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GGH

Gene
GGH
Protein
Gamma-glutamyl hydrolase
Organism
Bos taurus
Length
318 amino acids
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. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates. Exhibits either endo- or exopeptidase activity depending upon the tissue of origin. When secreted, it acts primarily as an endopeptidase (By similarity).
Similarity
Belongs to the peptidase C26 family.
Mass
35.683 kDa
Sequence
MARLGRLLSVLGLVLCGATGLGLSAPPAPTPKKPIIGILMQKCHNKNMRALGKYYIAASYVKFLESAGARVVPVRLDLKNEEYEKLFKSINGVLFPGGSVNLMRSGYARVAKMFYNLSIKSFGEGDYFPVWGTCLGFEELIYLVSGESLLTLTDTVGIKLPLNFSRGTLQSRMFQNFPADLLLSLAVEPLTAHFHKWSLSVMNFTKNEKLKAFFSILTTNTDGNIDFISTMEGYRYPIYGVQWHPEKAPYEWGQLRGISHAPNAVKAAFYLAEFFVAEARKSNHHFESDVEETKALIYQYRPTYTGNVSSFQQSYIFD

Gene
GGH
Protein
Gamma-glutamyl hydrolase
Organism
Homo sapiens
Length
318 amino acids
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. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates.
Similarity
Belongs to the peptidase C26 family.
Mass
35.964 kDa
Sequence
MASPGCLLCVLGLLLCGAASLELSRPHGDTAKKPIIGILMQKCRNKVMKNYGRYYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLRRSDYAKVAKIFYNLSIQSFDDGDYFPVWGTCLGFEELSLLISGECLLTATDTVDVAMPLNFTGGQLHSRMFQNFPTELLLSLAVEPLTANFHKWSLSVKNFTMNEKLKKFFNVLTTNTDGKIEFISTMEGYKYPVYGVQWHPEKAPYEWKNLDGISHAPNAVKTAFYLAEFFVNEARKNNHHFKSESEEEKALIYQFSPIYTGNISSFQQCYIFD

Gene
Ggh
Protein
Gamma-glutamyl hydrolase
Organism
Mus musculus
Length
317 amino acids
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. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates. Acts as endopeptidase. Lysosomal enzyme is activated by sulfhydryl compounds.
Similarity
Belongs to the peptidase C26 family.
Mass
35.47 kDa
Sequence
MANLGYLLCLLGLLLCGLSSPGMSRPYNHGSERPIIGVVMQECFGKMAKLGNYYIAASYVKYIESAGARVVPIRPDLSDAEYEELFRSINGVLLPGGGANLTDSGYSRVAKIFFSKALESFDNGDHFPVWGTCLGFEELSVLVSGENLLTSTDTKSKKLPLNFTEGARKSRMFKHFPTELLDSLALENLTANFHKWSLSVKNFTENEKLKKFFNILTTNTDGKTEFISSMEGFKYPVYAVQWHPEKAAFEWKNLGGISHAPNAVKTSFYLAEFLVSEARKNSHHFENVVKETASLIYKFNPIYTGNISSFQQAYMFD

Gene
Ggh
Protein
Gamma-glutamyl hydrolase
Organism
Rattus norvegicus
Length
317 amino acids
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. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates. Exhibits either endo- or exopeptidase activity depending upon the tissue of origin. When secreted, it acts primarily as an endopeptidase.
Similarity
Belongs to the peptidase C26 family.
Mass
35.83 kDa
Sequence
MASLGRLLCAWVLLLCGLASPGLSGSYERGSKRPIIGIIMQECYGNMTKLGRFYIAASYVKFIESAGARVVPIRLDLNDAQYETLFRSINGVLLPGGGANLTHSGYSRVAKIFFTKALESFDNGDYFPVWGTCLGLEELSVLVSNDNLLTLTNTSSVKLPLNFTRDSKQSRMFRNLPEELLNSLASENLTANFHKWSLSVKNFTENEKLKKFFNILTVNTDGKTEFISSMEGYKYPIYAVQWHPEKAPFEWKKLRGISHAPNAVKTSFYLAKFFISEALKNDHHFENELEETESLIYQFCPVYTGNISSFQQAYMFN