Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.3 Carboxy- and carbamoyltransferases
ID:2.1.3.6
Description:Putrescine carbamoyltransferase.
Cath: 3.75.10.10; 3.40.50.1370;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.3.6
BRENDA Enzyme Link: BRENDA 2.1.3.6
KEGG Enzyme Link: KEGG2.1.3.6
BioCyc Enzyme Link: BioCyc 2.1.3.6
ExPASy Enzyme Link: ExPASy2.1.3.6
EC2PDB Enzyme Link: EC2PDB 2.1.3.6
ExplorEnz Enzyme Link: ExplorEnz 2.1.3.6
PRIAM enzyme-specific profiles Link: PRIAM 2.1.3.6
IntEnz Enzyme Link: IntEnz 2.1.3.6
MEDLINE Enzyme Link: MEDLINE 2.1.3.6
MSA:

2.1.3.6;

Phylogenetic Tree:

2.1.3.6;

Uniprot:
M-CSA:
RHEA:21936 carbamoyl phosphate + putrescine = H(+) + N-carbamoylputrescine + phosphate
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[O;H0;+0:6]-[*:7]>>[*:1]-[NH;+0:2]-[C;H0;+0:4](=[*:3])-[*:5].[*:7]-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Fermentation of agmatine in Streptococcus faecalis: occurrence of putrescine transcarbamoylase.Roon RJ, Barker HA1972 Jan4621632
The gene cluster for agmatine catabolism of Enterococcus faecalis: study of recombinant putrescine transcarbamylase and agmatine deiminase and a snapshot of agmatine deiminase catalyzing its reaction.Llácer JL, Polo LM, Tavárez S, Alarcón B, Hilario R, Rubio V2007 Feb17028272
Structure and properties of the putrescine carbamoyltransferase of Streptococcus faecalis.Wargnies B, Lauwers N, Stalon V1979 Nov 1116850