EC number:6.3.1.18

Enzyme

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     6. Ligases
        6.3 Forming carbon-nitrogen bonds
            6.3.1 Acid-D-ammonia (or amine) ligases (amide synthases)
ID:6.3.1.18
Description:Gamma-glutamylanilide synthase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 6.3.1.18
BRENDA Enzyme Link: BRENDA 6.3.1.18
KEGG Enzyme Link: KEGG6.3.1.18
BioCyc Enzyme Link: BioCyc 6.3.1.18
ExPASy Enzyme Link: ExPASy6.3.1.18
EC2PDB Enzyme Link: EC2PDB 6.3.1.18
ExplorEnz Enzyme Link: ExplorEnz 6.3.1.18
PRIAM enzyme-specific profiles Link: PRIAM 6.3.1.18
IntEnz Enzyme Link: IntEnz 6.3.1.18
MEDLINE Enzyme Link: MEDLINE 6.3.1.18

EC number:6.3.1.18

MSA:

6.3.1.18;
Phylogenetic Tree:

6.3.1.18;
Uniprot:
M-CSA:
RHEA:41648 aniline + ATP + L-glutamate = ADP + N(5)-phenyl-L-glutamine + phosphate
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[OH;+0:6].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[O;H0;+0:11]-[*:12]>>[*:12]-[OH;+0:11].[*:3]=[C;H0;+0:4](-[*:5])-[NH;+0:2]-[*:1].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Function of a glutamine synthetase-like protein in bacterial aniline oxidation via γ-glutamylanilide.Takeo M, Ohara A, Sakae S, Okamoto Y, Kitamura C, Kato D, Negoro S2013 Oct23893114