Biochemical and genetic characterization of the membrane‐associated malate dehydrogenase (acceptor) from Corynebacterium glutamicum
Open accessAbstract
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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Membrane-associated malate quinone oxidoreductase oxidizes malate to oxaloacetate and transfers reducing equivalents to menaquinone.
“The membrane-associated malate quinone oxidoreductase (MQO) oxidizes malate to oxaloacetate and transfers the reducing equivalents to menaquinone (MK) (59, 60) (Figure 3).”
From Energetics of Respiration and Oxidative Phosphorylation in Mycobacteria (2014) · cites this paper as [60]
The introductory passage and the L-malate oxidation section state that Mqo oxidizes malate to oxaloacetate and donates electrons at the quinone pool; the latter section demonstrates reduction of ubiquinone-1. The paper does not establish menaquinone specifically as the electron acceptor: it says the natural direct acceptor is most likely a quinone, while menaquinone-4 did not stimulate activity in the reported assay. No page number is available in our copy. (LLM, conf=0.86)
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MACAW: a method for semi-automatic detection of errors in genome-scale metabolic models
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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
- 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
- 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
- Physical Sciences › Materials Science › Materials Chemistry › 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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