GLO1
From Wikipedia, the free encyclopedia
| Glyoxalase I | |||||||||||||
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Rendering based on 1bh5. |
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| Identifiers | |||||||||||||
| Symbols | GLO1; GLOD1; GLYI | ||||||||||||
| External IDs | OMIM: 138750 MGI: 95742 HomoloGene: 4880 GeneCards: GLO1 Gene | ||||||||||||
| EC number | 4.4.1.5 | ||||||||||||
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| RNA expression pattern | |||||||||||||
| More reference expression data | |||||||||||||
| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 2739 | 109801 | |||||||||||
| Ensembl | ENSG00000124767 | ENSMUSG00000024026 | |||||||||||
| UniProt | Q04760 | Q9CPU0 | |||||||||||
| RefSeq (mRNA) | NM_006708 | XM_992039 | |||||||||||
| RefSeq (protein) | NP_006699 | XP_997133 | |||||||||||
| Location (UCSC) | Chr 6: 38.64 – 38.67 Mb |
Chr 17: 30.73 – 30.75 Mb |
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| PubMed search | [1] | [2] | |||||||||||
Lactoylglutathione lyase is an enzyme that in humans is encoded by the GLO1 gene.[1][2][3] It is a Lactoylglutathione lyase.
The enzyme encoded by this gene is responsible for the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation with reduced glutatione. Glyoxalase I is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere.[3] Recent research demonstrates that GLO1 expression is upregulated in various human malignant tumors including metastatic melanoma.[4][5]
[edit] References
- ^ Ranganathan S, Walsh ES, Godwin AK, Tew KD (Apr 1993). "Cloning and characterization of human colon glyoxalase-I". J Biol Chem 268 (8): 5661–7. PMID 8449929.
- ^ Kim NS, Umezawa Y, Ohmura S, Kato S (Jun 1993). "Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida". J Biol Chem 268 (15): 11217–21. PMID 7684374.
- ^ a b "Entrez Gene: GLO1 glyoxalase I". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2739.
- ^ Bair WB 3rd, Cabello CM, Uchida K, Bause AS, Wondrak GT (April 2010). "GLO1 Overexpression in Human Malignant Melanoma". Melanoma Res 20 (2): 85–96. doi:10.1097/CMR.0b013e3283364903. PMC 2891514. PMID 20093988. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2891514.
- ^ Santarius T, Bignell GR, Greenman CD, Widaa S, Chen L, Mahoney CL, Butler A, Edkins S, Waris S, Thornalley PJ, Futreal PA, Stratton MR (August 2010). "GLO1-A novel amplified gene in human cancer". Genes Chromosomes Cancer 49 (8): 711–25. doi:10.1002/gcc.20784. PMID 20544845.
[edit] Further reading
- Reinsmoen NL, Friend PS, Miller WV et al (1977). "Inheritance of recombinant HLA-GLO haplotype suggesting the gene sequence". Nature 267 (5608): 276–8. doi:10.1038/267276a0. PMID 141008.
- Hansen HE, Eriksen B (1980). "HLA-GLO linkage analysis in 57 informative families". Hum. Hered. 29 (6): 355–60. doi:10.1159/000153072. PMID 511191.
- Meo T, Douglas T, Rijnbeek AM (1977). "Glyoxalase I polymorphism in the mouse: a new genetic marker linked to H-2". Science 198 (4314): 311–3. doi:10.1126/science.910130. PMID 910130.
- Kömpf J, Bissbort S, Gussmann S, Ritter H (1975). "Polymorphism of red cell glyoxalase I (EI: 4.4.1.5); a new genetic marker in man. Investigation of 169 mother-child combinations". Humangenetik 27 (2): 141–3. PMID 1150236.
- Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
- Goldman D, O'Brien SJ, Lucas-Derse S, Dean M (1992). "Linkage mapping of human polymorphic proteins identified by two-dimensional electrophoresis". Genomics 11 (4): 875–84. doi:10.1016/0888-7543(91)90010-C. PMID 1686020.
- Ridderström M, Mannervik B (1996). "Optimized heterologous expression of the human zinc enzyme glyoxalase I". Biochem. J. 314 ( Pt 2) (Pt 2): 463–7. PMC 1217073. PMID 8670058. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1217073.
- Cameron AD, Olin B, Ridderström M et al (1997). "Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping". EMBO J. 16 (12): 3386–95. doi:10.1093/emboj/16.12.3386. PMC 1169964. PMID 9218781. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1169964.
- Armeni T, Pieri C, Marra M et al (1998). "Studies on the life prolonging effect of food restriction: glutathione levels and glyoxalase enzymes in rat liver". Mech. Ageing Dev. 101 (1–2): 101–10. doi:10.1016/S0047-6374(97)00167-X. PMID 9593316.
- Ridderström M, Cameron AD, Jones TA, Mannervik B (1998). "Involvement of an active-site Zn2+ ligand in the catalytic mechanism of human glyoxalase I". J. Biol. Chem. 273 (34): 21623–8. doi:10.1074/jbc.273.34.21623. PMID 9705294.
- Cameron AD, Ridderström M, Olin B et al (1999). "Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue". Biochemistry 38 (41): 13480–90. doi:10.1021/bi990696c. PMID 10521255.
- Ranganathan S, Ciaccio PJ, Walsh ES, Tew KD (2000). "Genomic sequence of human glyoxalase-I: analysis of promoter activity and its regulation". Gene 240 (1): 149–55. doi:10.1016/S0378-1119(99)00420-5. PMID 10564821.
- Sakamoto H, Mashima T, Kizaki A et al (2000). "Glyoxalase I is involved in resistance of human leukemia cells to antitumor agent-induced apoptosis". Blood 95 (10): 3214–8. PMID 10807791.
- Sakamoto H, Mashima T, Sato S et al (2001). "Selective activation of apoptosis program by S-p-bromobenzylglutathione cyclopentyl diester in glyoxalase I-overexpressing human lung cancer cells". Clin. Cancer Res. 7 (8): 2513–8. PMID 11489834.
- Lupidi G, Venardi G, Bollettini M et al (2002). "Purification and partial characterization of glyoxalase I from bovine brain". Prep. Biochem. Biotechnol. 31 (3): 305–16. doi:10.1081/PB-100104911. PMID 11513094.
- Strausberg RL, Feingold EA, Grouse LH et al (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Vander Jagt DL, Hunsaker LA (2003). "Methylglyoxal metabolism and diabetic complications: roles of aldose reductase, glyoxalase-I, betaine aldehyde dehydrogenase and 2-oxoaldehyde dehydrogenase". Chem. Biol. Interact. 143-144: 341–51. doi:10.1016/S0009-2797(02)00212-0. PMID 12604221.
- Sergeev AS, Agapova RK, Bogadel'nikova IV, Perel'man MI (2003). "[The use of discrete characters in discriminant analysis for diagnosis of pulmonary tuberculosis and for classification of patients differing in treatment efficiency based on polymorphisms at nine codominant loci-HP, GC, TF, PI, PGM1, GLO1, C3, ACP1 and ESD]". Genetika 39 (7): 996–1002. PMID 12942785.
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