ArticleThe Journal of biological chemistry2014
Escherichia coli D-malate dehydrogenase, a generalist enzyme active in the leucine biosynthesis pathway.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
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- Discovery, Herbicidal Activity and Biosynthesis of a Novel Natural Tetramic Acid from Alternaria Species.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Substrate Promiscuity ofJACS Au · 2024Article
- Tartrate Dehydrogenase in Bacillus Species: Deciphering Unique Catalytic Diversity Through Kinetic, Structural and Molecular Docking Analysis.The protein journal · 2024Article
- Biochemical and structural elucidation of the L-carnitine degradation pathway of the human pathogenFrontiers in microbiology · 2024Article
- Development of a Genome-Scale Metabolic Model and Phenome Analysis of the ProbioticInternational journal of molecular sciences · 2021Article
- Uncovering a superfamily of nickel-dependent hydroxyacid racemases and epimerases.Scientific reports · 2020Article
- How enzyme promiscuity and horizontal gene transfer contribute to metabolic innovation.The FEBS journal · 2020Review
- d-2-Hydroxyglutarate dehydrogenase plays a dual role in l-serine biosynthesis and d-malate utilization in the bacteriumThe Journal of biological chemistry · 2018Article
- Evolutionary repurposing of a sulfatase: A new Michaelis complex leads to efficient transition state charge offset.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Characterization of two β-decarboxylating dehydrogenases from Sulfolobus acidocaldarius.Extremophiles : life under extreme conditions · 2016Article
- Bi-allelic CLPB mutations cause cataract, renal cysts, nephrocalcinosis and 3-methylglutaconic aciduria, a novel disorder of mitochondrial protein disaggregation.Journal of inherited metabolic disease · 2015Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The enzymes of the β-decarboxylating dehydrogenase superfamily catalyze the oxidative decarboxylation of D-malate-based substrates with various specificities. Here, we show that, in addition to its natural function affording bacterial growth on D-malate as a carbon source, the D-malate dehydrogenase of Escherichia coli (EcDmlA) naturally expressed from its chromosomal gene is capable of complementing leucine auxotrophy in a leuB(-) strain lacking the paralogous isopropylmalate dehydrogenase enzyme. To our knowledge, this is the first example of an enzyme that contributes with a physiologically relevant level of activity to two distinct pathways of the core metabolism while expressed from its chromosomal locus. EcDmlA features relatively high catalytic activity on at least three different substrates (L(+)-tartrate, D-malate, and 3-isopropylmalate). Because of these properties both in vivo and in vitro, EcDmlA may be defined as a generalist enzyme. Phylogenetic analysis highlights an ancient origin of DmlA, indicating that the enzyme has maintained its generalist character throughout evolution. We discuss the implication of these findings for protein evolution.
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