ArticleThe Biochemical journal2004
Investigation of metal binding and activation of Escherichia coli glyoxalase I: kinetic, thermodynamic and mutagenesis studies.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 63 citations in OpenAlex.
- Identification of glyoxalase A in group BInfection and immunity · 2025Article
- Identification of Glyoxalase A in Group BbioRxiv : the preprint server for biology · 2024Article
- Structural insights into the half-of-sites reactivity in homodimeric and homotetrameric metalloenzymes.Current opinion in chemical biology · 2023Review
- The Human Glyoxalase Gene Family in Health and Disease.Chemical research in toxicology · 2022Review
- Machine learning differentiates enzymatic and non-enzymatic metals in proteins.Nature communications · 2021Article
- Arginine glycosylation enhances methylglyoxal detoxification.Scientific reports · 2021Article
- Multiscale Process Modelling in Translational Systems Biology of Leishmania major: A Holistic view.Scientific reports · 2020Article
- Zn2+ dependent glyoxalase I plays the major role in methylglyoxal detoxification and salinity stress tolerance in plants.PloS one · 2020Article
- Dissecting the Physiological Function of Plant Glyoxalase I and Glyoxalase I-Like Proteins.Frontiers in plant science · 2018Article
- Defense against Reactive Carbonyl Species Involves at Least Three Subcellular Compartments Where Individual Components of the System Respond to Cellular Sugar Status.The Plant cell · 2017Article
- Characteristic Variations and Similarities in Biochemical, Molecular, and Functional Properties of Glyoxalases across Prokaryotes and Eukaryotes.International journal of molecular sciences · 2017Review
- Structure of the novel monomeric glyoxalase I from Zea mays.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Article
- Nonredox nickel enzymes.Chemical reviews · 2014Review
- Structural and biochemical characterization of human mitochondrial branched-chain α-ketoacid dehydrogenase phosphatase.The Journal of biological chemistry · 2012Article
- Structural variation in bacterial glyoxalase I enzymes: investigation of the metalloenzyme glyoxalase I from Clostridium acetobutylicum.The Journal of biological chemistry · 2011Article
- Alternative epimerization in C(7)N-aminocyclitol biosynthesis is catalyzed by ValD, a large protein of the vicinal oxygen chelate superfamily.Chemistry & biology · 2009Article
- Biosynthetic gene cluster of cetoniacytone A, an unusual aminocyclitol from the endosymbiotic Bacterium Actinomyces sp. Lu 9419.Chembiochem : a European journal of chemical biology · 2009Article
- Distinct classes of glyoxalase I: metal specificity of the Yersinia pestis, Pseudomonas aeruginosa and Neisseria meningitidis enzymes.The Biochemical journal · 2004Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
GlxI (glyoxalase I) isomerizes the hemithioacetal formed between glutathione and methylglyoxal. Unlike other GlxI enzymes, Escherichia coli GlxI exhibits no activity with Zn(2+) but maximal activation with Ni(2+). To elucidate further the metal site in E. coli GlxI, several approaches were undertaken. Kinetic studies indicate that the catalytic metal ion affects the k (cat) without significantly affecting the K (m) for the substrate. Inductively coupled plasma analysis and isothermal titration calorimetry confirmed one metal ion bound to the enzyme, including Zn(2+), which produces an inactive enzyme. Isothermal titration calorimetry was utilized to determine the relative binding affinity of GlxI for various bivalent metals. Each metal ion examined bound very tightly to GlxI with an association constant ( K (a))>10(7) M(-1), with the exception of Mn(2+) ( K (a) of the order of 10(6) M(-1)). One of the ligands to the catalytic metal, His(5), was altered to glutamine, a side chain found in the Zn(2+)-active Homo sapiens GlxI. The affinity of the mutant protein for all bivalent metals was drastically decreased. However, low levels of activity were now observed for Zn(2+)-bound GlxI. Although this residue has a marked effect on metal binding and activation, it is not the sole factor determining the differential metal activation between the human and E. coli GlxI enzymes.
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