GLO1

From Wikipedia, the free encyclopedia

Glyoxalase I

Rendering based on 1bh5.

Available structures: 1bh5, 1fro, 1qin, 1qip

Identifiers

Symbol(s)

GLO1; GLYI

External IDs

OMIM: 138750 MGI: 95742 HomoloGene: 4880

EC number

4.4.1.5

Gene ontology
Molecular Function:	• lactoylglutathione lyase activity • zinc ion binding • lyase activity • metal ion binding
Cellular Component:	• cytoplasm
Biological Process:	• carbohydrate metabolic process • anti-apoptosis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006708 (mRNA)
NP_006699 (protein)

XM_992039 (mRNA)
XP_997133 (protein)

Location

Chr 6: 38.75 - 38.78 Mb

Chr 17: 30.32 - 30.34 Mb

Pubmed search

[1]

[2]

Glyoxalase I, also known as GLO1, is a human gene.^[1] 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 and reduced glutatione. Glyoxalase I is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere.^[1]

[edit] References

^ ^a ^b Entrez Gene: GLO1 glyoxalase I.

[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. PMID 141008.
Hansen HE, Eriksen B (1980). "HLA-GLO linkage analysis in 57 informative families.". Hum. Hered. 29 (6): 355-60. 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. 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. 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. PMID 1686020.
Kim NS, Umezawa Y, Ohmura S, Kato S (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.
Ranganathan S, Walsh ES, Godwin AK, Tew KD (1993). "Cloning and characterization of human colon glyoxalase-I.". J. Biol. Chem. 268 (8): 5661-7. PMID 8449929.
Ridderström M, Mannervik B (1996). "Optimized heterologous expression of the human zinc enzyme glyoxalase I.". Biochem. J. 314 ( Pt 2): 463-7. PMID 8670058.
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. PMID 9218781.
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. 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. 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. 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. 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. 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. PMID 12477932.
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. 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.