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gamma-glutamyl hydrolase; conjugase; GH; gamma-Glu-X carboxypeptidase (GGH)

Function: - hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates - progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) & free glutamate - may play an important role in the bioavailability of dietary pteroylpolyglutamates & in the metabolism of pteroylpolyglutamates & antifolates - hydrolysis of a gamma-glutamyl bond - homodimer (probable) Structure: - belongs to the peptidase C26 family - contains 1 gamma-glutamyl hydrolase domain Compartment: - secreted, extracellular space - lysosome, melanosome - intracellular location is primarily the lysosome; however, most of enzyme activity is secreted - identified by mass spectrometry in melanosome fractions from stage 1 to stage 4

General

carboxypeptidase glycoprotein

Properties

SIZE: entity length = 318 aa MW = 36 kD COMPARTMENT: lysosome MOTIF: signal sequence {1-24} Gamma-glutamyl hydrolase {25-318} MOTIF: N-glycosylation site {N116} cysteine residue {C134} N-glycosylation site {N163} N-glycosylation site {N203} histidine residue {H244} N-glycosylation site {N307}

Database Correlations

OMIM 601509 UniProt Q92820 Pfam PF07722 Entrez Gene 8836 Kegg hsa:8836 ENZYME 3.4.19.9

References

  1. UniProt :accession Q92820
  2. Atlas of Genetics & Cytogenetics in Oncology & Haematology http://atlasgeneticsoncology.org/genes/GGHID44358ch8q12.html