EC number:3.5.1.107

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:3.5.1.107
Description:Maleamate amidohydrolase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.107
BRENDA Enzyme Link: BRENDA 3.5.1.107
KEGG Enzyme Link: KEGG3.5.1.107
BioCyc Enzyme Link: BioCyc 3.5.1.107
ExPASy Enzyme Link: ExPASy3.5.1.107
EC2PDB Enzyme Link: EC2PDB 3.5.1.107
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.107
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.107
IntEnz Enzyme Link: IntEnz 3.5.1.107
MEDLINE Enzyme Link: MEDLINE 3.5.1.107

EC number:3.5.1.107

MSA:

3.5.1.107;
Phylogenetic Tree:

3.5.1.107;
Uniprot:
M-CSA:
RHEA:27385 H2O + maleamate = maleate + NH4(+)
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
Structure and catalytic mechanism of nicotinate (vitamin B3) degradative enzyme maleamate amidohydrolase from Bordetella bronchiseptica RB50.Kincaid VA, Sullivan ED, Klein RD, Noel JW, Rowlett RS, Snider MJ2012 Jan 1022214383
Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440.Jiménez JI, Canales A, Jiménez-Barbero J, Ginalski K, Rychlewski L, García JL, Díaz E2008 Aug 1218678916