ArticleThe Biochemical journal2004
Distinct classes of glyoxalase I: metal specificity of the Yersinia pestis, Pseudomonas aeruginosa and Neisseria meningitidis enzymes.
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 24 papers.
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Who cites it
24 citing papers in PubMed, 75 citations in OpenAlex.
- AtGLYI3 and AtGLYI6 play the major role in nickel stress tolerance in Arabidopsis thaliana.Plant cell reports · 2026Article
- Viridiplantae-specific GLXI and GLXII isoforms co-evolved and detoxify glucosone in planta.Plant physiology · 2023Article
- Antisense-acting riboswitches: A poorly characterized yet important model of transcriptional regulation in prokaryotic organisms.PloS one · 2023Article
- Metal-ion promiscuity of microbial enzyme DapE at its second metal-binding site.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- Bioinformatics of Metalloproteins and Metalloproteomes.Molecules (Basel, Switzerland) · 2020Review
- Ni(II) Interactions in BorealFrontiers in microbiology · 2019Article
- Article
- Characteristic Variations and Similarities in Biochemical, Molecular, and Functional Properties of Glyoxalases across Prokaryotes and Eukaryotes.International journal of molecular sciences · 2017Review
- Composition and Predicted Metabolic Capacity of Upper and Lower Airway Microbiota of Healthy Dogs in Relation to the Fecal Microbiota.PloS one · 2016Article
- Article
- Structure of the novel monomeric glyoxalase I from Zea mays.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Article
- Nonredox nickel enzymes.Chemical reviews · 2014Review
- Episodes of horizontal gene-transfer and gene-fusion led to co-existence of different metal-ion specific glyoxalase I.Scientific reports · 2013Article
- Structural variation in bacterial glyoxalase I enzymes: investigation of the metalloenzyme glyoxalase I from Clostridium acetobutylicum.The Journal of biological chemistry · 2011Article
- Mycobacterium tuberculosis NmtR harbors a nickel sensing site with parallels to Escherichia coli RcnR.Biochemistry · 2011Article
- Comparative genomics of trace element dependence in biology.The Journal of biological chemistry · 2011Review
- Methylglyoxal metabolism in trypanosomes and leishmania.Seminars in cell & developmental biology · 2011Review
- Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of glyoxalase I from Leishmania infantum.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Comparative genomic analyses of nickel, cobalt and vitamin B12 utilization.BMC genomics · 2009Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The metalloisomerase glyoxalase I (GlxI) catalyses the conversion of methylglyoxal-glutathione hemithioacetal and related derivatives into the corresponding thioesters. In contrast with the previously characterized GlxI enzymes of Homo sapiens, Pseudomonas putida and Saccharomyces cerevisiae, we recently determined that Escherichia coli GlxI surprisingly did not display Zn2+-activation, but instead exhibited maximal activity with Ni2+. To investigate whether non-Zn2+ activation defines a distinct, previously undocumented class of GlxI enzymes, or whether the E. coli GlxI is an exception to the previously established Zn2+-activated GlxI, we have cloned and characterized the bacterial GlxI from Yersinia pestis, Pseudomonas aeruginosa and Neisseria meningitidis. The metal-activation profiles for these additional GlxIs firmly establish the existence of a non-Zn2+-dependent grouping within the general category of GlxI enzymes. This second, established class of metal activation was formerly unidentified for this metalloenzyme. Amino acid sequence comparisons indicate a more extended peptide chain in the Zn2+-dependent forms of GlxI (H. sapiens, P. putida and S. cerevisiae), compared with the GlxI enzymes of E. coli, Y. pestis, P. aeruginosa and N. meningitidis. The longer sequence is due in part to the presence of additional regions situated fairly close to the metal ligands in the Zn2+-dependent forms of the lyase. With respect to sequence alignments, these inserts may potentially contribute to defining the metal specificity of GlxI at a structural level.
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