| Standard Name | GLO1 |
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| 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 |
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| Note: this feature is encoded on the Crick strand. | |
| View Computational GO annotations for GLO1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| High-throughput |
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| Classical genetics | |
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| null |
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| Large-scale survey | |
| null | |
| Resources |
| 12 total interaction(s) for 10 unique genes/features. | |
| Physical Interactions |
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| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
| Note: this feature is encoded on the Crick strand. | |||||||||||||
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| Last Update | Coordinates: 1996-07-31 | Sequence: 1996-07-31 | ||||||||||||
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| S288C only | |
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| 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 |
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| Primary SGDID | S000004463 |
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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 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,
| 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 |





