Enzyme

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EC Tree
     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.1 In linear amides
ID:3.5.1.84
Description:Biuret amidohydrolase.
Cath: 3.10.490.10; 3.30.1330.160; 3.30.1330.170; 3.30.1330.180; 3.30.1360.40; 3.90.1300.10; 1.20.58.1700; 2.40.100.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.84
BRENDA Enzyme Link: BRENDA 3.5.1.84
KEGG Enzyme Link: KEGG3.5.1.84
BioCyc Enzyme Link: BioCyc 3.5.1.84
ExPASy Enzyme Link: ExPASy3.5.1.84
EC2PDB Enzyme Link: EC2PDB 3.5.1.84
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.84
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.84
IntEnz Enzyme Link: IntEnz 3.5.1.84
MEDLINE Enzyme Link: MEDLINE 3.5.1.84
MSA:

3.5.1.84;

Phylogenetic Tree:

3.5.1.84;

Uniprot:
M-CSA:
RHEA:17525 biuret + H2O = NH4(+) + urea-1-carboxylate
RULE(radius=1) [*:1]-[C;H0;+0:2](=[*:3])-[NH2;+0:4].[OH2;+0:5]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:5].[NH3;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structural and biochemical characterization of the biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv. viciae 3841.Esquirol L, Peat TS, Wilding M, Lucent D, French NG, Hartley CJ, Newman J, Scott C201829425231
A New Family of Biuret Hydrolases Involved in S-Triazine Ring Metabolism.Cameron SM, Durchschein K, Richman JE, Sadowsky MJ, Wackett LP2011 Aug 121897878
Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism.Cheng G, Shapir N, Sadowsky MJ, Wackett LP2005 Aug16085834
Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP.Shapir N, Sadowsky MJ, Wackett LP2005 Jun15901697
Complete nucleotide sequence and organization of the atrazine catabolic plasmid pADP-1 from Pseudomonas sp. strain ADP.Martinez B, Tomkins J, Wackett LP, Wing R, Sadowsky MJ2001 Oct11544232