GLO1/YML004C Summary Help

GLO1 BASIC INFORMATION

Standard Name GLO1
Systematic Name YML004C
Feature Type ORF, Verified
Description Monomeric glyoxalase I, catalyzes the detoxification of methylglyoxal (a by-product of glycolysis) via condensation with glutathione to produce S-D-lactoylglutathione; expression regulated by methylglyoxal levels and osmotic stress (1, 2, 3, 4 and see Summary Paragraph)
Name Description GLyOxalase 2
GO Annotations All GLO1 GO evidence and references
    View Computational GO annotations for GLO1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Pathways
Mutant Phenotype All GLO1 Phenotype details and references
Classical genetics
null
Large-scale survey
null
Interactions GLO1 All interactions details and references
6 total interaction(s) for 4 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 2
  • Affinity Capture-RNA: 1
  • Biochemical Activity: 1
Genetic Interactions
  • Dosage Rescue: 1
  • Phenotypic Enhancement: 1
Sequence Information
ChrXIII:262685 to 261705 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..981 262685..261705 1996-07-31 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000004463

GLO1 RESOURCES

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SGD ORF mapGBrowse
SGD ORF map
 GBrowse
  • Literature
  • Retrieve Sequences
  • Sequence Analysis Tools
  • Protein Info & Structure
  • Localization Resources
  • Interactions
  • Phenotype Resources
  • Maps & Displays
  • Comparison Resources
  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for GLO1

SUMMARY PARAGRAPH for GLO1

GLO1 is a non-essential gene that encodes glyoxalase I (EC 4.4.1.5), which is involved in methylglyoxal catabolism (2). Methylglyoxal is a toxic compound formed as a by-product of glycolysis. One method of methylglyoxal catabolism comprises a glyoxalase system in which methylglyoxal is condensed with glutathione by Glo1p to produce S-D-lactoylglutathione (2). This glutathione thiolester is then hydrolyzed to lactic acid and glutathione by glyoxalase II (Glo2p and Glo4p) (5). GLO1 expression is induced by methylglyoxal (4) and is specifically induced by osmotic stress in a high osmolarity glycerol (Hog1p)-mitogen-activated protein (MAP) kinase-dependent manner (1).

Deletion of GLO1 results in slow growth on glycerol and hypersensitivity to methylglyoxal (2). The Glo1p homolog from Schizosaccharomyces pombe can complement the growth defects of a Saccharomyces cerevisiae glo1 null mutant (6). In S. cerevisiae, glyoxalase I (Glo1p) is a monomer. Mammals, including humans, also contain a glyoxalase I enzyme, but the enzyme in these species is dimeric (7). A single nucleotide polymorphism in human glyoxylase I, GLO1, has been identified as an autism susceptibility factor (8).

Last updated: 2007-05-24

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for GLO1]

1) Inoue Y, et al.  (1998) Expression of the glyoxalase I gene of Saccharomyces cerevisiae is regulated by high osmolarity glycerol mitogen-activated protein kinase pathway in osmotic stress response. J Biol Chem 273(5):2977-83
2) Inoue Y and Kimura A  (1996) Identification of the structural gene for glyoxalase I from Saccharomyces cerevisiae. J Biol Chem 271(42):25958-65
3) Frickel EM, et al.  (2001) Yeast glyoxalase I is a monomeric enzyme with two active sites. J Biol Chem 276(3):1845-9
4) Aguilera J and Prieto JA  (2004) Yeast cells display a regulatory mechanism in response to methylglyoxal. FEMS Yeast Res 4(6):633-41
5) Bito A, et al.  (1997) Identification and phenotypic analysis of two glyoxalase II encoding genes from Saccharomyces cerevisiae, GLO2 and GLO4, and intracellular localization of the corresponding proteins. J Biol Chem 272(34):21509-19
6) Takatsume Y, et al.  (2004) Identification of thermostable glyoxalase I in the fission yeast Schizosaccharomyces pombe. Arch Microbiol 181(5):371-7
7) Ridderstrom M and Mannervik B  (1996) The primary structure of monomeric yeast glyoxalase I indicates a gene duplication resulting in two similar segments homologous with the subunit of dimeric human glyoxalase I. Biochem J 316 ( Pt 3):1005-6
8) Junaid MA, et al.  (2004) Proteomic studies identified a single nucleotide polymorphism in glyoxalase I as autism susceptibility factor. Am J Med Genet A 131(1):11-7