GSTZ1

Glutathione transferase zeta 1
PDB rendering based on 1fw1.
Available structures PDB 1fw1
Identifiers
Symbols	GSTZ1; GSTZ1-1; MAAI; MAI; MGC2029
External IDs	OMIM: 603758 MGI: 1341859 HomoloGene: 7747 GeneCards: GSTZ1 Gene
Gene Ontology Molecular function • glutathione transferase activity • glutathione peroxidase activity • protein binding • maleylacetoacetate isomerase activity • maleylacetoacetate isomerase activity • transferase activity • isomerase activity • protein homodimerization activity Cellular component • cytoplasm • mitochondrion • cytosol Biological process • L-phenylalanine catabolic process • tyrosine catabolic process • glutathione metabolic process • aromatic amino acid family metabolic process • cellular nitrogen compound metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2954	14874
Ensembl	ENSG00000100577	ENSMUSG00000021033
UniProt	O43708	Q9JJA0
RefSeq (mRNA)	NM_001513.3	NM_010363.3
RefSeq (protein)	NP_001504.2	NP_034493.1
Location (UCSC)	Chr 14: 77.79 – 77.8 Mb	Chr 12: 88.49 – 88.51 Mb
PubMed search	[1]	[2]

Maleylacetoacetate isomerase is an enzyme that in humans is encoded by the GSTZ1 gene.

This gene is a member of the glutathione S-transferase (GSTs) super-family which encodes multifunctional enzymes important in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. This enzyme also plays a significant role in the catabolism of phenylalanine and tyrosine. Thus defects in this enzyme may lead to severe metabolic disorders including alkaptonuria, phenylketonuria and tyrosinaemia. Several transcript variants of this gene encode multiple protein isoforms.

Further reading

• Ketterer B (2001). "A bird's eye view of the glutathione transferase field.". Chem. Biol. Interact. 138 (1): 27–42. doi:10.1016/S0009-2797(01)00277-0. PMID 11640913. 
• Tong Z, Board PG, Anders MW (1998). "Glutathione transferase zeta catalyses the oxygenation of the carcinogen dichloroacetic acid to glyoxylic acid.". Biochem. J.. 331 ( Pt 2): 371–4. PMC 1219363. PMID 9531472. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1219363. 
• Tong Z, Board PG, Anders MW (1999). "Glutathione transferase zeta-catalyzed biotransformation of dichloroacetic acid and other alpha-haloacids.". Chem. Res. Toxicol. 11 (11): 1332–8. doi:10.1021/tx980144f. PMID 9815194. 
• Blackburn AC, Woollatt E, Sutherland GR, Board PG (1999). "Characterization and chromosome location of the gene GSTZ1 encoding the human Zeta class glutathione transferase and maleylacetoacetate isomerase.". Cytogenet. Cell Genet. 83 (1-2): 109–14. doi:10.1159/000015145. PMID 9925947. 
• Fernández-Cañón JM, Hejna J, Reifsteck C, et al. (1999). "Gene structure, chromosomal location, and expression pattern of maleylacetoacetate isomerase.". Genomics 58 (3): 263–9. doi:10.1006/geno.1999.5832. PMID 10373324. 
• Blackburn AC, Tzeng HF, Anders MW, Board PG (2000). "Discovery of a functional polymorphism in human glutathione transferase zeta by expressed sequence tag database analysis.". Pharmacogenetics 10 (1): 49–57. doi:10.1097/00008571-200002000-00007. PMID 10739172. 
• Polekhina G, Board PG, Blackburn AC, Parker MW (2001). "Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity.". Biochemistry 40 (6): 1567–76. doi:10.1021/bi002249z. PMID 11327815. 
• Blackburn AC, Coggan M, Tzeng HF, et al. (2002). "GSTZ1d: a new allele of glutathione transferase zeta and maleylacetoacetate isomerase.". Pharmacogenetics 11 (8): 671–8. doi:10.1097/00008571-200111000-00005. PMID 11692075. 
• 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. 
• Heilig R, Eckenberg R, Petit JL, et al. (2003). "The DNA sequence and analysis of human chromosome 14.". Nature 421 (6923): 601–7. doi:10.1038/nature01348. PMID 12508121. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Ricci G, Turella P, De Maria F, et al. (2004). "Binding and kinetic mechanisms of the Zeta class glutathione transferase.". J. Biol. Chem. 279 (32): 33336–42. doi:10.1074/jbc.M404631200. PMID 15173170. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Hui J, Hung LH, Heiner M, et al. (2005). "Intronic CA-repeat and CA-rich elements: a new class of regulators of mammalian alternative splicing.". EMBO J. 24 (11): 1988–98. doi:10.1038/sj.emboj.7600677. PMC 1142610. PMID 15889141. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1142610. 
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
• Fang YY, Kashkarov U, Anders MW, Board PG (2006). "Polymorphisms in the human glutathione transferase zeta promoter.". Pharmacogenet. Genomics 16 (5): 307–13. doi:10.1097/01.fpc.0000205000.07054.b3. PMID 16609361.