EC number:3.5.3.7

Enzyme

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EC Tree
     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.3 In linear amidines
ID:3.5.3.7
Description:Guanidinobutyrase.
Prosite: PDOC00135;
PDB:
PDBScop
Cath: 3.40.800.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.3.7
BRENDA Enzyme Link: BRENDA 3.5.3.7
KEGG Enzyme Link: KEGG3.5.3.7
BioCyc Enzyme Link: BioCyc 3.5.3.7
ExPASy Enzyme Link: ExPASy3.5.3.7
EC2PDB Enzyme Link: EC2PDB 3.5.3.7
ExplorEnz Enzyme Link: ExplorEnz 3.5.3.7
PRIAM enzyme-specific profiles Link: PRIAM 3.5.3.7
IntEnz Enzyme Link: IntEnz 3.5.3.7
MEDLINE Enzyme Link: MEDLINE 3.5.3.7

EC number:3.5.3.7

MSA:

3.5.3.7;
Phylogenetic Tree:

3.5.3.7;
Uniprot:
M-CSA:
RHEA:19501 4-guanidinobutanoate + H2O = 4-aminobutanoate + urea
RULE(radius=1) [*:1]-[C;H0;+0:2](=[NH;+0:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](-[NH2;+0:3])=[O;H0;+0:6].[*:5]-[NH2;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Crystal structures of Pseudomonas aeruginosa guanidinobutyrase and guanidinopropionase, members of the ureohydrolase superfamily.Lee SJ, Kim DJ, Kim HS, Lee BI, Yoon HJ, Yoon JY, Kim KH, Jang JY, Im HN, An DR, Song JS, Kim HJ, Suh SW2011 Sep21600989
Characterization and regulation of the gbuA gene, encoding guanidinobutyrase in the arginine dehydrogenase pathway of Pseudomonas aeruginosa PAO1.Nakada Y, Itoh Y2002 Jun12029055
An alternative, arginase-independent pathway for arginine metabolism in Kluyveromyces lactis involves guanidinobutyrase as a key enzyme.Romagnoli G, Verhoeven MD, Mans R, Fleury Rey Y, Bel-Rhlid R, van den Broek M, Seifar RM, Ten Pierick A, Thompson M, Müller V, Wahl SA, Pronk JT, Daran JM2014 Jul24912400