Gamma-glutamyltransferase 1

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

GGT1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4GDX, 4GG2, 4Z9O, 4ZBK, 4ZC6, 4ZCG
Identifiers
Aliases	GGT1, CD224, D22S672, D22S732, GGT, GGT 1, GTG, gamma-glutamyltransferase 1, GGTD
External IDs	OMIM: 612346; MGI: 95706; HomoloGene: 68450; GeneCards: GGT1; OMA:GGT1 - orthologs
EC number	3.4.19.13
Gene location (Human) Chr. Chromosome 22 (human) Band 22q11.23 Start 24,594,811 bp End 24,629,005 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10|10 C1 Start 75,561,604 bp End 75,586,200 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver mucosa of transverse colon gallbladder right lung body of pancreas upper lobe of left lung right lobe of thyroid gland human kidney left lobe of thyroid gland gonad Top expressed in right kidney proximal tubule human kidney intestinal villus duodenum seminal vesicula epithelium of small intestine jejunum decidua efferent ductule More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity peptidase activity protein binding acyltransferase activity hydrolase activity glutathione hydrolase activity hypoglycin A gamma-glutamyl transpeptidase activity peptidyltransferase activity leukotriene-C(4) hydrolase leukotriene C4 gamma-glutamyl transferase activity Cellular component integral component of membrane membrane plasma membrane extracellular exosome extracellular space Biological process leukotriene metabolic process zymogen activation glutathione biosynthetic process regulation of immune system process cysteine biosynthetic process spermatogenesis regulation of inflammatory response xenobiotic metabolic process glutamate metabolic process glutathione catabolic process proteolysis cellular amino acid metabolic process glutathione metabolic process fatty acid metabolic process leukotriene D4 biosynthetic process protein biosynthesis peptide modification response to estradiol response to lipopolysaccharide response to tumor necrosis factor Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2678 14598 Ensembl ENSG00000100031 ENSMUSG00000006345 UniProt P19440 Q60928 RefSeq (mRNA) NM_013430 NM_001032364 NM_001032365 NM_001288833 NM_005265 NM_013421 NM_008116 NM_001305992 RefSeq (protein) NP_001275762 NP_038265 NP_038347 NP_001292921 NP_032142 NP_001366466 NP_001366467 NP_001366468 NP_001366469 NP_001366470 Location (UCSC) Chr 22: 24.59 – 24.63 Mb Chr 10: 75.56 – 75.59 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

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.

See also

• Cluster of differentiation

Further reading

• Chikhi N, Holic N, Guellaen G, Laperche Y (April 1999). "Gamma-glutamyl transpeptidase gene organization and expression: a comparative analysis in rat, mouse, pig and human species". Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology. 122 (4): 367–80. doi:10.1016/S0305-0491(99)00013-9. PMID 10392451.
• Indirani N, Hill PG (July 1977). "Partial purification and some properties of gamma-glutamyl transpeptidase from human bile". Biochimica et Biophysica Acta (BBA) - Enzymology. 483 (1): 57–62. doi:10.1016/0005-2744(77)90007-9. PMID 18198.
• Tate SS, Ross ME (September 1977). "Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit". The Journal of Biological Chemistry. 252 (17): 6042–5. doi:10.1016/S0021-9258(17)40026-3. 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, Visvikis A, Diederich M, Wellman M, Siest G (June 1992). "Gamma-glutamyltransferase: nucleotide sequence of the human pancreatic cDNA. Evidence for a ubiquitous gamma-glutamyltransferase polypeptide in human tissues". Biochemical Pharmacology. 43 (12): 2527–33. doi:10.1016/0006-2952(92)90140-E. PMID 1378736.
• Pawlak A, Cohen EH, Octave JN, Schweickhardt R, Wu SJ, Bulle F, Chikhi N, Baik JH, Siegrist S, Guellaën G (February 1990). "An alternatively processed mRNA specific for gamma-glutamyl transpeptidase in human tissues". The Journal of Biological Chemistry. 265 (6): 3256–62. doi:10.1016/S0021-9258(19)39761-3. PMID 1968061.
• Pitot HC, Goodspeed D, Dunn T, Hendrich S, Maronpot RR, Moran S (January 1989). "Regulation of the expression of some genes for enzymes of glutathione metabolism in hepatotoxicity and hepatocarcinogenesis". Toxicology and Applied Pharmacology. 97 (1): 23–34. doi:10.1016/0041-008X(89)90052-5. PMID 2563599.
• Goodspeed DC, Dunn TJ, Miller CD, Pitot HC (March 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, Suzuki A, Chikhi N, Ferry N, Baik JH, Siegrist S, Guellaën G (October 1989). "Different gamma-glutamyl transpeptidase mRNAs are expressed in human liver and kidney". Biochemical and Biophysical Research Communications. 164 (2): 912–8. doi:10.1016/0006-291X(89)91545-3. PMID 2573352.
• Laperche Y, Bulle F, Aissani T, Chobert MN, Aggerbeck M, Hanoune J, Guellaën G (February 1986). "Molecular cloning and nucleotide sequence of rat kidney gamma-glutamyl transpeptidase cDNA". Proceedings of the National Academy of Sciences of the United States of America. 83 (4): 937–41. Bibcode:1986PNAS...83..937L. doi:10.1073/pnas.83.4.937. PMC 322985. PMID 2869484.
• Bulle F, Mattei MG, Siegrist S, Pawlak A, Passage E, Chobert MN, Laperche Y, Guellaën G (July 1987). "Assignment of the human gamma-glutamyl transferase gene to the long arm of chromosome 22". Human Genetics. 76 (3): 283–6. doi:10.1007/BF00283624. PMID 2885259. S2CID 32375892.
• Tate SS, Khadse V, Wellner D (May 1988). "Renal gamma-glutamyl transpeptidases: structural and immunological studies". Archives of Biochemistry and Biophysics. 262 (2): 397–408. doi:10.1016/0003-9861(88)90390-6. PMID 2896486.
• Tate SS, Galbraith RA (August 1988). "In vitro translation and processing of human hepatoma cell (Hep G2) gamma-glutamyl transpeptidase". Biochemical and Biophysical Research Communications. 154 (3): 1167–73. doi:10.1016/0006-291X(88)90263-X. PMID 2900635.
• Rajpert-De Meyts E, Heisterkamp N, Groffen J (December 1988). "Cloning and nucleotide sequence of human gamma-glutamyl transpeptidase". Proceedings of the National Academy of Sciences of the United States of America. 85 (23): 8840–4. Bibcode:1988PNAS...85.8840R. doi:10.1073/pnas.85.23.8840. PMC 282602. PMID 2904146.
• Sakamuro D, Yamazoe M, Matsuda Y, Kangawa K, Taniguchi N, Matsuo H, Yoshikawa H, Ogasawara N (December 1988). "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, Taniguchi N, Meister A (September 1995). "Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase". The Journal of Biological Chemistry. 270 (38): 22223–8. doi:10.1074/jbc.270.38.22223. PMID 7673200.
• Wetmore LA, Gerard C, Drazen JM (August 1993). "Human lung expresses unique gamma-glutamyl transpeptidase transcripts". Proceedings of the National Academy of Sciences of the United States of America. 90 (16): 7461–5. Bibcode:1993PNAS...90.7461W. doi:10.1073/pnas.90.16.7461. PMC 47161. PMID 7689219.
• Ikeda Y, Fujii J, Taniguchi N, Meister A (May 1995). "Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit". The Journal of Biological Chemistry. 270 (21): 12471–5. doi:10.1074/jbc.270.21.12471. PMID 7759490.
• Courtay C, Heisterkamp N, Siest G, Groffen J (February 1994). "Expression of multiple gamma-glutamyltransferase genes in man". The Biochemical Journal. 297 (Pt 3): 503–8. doi:10.1042/bj2970503. PMC 1137862. PMID 7906515.
• Ikeda Y, Fujii J, Taniguchi N (February 1993). "Significance of Arg-107 and Glu-108 in the catalytic mechanism of human gamma-glutamyl transpeptidase. Identification by site-directed mutagenesis". The Journal of Biological Chemistry. 268 (6): 3980–5. doi:10.1016/S0021-9258(18)53567-5. PMID 8095045.

External links

• GGT1 +protein,+human at the U.S. 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.