GGT1

Gamma-glutamyltransferase 1
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 4GDX​, 4GG2​, 4Z9O​, 4ZBK​, 4ZC6​, 4ZCG​
Identifiers
Symbols	GGT1 ; CD224; D22S672; D22S732; GGT; GGT 1; GTG
External IDs	OMIM: 612346 MGI: 95706 HomoloGene: 68450 ChEMBL: 5696 GeneCards: GGT1 Gene
EC number	2.3.2.2, 3.4.19.13, 3.4.19.14
Gene ontology Molecular function • gamma-glutamyltransferase activity • protein binding • glutathione hydrolase activity Cellular component • extracellular space • plasma membrane • integral component of membrane • anchored component of external side of plasma membrane • extracellular exosome Biological process • regulation of immune system process • cellular amino acid metabolic process • glutamate metabolic process • leukotriene metabolic process • glutathione metabolic process • glutathione biosynthetic process • glutathione catabolic process • xenobiotic metabolic process • spermatogenesis • cysteine biosynthetic process • arachidonic acid metabolic process • leukotriene biosynthetic process • zymogen activation • small molecule metabolic process • regulation of inflammatory response • glutathione derivative biosynthetic process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	2678	14598
Ensembl	ENSG00000100031	ENSMUSG00000006345
UniProt	P19440	Q60928
RefSeq (mRNA)	NM_001032364	NM_001305992
RefSeq (protein)	NP_001275762	NP_001292921
Location (UCSC)	Chr 22: 24.58 – 24.63 Mb	Chr 10: 75.56 – 75.59 Mb
PubMed search

Gamma-glutamyltransferase 1, (GGT1) also known as CD224 (Cluster of Differentiation 224 ), is a human gene.^[1]

Human gamma-glutamyltransferase catalyzes the transfer of the glutamyl moiety of glutathione to a variety of amino acids and dipeptide acceptors. This heteroduplex enzyme is composed of a heavy chain and a light chain, which are derived from a single precursor protein, and is present in tissues involved in absorption and secretion. This enzyme is a member of the gamma-glutamyltransferase protein family, of which many members have not yet been fully characterized. This gene encodes several transcript variants; studies suggest that many transcripts of this gene family may be non-functional or represent pseudogenes. The functional transcripts which have been fully characterized have been grouped and classified as type I gamma-glutamyltransferase. Complex splicing events may take place in a tissue-specific manner, resulting in marked dissimilarity in the 5' UTRs. Several 5' UTR transcript variants of the type I gene have been identified in different tissues and cancer cells.^[1]

See also

• Cluster of differentiation

References

1. "Entrez Gene: GGT1 gamma-glutamyltransferase 1".

Further reading

• Chikhi N, Holic N, Guellaen G, Laperche Y (1999). "Gamma-glutamyl transpeptidase gene organization and expression: a comparative analysis in rat, mouse, pig and human species". Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 122 (4): 367–80. doi:10.1016/S0305-0491(99)00013-9. PMID 10392451.
• Indirani N, Hill PG (1977). "Partial purification and some properties of gamma-glutamyl transpeptidase from human bile". Biochim. Biophys. Acta 483 (1): 57–62. doi:10.1016/0005-2744(77)90007-9. PMID 18198.
• Tate SS, Ross ME (1977). "Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit". J. Biol. Chem. 252 (17): 6042–5. PMID 19463.
• Welbourne TC (1978). "Cytoplasmic gamma-glutamyltransferase: isolation, product formation and physiological role". Current problems in clinical biochemistry 8: 201–15. PMID 28899.
• Courtay C, Oster T, Michelet F, et al. (1992). "Gamma-glutamyltransferase: nucleotide sequence of the human pancreatic cDNA. Evidence for a ubiquitous gamma-glutamyltransferase polypeptide in human tissues". Biochem. Pharmacol. 43 (12): 2527–33. doi:10.1016/0006-2952(92)90140-E. PMID 1378736.
• Pawlak A, Cohen EH, Octave JN, et al. (1990). "An alternatively processed mRNA specific for gamma-glutamyl transpeptidase in human tissues". J. Biol. Chem. 265 (6): 3256–62. PMID 1968061.
• Pitot HC, Goodspeed D, Dunn T, et al. (1989). "Regulation of the expression of some genes for enzymes of glutathione metabolism in hepatotoxicity and hepatocarcinogenesis". Toxicol. Appl. Pharmacol. 97 (1): 23–34. doi:10.1016/0041-008X(89)90052-5. PMID 2563599.
• Goodspeed DC, Dunn TJ, Miller CD, Pitot HC (1989). "Human gamma-glutamyl transpeptidase cDNA: comparison of hepatoma and kidney mRNA in the human and rat". Gene 76 (1): 1–9. doi:10.1016/0378-1119(89)90002-4. PMID 2568315.
• Pawlak A, Wu SJ, Bulle F, et al. (1989). "Different gamma-glutamyl transpeptidase mRNAs are expressed in human liver and kidney". Biochem. Biophys. Res. Commun. 164 (2): 912–8. doi:10.1016/0006-291X(89)91545-3. PMID 2573352.
• Laperche Y, Bulle F, Aissani T, et al. (1986). "Molecular cloning and nucleotide sequence of rat kidney gamma-glutamyl transpeptidase cDNA". Proc. Natl. Acad. Sci. U.S.A. 83 (4): 937–41. doi:10.1073/pnas.83.4.937. PMC 322985. PMID 2869484.
• Bulle F, Mattei MG, Siegrist S, et al. (1987). "Assignment of the human gamma-glutamyl transferase gene to the long arm of chromosome 22". Hum. Genet. 76 (3): 283–6. doi:10.1007/BF00283624. PMID 2885259. replacement character in |last8= at position 7 (help)
• Tate SS, Khadse V, Wellner D (1988). "Renal gamma-glutamyl transpeptidases: structural and immunological studies". Arch. Biochem. Biophys. 262 (2): 397–408. doi:10.1016/0003-9861(88)90390-6. PMID 2896486.
• Tate SS, Galbraith RA (1988). "In vitro translation and processing of human hepatoma cell (Hep G2) gamma-glutamyl transpeptidase". Biochem. Biophys. Res. Commun. 154 (3): 1167–73. doi:10.1016/0006-291X(88)90263-X. PMID 2900635.
• Rajpert-De Meyts E, Heisterkamp N, Groffen J (1988). "Cloning and nucleotide sequence of human gamma-glutamyl transpeptidase". Proc. Natl. Acad. Sci. U.S.A. 85 (23): 8840–4. doi:10.1073/pnas.85.23.8840. PMC 282602. PMID 2904146.
• Sakamuro D, Yamazoe M, Matsuda Y, et al. (1989). "The primary structure of human gamma-glutamyl transpeptidase". Gene 73 (1): 1–9. doi:10.1016/0378-1119(88)90307-1. PMID 2907498.
• Ikeda Y, Fujii J, Anderson ME, et al. (1995). "Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase". J. Biol. Chem. 270 (38): 22223–8. doi:10.1074/jbc.270.38.22223. PMID 7673200.
• Wetmore LA, Gerard C, Drazen JM (1993). "Human lung expresses unique gamma-glutamyl transpeptidase transcripts". Proc. Natl. Acad. Sci. U.S.A. 90 (16): 7461–5. doi:10.1073/pnas.90.16.7461. PMC 47161. PMID 7689219.
• Ikeda Y, Fujii J, Taniguchi N, Meister A (1995). "Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit". J. Biol. Chem. 270 (21): 12471–5. doi:10.1074/jbc.270.21.12471. PMID 7759490.
• Courtay C, Heisterkamp N, Siest G, Groffen J (1994). "Expression of multiple gamma-glutamyltransferase genes in man". Biochem. J. 297 ( Pt 3) (Pt 3): 503–8. PMC 1137862. PMID 7906515.
• Ikeda Y, Fujii J, Taniguchi N (1993). "Significance of Arg-107 and Glu-108 in the catalytic mechanism of human gamma-glutamyl transpeptidase. Identification by site-directed mutagenesis". J. Biol. Chem. 268 (6): 3980–5. PMID 8095045.

External links

• GGT1 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.