Enzyme

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     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.3 In linear amidines
ID:3.5.3.22
Description:Proclavaminate amidinohydrolase.
Alternative Name: Proclavaminic acid amidino hydrolase.
Proclavaminate amidino hydrolase.
PAH.
Prosite: PDOC00135;
PDB:
PDBScop
Cath: 3.40.800.10; 3.60.130.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.3.22
BRENDA Enzyme Link: BRENDA 3.5.3.22
KEGG Enzyme Link: KEGG3.5.3.22
BioCyc Enzyme Link: BioCyc 3.5.3.22
ExPASy Enzyme Link: ExPASy3.5.3.22
EC2PDB Enzyme Link: EC2PDB 3.5.3.22
ExplorEnz Enzyme Link: ExplorEnz 3.5.3.22
PRIAM enzyme-specific profiles Link: PRIAM 3.5.3.22
IntEnz Enzyme Link: IntEnz 3.5.3.22
MEDLINE Enzyme Link: MEDLINE 3.5.3.22
MSA:

3.5.3.22;

Phylogenetic Tree:

3.5.3.22;

Uniprot:
M-CSA:
RHEA:17001 amidinoproclavaminate + H2O = proclavaminate + urea
RULE(radius=1) [*:1]-[NH;+0:2]-[C;H0;+0:3](-[*:4])=[NH;+0:5].[OH2;+0:6]>>[*:4]-[C;H0;+0:3](-[NH2;+0:5])=[O;H0;+0:6].[*:1]-[NH2;+0:2]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Identification, cloning, sequencing, and overexpression of the gene encoding proclavaminate amidino hydrolase and characterization of protein function in clavulanic acid biosynthesis.Wu TK, Busby RW, Houston TA, McIlwaine DB, Egan LA, Townsend CA1995 Jul7601835
Oligomeric structure of proclavaminic acid amidino hydrolase: evolution of a hydrolytic enzyme in clavulanic acid biosynthesis.Elkins JM, Clifton IJ, Hernández H, Doan LX, Robinson CV, Schofield CJ, Hewitson KS2002 Sep 112020346
New reactions in clavulanic acid biosynthesis.Townsend CA2002 Oct12413541
Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional alpha-KG-dependent non-heme iron enzyme: correlation with mechanisms and reactivities.Zhou J, Kelly WL, Bachmann BO, Gunsior M, Townsend CA, Solomon EI2001 Aug 111472170