GGTLA1

GGTLA1

Gamma-glutamyltransferase-like activity 1, also known as GGTLA1, is a human gene.cite web | title = Entrez Gene: GGTLA1 gamma-glutamyltransferase-like activity 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2687| accessdate = ]

PBB_Summary
section_title =
summary_text = Gamma-glutamyltransferase-like activity 1 (GGTLA1) is a member of a gene family with at least 4 members (GGTLA1, GGTLA2, GGTLA3 and GGTLA4). The enzyme encoded by GGTLA1 is related to, but distinct from, gamma-glutamyl transpeptidase (GGT). The GGTLA1 enzyme consists of a heavy and a light chain and is able to hydrolyze the gamma-glutamyl moiety of glutathione. It converts leukotriene C4 to leukotriene D4, however, it doesn't convert synthetic substrates that are commonly used to assay GGT. Its amino acid sequence shows an overall similarity of 39.5% with human GGT.cite web | title = Entrez Gene: GGTLA1 gamma-glutamyltransferase-like activity 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2687| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Heisterkamp N, Groffen J, Warburton D, Sneddon TP |title=The human gamma-glutamyltransferase gene family. |journal=Hum. Genet. |volume= |issue= |pages= |year= |pmid= 18357469 |doi= 10.1007/s00439-008-0487-7
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Enoiu M, Aberkane H, Salazar JF, "et al." |title=Evidence for the pro-oxidant effect of gamma-glutamyltranspeptidase-related enzyme. |journal=Free Radic. Biol. Med. |volume=29 |issue= 9 |pages= 825–33 |year= 2000 |pmid= 11063908 |doi=
*cite journal | author=Dunham I, Shimizu N, Roe BA, "et al." |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489–95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031
*cite journal | author=Edelmann L, Pandita RK, Morrow BE |title=Low-copy repeats mediate the common 3-Mb deletion in patients with velo-cardio-facial syndrome. |journal=Am. J. Hum. Genet. |volume=64 |issue= 4 |pages= 1076–86 |year= 2000 |pmid= 10090893 |doi=
*cite journal | author=Potdar PD, Andrews KL, Nettesheim P, Ostrowski LE |title=Expression and regulation of gamma-glutamyl transpeptidase-related enzyme in tracheal cells. |journal=Am. J. Physiol. |volume=273 |issue= 5 Pt 1 |pages= L1082–9 |year= 1997 |pmid= 9374738 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Morris C, Courtay C, Geurts van Kessel A, "et al." |title=Localization of a gamma-glutamyl-transferase-related gene family on chromosome 22. |journal=Hum. Genet. |volume=91 |issue= 1 |pages= 31–6 |year= 1993 |pmid= 8095916 |doi=
*cite journal | author=Heisterkamp N, Rajpert-De Meyts E, Uribe L, "et al." |title=Identification of a human gamma-glutamyl cleaving enzyme related to, but distinct from, gamma-glutamyl transpeptidase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 14 |pages= 6303–7 |year= 1991 |pmid= 1676842 |doi=

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