The DOI matches its Crossref record; 3 of the 5 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
(1975) · Journal of AOAC INTERNATIONAL · doi:10.1093/jaoac/58.5.1085 · Cited by 20,078
(1985) · International Journal of Biochemistry · doi:10.1016/0020-711x(85)90098-9 · Cited by 3,494
The Enzymes of Biological Membranes
Martonosi, A. N. (1985) · Springer eBooks · doi:10.1007/978-1-4613-2355-6 · Cited by 1,356
Research works printed but not linked: 4
- Abe, S., Takayama, K. & Kinoshita, S. (1967) J. Gen. Appl. Micro- of both a NAD-dependent malate dehydrogenase and a Mqo is biol. 13, 279Ϫ301. unclear. However, it should be borne in mind that the Gibbs 20. Vrljic ´, M., Sahm, H. & Eggeling, L. (1996) Mol. Microbiol. 22, standard free energies for both reactions differ dramatically. 815Ϫ826. Whereas the NAD-dependent reaction has a highly unfavourable 21. Menkel, E., Thierbach, G., Eggeling, L. & Sahm, H. (1989) Appl. Environ. Microbiol. 55, 684Ϫ688. ∆G°′ for oxaloacetate formation equal to ϩ28.6 kJ/mol, the 14321033, 1998, 2, Downloaded from https://febs.onlinelibrary.wiley.com/doi/10.1046/j.1432-1327.1998.2540395.x, Wiley Online Library on [23/06/2026]. See the Terms and Conditions (https://onlinelibrary.wiley.com/terms-and-conditions) on Wiley Online Library for rules of use; OA articles are governed by the applicable Creative Commons License
- Wendisch, V. F. (1997) Thesis, Heinrich-Heine-Universität, Düssel- 31.
- Sanger, F., Nicklen, S. & Coulson, A. R. (1977) Proc. Natl Acad. Sci. USA 74, 5463Ϫ5467. 187, 101Ϫ107.
- Davis, K. A. & Hatefi, Y. (1972) Arch. Biochem. Biophys. 149, 39. Thauer, R. K., Jungermann, K. & Decker, K. (1977) Bacteriol. Rev. 41, 100Ϫ180. 505Ϫ512. 14321033, 1998, 2, Downloaded from https://febs.onlinelibrary.wiley.com/doi/10.1046/j.1432-1327.1998.2540395.x, Wiley Online Library on [23/06/2026]. See the Terms and Conditions (https://onlinelibrary.wiley.com/terms-and-conditions) on Wiley Online Library for rules of use; OA articles are governed by the applicable Creative Commons License
Cited by
Sorted by citations
Kalinowski, J., Bathe, B., Bartels, D., Bischoff, N., Bott, M. H., Burkovski, A., Dusch, N., Eggeling, L., Eikmanns, B. J., Gaigalat, L., et al. (2003) · Journal of Biotechnology · doi:10.1016/s0168-1656(03)00154-8 · Cited by 900
van der Rest, M. E., Lange, C. M., & Douwe Molenaar, B. (1999) · Applied Microbiology and Biotechnology · doi:10.1007/s002530051557 · Cited by 467
Lenaz, G., & Genova, M. L. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2704 · Cited by 284
Energetics of Respiration and Oxidative Phosphorylation in Mycobacteria
Cook, G. M., Hards, K., Vilchèze, C., Hartman, T., & Berney, M. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.mgm2-0015-2013 · Cited by 212
“The membrane-associated malate quinone oxidore-ductase (MQO) oxidizes malate to oxaloacetate and transfers the reducing equivalents to menaquinone (59, 60) (Fig.”
BackgroundMethodAcetate metabolism and its regulation in Corynebacterium glutamicum
Gerstmeir, R., Wendisch, V. F., Schnicke, S., Ruan, H., Farwick, M., Reinscheid, D. J., & Eikmanns, B. J. (2003) · Journal of Biotechnology · doi:10.1016/s0168-1656(03)00167-6 · Cited by 216
Metadata
- 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
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
