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Gamma-glutamyltransferase 1
Symbols GGT1; CD224; D22S672; D22S732; GGT; GTG; MGC96892; MGC96904; MGC96963
External IDs OMIM231950 MGI95706 HomoloGene68450 GeneCards: GGT1 Gene
EC number EC
Species Human Mouse
Entrez 2678 14598
Ensembl n/a ENSMUSG00000006345
UniProt n/a Q4FK56
RefSeq (mRNA) NM_001032364 NM_008116
RefSeq (protein) NP_001027536 NP_032142
Location (UCSC) n/a Chr 10:
75.01 - 75.03 Mb
PubMed search [1] [2]

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


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. 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. 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.  
  • 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. 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. 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): 503–8. 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

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



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