Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida.
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Human GLO1 catalyzes conversion of methylglyoxal and glutathione to S-lactoylglutathione.
"Glyoxalase I (EC 4.4.1.5) catalyzes the transformation of methylglyoxal and glutathione to S-lactoylglutathione."
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Expression of human GLO1 confers methylglyoxal resistance and high glyoxalase activity in bacteria.
"The Escherichia coli cells carrying the expression vector of this cDNA acquired methylglyoxal resistance and the cell lysate showed the high activity of glyoxalase I."
Involvement of an active-site Zn2+ ligand in the catalytic mechanism of human glyoxalase I.
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Active-site zinc ligands are required for human GLO1 catalysis.
"No catalytic activity could be detected with the double mutant Q33E/E172Q"
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The catalytic glutamate directly participates in proton transfer.
"The results suggest that the metal ligand glutamate 172 is directly involved in the catalytic mechanism of the enzyme"
Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue.
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Transition-state-analogue structures support a zinc-coordinated cis-enediolate mechanism.
"The structure of the complex with the enediolate analogue supports an "inner sphere mechanism" in which the GSH-methylglyoxal thiohemiacetal substrate is converted to product via a cis-enediolate intermediate."
Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping.
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Human GLO1 is a zinc-dependent homodimer with active sites at the dimer interface.
"the active site being situated in the dimer interface, with the inhibitor and essential zinc ion interacting with side chains from both subunits"
Posttranslational modification of human glyoxalase 1 indicates redox-dependent regulation.
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GLO1 is a cytosolic component of the methylglyoxal-detoxifying glyoxalase system.
"Glyoxalases (Glo1, E.C. 4.4.1.5, and Glo2, E.C.3.1.2.6) constitute an ubiquitous detoxification system that protects against cellular damage caused by reactive 2-oxo-aldehydes such as methylglyoxal (MGO)."
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Cys139 glutathionylation directly inhibits GLO1 activity.
"In contrast, glutathionylation strongly inhibited Glo1 activity in vitro."
Design and evaluation of azaindole-substituted N-hydroxypyridones as glyoxalase I inhibitors.
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GLO1 inhibitor binding was validated by X-ray crystallography and thermodynamic measurements.
"We validated this inhibitor design by comparing its structure-activity relationship (SAR) with that of corresponding indole derivatives, by analyzing the binding mode with X-ray crystallography and by evaluating its thermodynamic binding parameters."
Glyoxalase I is involved in resistance of human leukemia cells to antitumor agent-induced apoptosis.
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GLO1 overexpression suppresses drug-induced caspase activation and apoptosis in human cells.
"When overexpressed in human Jurkat cells, GLO1 inhibited etoposide- and adriamycin-induced caspase activation and apoptosis"
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GLO1 inhibition resensitizes a resistant leukemia line to etoposide-induced apoptosis.
"cotreatment with S-p-bromobenzylglutathione cyclopentyl diester (BBGC), a cell-permeable inhibitor of GLO1, enhanced etoposide-induced apoptosis in resistant UK711 cells"
Selective activation of apoptosis program by S-p-bromobenzylglutathione cyclopentyl diester in glyoxalase I-overexpressing human lung cancer cells.
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GLO1 inhibition preferentially induces apoptosis in tumor cells with high GLO1 activity.
"Human lung cancer NCI-H522 and DMS114 cells, expressing higher GLO1 activity, underwent apoptosis when treated with BBGC, whereas A549 cells, expressing lower activity, did not."
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The study describes GLO1 as a methylglyoxal-detoxifying enzyme.
"Glyoxalase I (GLO1) is an enzyme that plays a role in the detoxification of methylglyoxal, a side-product of glycolysis."
Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis.
Large-scale proteomics and phosphoproteomics of urinary exosomes.
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The study identified proteins by large-scale LC-MS/MS profiling of human urinary exosomes.
"Overall, the analysis identified 1132 proteins unambiguously"
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
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The study identified approximately 900 proteins in EPS-urine exosome preparations.
"In pooled EPS-urine exosome samples, ~900 proteins were detected."
A reference map of the human binary protein interactome.
Tumour necrosis factor induces phosphorylation primarily of the nitric-oxide-responsive form of glyoxalase I.
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TNF induces phosphorylation of GLO1 in a cell-death model.
"TNF (tumour necrosis factor) induces phosphorylation of GLO1 (glyoxalase I), which is required for cell death in L929 cells."
Phosphorylation on Thr-106 and NO-modification of glyoxalase I suppress the TNF-induced transcriptional activity of NF-kappaB.
GLO1 dimer:2xZn2+ transforms MGXL and GSH to (R)-S-LGSH
UniProtKB record for human GLO1 (Q04760)
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GLO1 is a reviewed 184-amino-acid human protein.
"Reviewed; 184 AA."
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GLO1 is a homodimer.
"CC -!- SUBUNIT: Homodimer."
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Isoform 2 lacks residues 105-119 of the canonical protein.
"FT VAR_SEQ 105..119"
Manual literature and annotation review notes for human GLO1
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All 27 GOA annotation rows were manually adjudicated.
"## Existing annotation decisions"
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The review separates the catalytic core from context-specific phenotypes and discovery localizations.
"## Context-specific phenotypes"
Manual literature synthesis for human GLO1 (Q04760)
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GLO1 is a cytosolic zinc-dependent methylglyoxal-detoxification enzyme.
"The best-supported core picture is therefore a cytosolic, zinc-dependent methylglyoxal-detoxification enzyme."