EC 3 - Hydrolases
EC 3.5 - Acting on carbon-nitrogen bonds, other than peptide bonds
EC 3.5.3 - In linear amidines
EC 3.5.3.7 - Guanidinobutyrase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 3.5.3.7
Names
Accepted name:
guanidinobutyrase
Other
names:
4-guanidinobutyrate amidinobutyrase
γ-guanidinobutyrate amidinohydrolase
γ-guanidobutyrase
G-Base
GBH
guanidinobutyrate ureahydrolase
γ-guanidinobutyrate amidinohydrolase
γ-guanidobutyrase
G-Base
GBH
guanidinobutyrate ureahydrolase
Systematic name:
4-guanidinobutanoate amidinohydrolase
Reaction
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19501 [IUBMB]4-guanidinobutanoateName origin: UniProt - CHECKED (C)Formula: C5H11N3O2
Charge: 0ChEBI compound status: CHECKED (C)H2OName origin: UniProt - CHECKED (C)Formula: H2O
Charge: 0ChEBI compound status: CHECKED (C)<?>4-aminobutanoateName origin: UniProt - CHECKED (C)Formula: C4H9NO2
Charge: 0ChEBI compound status: CHECKED (C)
Cofactor
Comments:
Requires Mn2+. Also acts, very slowly, on 5-guanidinopentanoate and 6-guanidinohexanoate.
Links to other databases
Protein domains and families:
PROSITE:PDOC00135
Gene Ontology:
GO:0047971
CAS Registry Number:
9013-69-8
UniProtKB/Swiss-Prot:
References
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Characteristics of arginases from ureotelic and non-ureotelic animals.Biochem. J. 96: 588-594 (1965). [PMID: 5862400]
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[Induction and specificity of enzymes of the new catabolic arginine pathway].Biochim. Biophys. Acta 115: 73-80 (1966). [PMID: 5936244]
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4-Guanidinobutyrate amidinohydrolase from Pseudomonas sp ATCC 14676: purification to homogeneity and properties.Agric. Biol. Chem. 44: 1127-1134 (1980).
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Distribution of amidinohydrolases among Pseudomonas and comparative studies of some purified enzymes by one-dimensional peptide mapping.Agric. Biol. Chem. 47: 2825-2830 (1983).
[EC 3.5.3.7 created 1972]