Gamma-glutamyl hydrolase
Details
- Name
- Gamma-glutamyl hydrolase
- Kind
- protein
- Synonyms
- 3.4.19.9
- Conjugase
- Gamma-Glu-X carboxypeptidase
- GH
- Gene Name
- GGH
- UniProtKB Entry
- Q92820Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0018932|Gamma-glutamyl hydrolase MASPGCLLCVLGLLLCGAASLELSRPHGDTAKKPIIGILMQKCRNKVMKNYGRYYIAASY VKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLRRSDYAKVAKIFYNLSIQ SFDDGDYFPVWGTCLGFEELSLLISGECLLTATDTVDVAMPLNFTGGQLHSRMFQNFPTE LLLSLAVEPLTANFHKWSLSVKNFTMNEKLKKFFNVLTTNTDGKIEFISTMEGYKYPVYG VQWHPEKAPYEWKNLDGISHAPNAVKTAFYLAEFFVNEARKNNHHFKSESEEEKALIYQF SPIYTGNISSFQQCYIFD
- Number of residues
- 318
- Molecular Weight
- 35964.045
- Theoretical pI
- 7.14
- GO Classification
- Componentsazurophil granule lumen / extracellular region / specific granule lumen / tertiary granule lumen
- General Function
- Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate (PubMed:11005824, PubMed:8816764). May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates
- Specific Function
- exopeptidase activity
- Pfam Domain Function
- Peptidase_C26 (PF07722)
- Signal Regions
- 1-24
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted, extracellular space
- Gene sequence
>lcl|BSEQ0018933|Gamma-glutamyl hydrolase (GGH) ATGGCCAGTCCGGGCTGCCTGCTGTGCGTGCTGGGCCTGCTACTCTGCGGGGCGGCGAGC CTCGAGCTGTCTAGACCCCACGGCGACACCGCCAAGAAGCCCATCATCGGAATATTAATG CAAAAATGCCGTAATAAAGTCATGAAAAACTATGGAAGATACTATATTGCTGCGTCCTAT GTAAAGTACTTGGAGTCTGCAGGTGCGAGAGTTGTACCAGTAAGGCTGGATCTTACAGAG AAAGACTATGAAATACTTTTCAAATCTATTAATGGAATCCTTTTCCCTGGAGGAAGTGTT GACCTCAGACGCTCAGATTATGCTAAAGTGGCCAAAATATTTTATAACTTGTCCATACAG AGTTTTGATGATGGAGACTATTTTCCTGTGTGGGGCACATGCCTTGGATTTGAAGAGCTT TCACTGCTGATTAGTGGAGAGTGCTTATTAACTGCCACAGATACTGTTGACGTGGCAATG CCGCTGAACTTCACTGGAGGTCAATTGCACAGCAGAATGTTCCAGAATTTTCCTACTGAG TTGTTGCTGTCATTAGCAGTAGAACCTCTGACTGCCAATTTCCATAAGTGGAGCCTCTCC GTGAAGAATTTTACAATGAATGAAAAGTTAAAGAAGTTTTTCAATGTCTTAACTACAAAT ACAGATGGCAAGATTGAGTTTATTTCAACAATGGAAGGATATAAGTATCCAGTATATGGT GTCCAGTGGCATCCAGAGAAAGCACCTTATGAGTGGAAGAATTTGGATGGCATTTCCCAT GCACCTAATGCTGTGAAAACCGCATTTTATTTAGCAGAGTTTTTTGTTAATGAAGCTCGG AAAAACAACCATCATTTTAAATCTGAATCTGAAGAGGAGAAAGCATTGATTTATCAGTTC AGTCCAATTTATACTGGAAATATTTCTTCATTTCAGCAATGTTACATATTTGATTGA
- Chromosome Location
- 8
- Locus
- 8q12.3
- External Identifiers
Resource Link UniProtKB ID Q92820 UniProtKB Entry Name GGH_HUMAN GenBank Protein ID 2951931 GenBank Gene ID U55206 GeneCard ID GGH GenAtlas ID GGH HGNC ID HGNC:4248 PDB ID(s) 1L9X KEGG ID hsa:8836 NCBI Gene ID 8836 - General References
- Yao R, Schneider E, Ryan TJ, Galivan J: Human gamma-glutamyl hydrolase: cloning and characterization of the enzyme expressed in vitro. Proc Natl Acad Sci U S A. 1996 Sep 17;93(19):10134-8. [Article]
- Yin D, Chave KJ, Macaluso CR, Galivan J, Yao R: Structural organization of the human gamma-glutamyl hydrolase gene. Gene. 1999 Oct 1;238(2):463-70. [Article]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
- Chave KJ, Galivan J, Ryan TJ: Site-directed mutagenesis establishes cysteine-110 as essential for enzyme activity in human gamma-glutamyl hydrolase. Biochem J. 1999 Nov 1;343 Pt 3:551-5. [Article]
- Chave KJ, Auger IE, Galivan J, Ryan TJ: Molecular modeling and site-directed mutagenesis define the catalytic motif in human gamma -glutamyl hydrolase. J Biol Chem. 2000 Dec 22;275(51):40365-70. [Article]
- Basrur V, Yang F, Kushimoto T, Higashimoto Y, Yasumoto K, Valencia J, Muller J, Vieira WD, Watabe H, Shabanowitz J, Hearing VJ, Hunt DF, Appella E: Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. J Proteome Res. 2003 Jan-Feb;2(1):69-79. [Article]
- Eisele LE, Chave KJ, Lehning AC, Ryan TJ: Characterization of Human gamma-glutamyl hydrolase in solution demonstrates that the enzyme is a non-dissociating homodimer. Biochim Biophys Acta. 2006 Sep;1764(9):1479-86. Epub 2006 Jul 12. [Article]
- Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [Article]
- Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
- Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
- Li H, Ryan TJ, Chave KJ, Van Roey P: Three-dimensional structure of human gamma -glutamyl hydrolase. A class I glatamine amidotransferase adapted for a complex substate. J Biol Chem. 2002 Jul 5;277(27):24522-9. Epub 2002 Apr 12. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Folic acid approved, nutraceutical, vet_approved unknown enzyme substrate Details Methotrexate approved unknown enzyme substrate Details