Cited by 105Bacterial Genetics and BiotechnologyMicrobial metabolism and enzyme functionEnzyme Structure and Function

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Biochemical and genetic characterization of the membrane‐associated malate dehydrogenase (acceptor) from Corynebacterium glutamicum

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Molenaar, Douwe, van der Rest, Michel E., Petrović, Sonja·1998·European Journal of Biochemistry

DOI 10.1046/j.1432-1327.1998.2540395.x

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Abstract

In addition to a cytoplasmic, NAD‐dependent malate dehydrogenase ( EC1.1.1.37), Corynebacterium glutamicum possesses a highly active membrane‐associated malate dehydrogenase (acceptor) ( EC1.1.99.16). This enzyme also takes part in the citric acid cycle. It oxidizes L‐malate to oxaloacetate and donates electrons to ubiquinone‐1 and other artificial acceptors or, via the electron transfer chain, to oxygen. NAD is not an acceptor and the natural direct acceptor for the enzyme is most likely a quinone. The enzyme is therefore called malate :quinone oxidoreductase, abbreviated to Mqo. Mqo is a peripheral membrane protein and can be released from the membrane by addition of chelators. The solubilized form was partially purified and characterized biochemically. FAD is probably a tightly but non‐covalently bound prosthetic group, and the enzyme is activated by lipids. A C. glutamicum mutant completely lacking Mqo activity was isolated. It grows poorly on several substrates tested. The mutant possesses normal levels of cytoplasmic NAD‐dependent malate dehydrogenase. A plasmid containing the gene from C. glutamicum coding for Mqo was isolated by complementation of the Mqo‐negative phenotype. It leads to overexpression of Mqo activity in the mutant. The nucleotide sequence of the mqo gene was determined and is the first sequence known for this enzyme. The derived protein sequence is similar to hypothetical proteins from Escherichia coli, Klebsiella pneumoniae, and Mycobacterium tuberculosis.

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Authors: Molenaar, D., van der Rest, M. E., & Petrović, S.
Affiliations: Heinrich Heine University Düsseldorf (DE)
Venue: European Journal of Biochemistry
Publisher: Wiley
Published: 1998-06
Volume: 254
Issue: 2
Pages: 395-403
ISSN: 0014-2956 (ISSN-L)
1432-1033
DOI: 10.1046/j.1432-1327.1998.2540395.x
OpenAlex: W2042795207
Cited by: 105
References: 5
Citations by year: 2026: 2 · 2025: 4 · 2024: 1 · 2023: 3 · 2022: 3 · 2021: 5 · 2020: 2 · 2019: 4 · 2018: 2 · 2017: 1 · 2016: 7 · 2015: 4 · 2014: 7 · 2013: 2 · 2012: 8
FWCI: 1.71
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 1303 d)
Locations: European Journal of Biochemistry (publishedVersion)
PubMed (publishedVersion)
VU Research Portal (submittedVersion)
Data Archiving and Networked Services (DANS) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: malate:quinone oxidoreductase, Corynebacterium glutamicum, TCA cycle, FAD prosthetic group, quinone acceptors, peripheral membrane proteins, gene complementation, NAD-dependent malate dehydrogenase, protein sequence similarity
MeSH terms: Amino Acid Sequence, Base Sequence, Cloning, Molecular, Corynebacterium, Enzyme Activation, Flavin-Adenine Dinucleotide, Genes, Bacterial, Lipids, Malate Dehydrogenase, Malates, Membranes, Molecular Sequence Data, Mutation, Oligodeoxyribonucleotides, Oxaloacetates, Oxidation-Reduction, Solubility, Substrate Specificity, Ubiquinone, Sequence Homology, Amino Acid

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Biochemical and genetic characterization of the membrane‐associated malate dehydrogenase (acceptor) from Corynebacterium glutamicum

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