ArticleThe Journal of biological chemistry2011
Structural variation in bacterial glyoxalase I enzymes: investigation of the metalloenzyme glyoxalase I from Clostridium acetobutylicum.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 43 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
- Tracing the intraspecies expansion of glyoxalase genes and their expanding roles across the genus Oryza.Functional & integrative genomics · 2024Article
- Genome-Wide Analysis and Expression Profiling of Glyoxalase Gene Families Under Abiotic Stresses in Cucumber (International journal of molecular sciences · 2024Article
- Viridiplantae-specific GLXI and GLXII isoforms co-evolved and detoxify glucosone in planta.Plant physiology · 2023Article
- GLO1 Contributes to the Drug Resistance ofInfection and drug resistance · 2022Article
- Characterization of a highly xylose tolerant β-xylosidase isolated from high temperature horse manure compost.BMC biotechnology · 2021Article
- From methylglyoxal to pyruvate: a genome-wide study for the identification of glyoxalases and D-lactate dehydrogenases in Sorghum bicolor.BMC genomics · 2020Article
- Functional Changes of the Community of Microbes With Ni-Dependent Enzyme Genes Accompany Adaptation of the Ruminal Microbiome to Urea-Supplemented Diets.Frontiers in microbiology · 2020Article
- Genome-wide analysis of glyoxalase-like gene families in grape (Vitis vinifera L.) and their expression profiling in response to downy mildew infection.BMC genomics · 2019Article
- Characteristic Variations and Similarities in Biochemical, Molecular, and Functional Properties of Glyoxalases across Prokaryotes and Eukaryotes.International journal of molecular sciences · 2017Review
- Genome-Wide Identification of Glyoxalase Genes inFrontiers in plant science · 2017Article
- Genome-wide analysis and expression profiling of glyoxalase gene families in soybean (Glycine max) indicate their development and abiotic stress specific response.BMC plant biology · 2016Article
- Article
- Structure of the novel monomeric glyoxalase I from Zea mays.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Metals in cyanobacteria: analysis of the copper, nickel, cobalt and arsenic homeostasis mechanisms.Life (Basel, Switzerland) · 2014Review
- Metal preferences and metallation.The Journal of biological chemistry · 2014Review
- Nonredox nickel enzymes.Chemical reviews · 2014Review
- Synthesis of azide derivative and discovery of glyoxalase pathway inhibitor against pathogenic bacteria.Bioorganic & medicinal chemistry letters · 2013Article
- Episodes of horizontal gene-transfer and gene-fusion led to co-existence of different metal-ion specific glyoxalase I.Scientific reports · 2013Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The glyoxalase system catalyzes the conversion of toxic, metabolically produced α-ketoaldehydes, such as methylglyoxal, into their corresponding nontoxic 2-hydroxycarboxylic acids, leading to detoxification of these cellular metabolites. Previous studies on the first enzyme in the glyoxalase system, glyoxalase I (GlxI), from yeast, protozoa, animals, humans, plants, and Gram-negative bacteria, have suggested two metal activation classes, Zn(2+) and non-Zn(2+) activation. Here, we report a biochemical and structural investigation of the GlxI from Clostridium acetobutylicum, which is the first GlxI enzyme from Gram-positive bacteria that has been fully characterized as to its three-dimensional structure and its detailed metal specificity. It is a Ni(2+)/Co(2+)-activated enzyme, in which the active site geometry forms an octahedral coordination with one metal atom, two water molecules, and four metal-binding ligands, although its inactive Zn(2+)-bound form possesses a trigonal bipyramidal geometry with only one water molecule liganded to the metal center. This enzyme also possesses a unique dimeric molecular structure. Unlike other small homodimeric GlxI where two active sites are located at the dimeric interface, the C. acetobutylicum dimeric GlxI enzyme also forms two active sites but each within single subunits. Interestingly, even though this enzyme possesses a different dimeric structure from previously studied GlxI, its metal activation characteristics are consistent with properties of other GlxI. These findings indicate that metal activation profiles in this class of enzyme hold true across diverse quaternary structure arrangements.
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