-z

    DOI

    http://dx.doi.org/10.1007/s10529-005-2541-z

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1042475206

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/15928858


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    31 schema:description A bifunctional alcohol/acetaldehyde dehydrogenase (AdhE) gene (adhE) was cloned from Leuconostoc mesenteroides C7 (LMC7), which is the dominant lactic acid bacterium produced during heterofermentation of kimchi. The nucleotide sequence of the DNA fragment containing putative adhE, which is 2685 bp long and encodes an 886 amino acid polypeptide, exhibits 99% homology with Leu. mesenteroides sp. cremoris. The deduced AdhE comprises two conserved domains: alcohol dehydrogenase (Adh) and acetaldehyde dehydrogenase (Aldh). Moreover, two NAD-binding sites were observed, based on the presence of the GXGXXG motif. A pADHE containing the adhE gene expressed AdhE at the translational level in Escherichia coli BL21, which was at a higher level than in E. coli DH5alpha and E. coli JM109. The AdhE of LMC7 showed Adh and Aldh activities that, when expressed in E. coli. BL21, were 7.5 and 5.7 U mg(-1) , respectively.
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