GLO1/YML004C Summary Help

Standard Name GLO1 1
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 1
Chromosomal Location
ChrXIII:262685 to 261705 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All GLO1 GO evidence and references
  View Computational GO annotations for GLO1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Regulators 5 genes
Classical genetics
Large-scale survey
13 total interaction(s) for 11 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 3
  • Affinity Capture-RNA: 2
  • Biochemical Activity: 1

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 2
  • Phenotypic Enhancement: 1
  • Positive Genetic: 3

Expression Summary
Length (a.a.) 326
Molecular Weight (Da) 37,209
Isoelectric Point (pI) 6.83
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXIII:262685 to 261705 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..981 262685..261705 1996-07-31 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004463

GLO1 is a non-essential gene that encodes glyoxalase I (EC, which is involved in methylglyoxal catabolism (1). 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 (1). 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 (2).

Deletion of GLO1 results in hypersensitivity to methylglyoxal (1). 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: 2012-01-03 Contact SGD

References cited on this page View Complete Literature Guide for GLO1
1) Inoue Y and Kimura A  (1996) Identification of the structural gene for glyoxalase I from Saccharomyces cerevisiae. J Biol Chem 271(42):25958-65
2) 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
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 Antonio Prieto J  (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