EC Tree |
3. Hydrolases |
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
3.5.1 In linear amides |
ID: | 3.5.1.123 |
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Description: | Gamma-glutamylanilide hydrolase. |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 3.5.1.123 |
BRENDA Enzyme Link: | BRENDA 3.5.1.123 |
KEGG Enzyme Link: | KEGG3.5.1.123 |
BioCyc Enzyme Link: | BioCyc 3.5.1.123 |
ExPASy Enzyme Link: | ExPASy3.5.1.123 |
EC2PDB Enzyme Link: | EC2PDB 3.5.1.123 |
ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.123 |
PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.123 |
IntEnz Enzyme Link: | IntEnz 3.5.1.123 |
MEDLINE Enzyme Link: | MEDLINE 3.5.1.123 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:50684 | H2O + N(5)-phenyl-L-glutamine = aniline + H(+) + L-glutamate |
RULE(radius=1) | [*:1]-[NH;+0:2]-[C;H0;+0:3](-[*:4])=[*:5].[OH2;+0:6]>>[*:4]-[C;H0;+0:3](=[*:5])-[OH;+0:6].[*:1]-[NH2;+0:2] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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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 S | 2013 Oct | 23893114 |