EC |
3.5.1.123 |
Accepted name: |
γ-glutamylanilide hydrolase |
Reaction: |
N5-phenyl-L-glutamine + H2O = L-glutamate + aniline |
Glossary: |
γ-glutamylanilide = N5-phenyl-L-glutamine |
Other name(s): |
atdA2 (gene name) |
Systematic name: |
N5-phenyl-L-glutamine amidohydrolase |
Comments: |
The enzyme, characterized from the bacterium Acinetobacter sp. YAA, catalyses the opposite reaction from that catalysed by EC 6.3.1.18, γ-glutamylanilide synthase, which is part of an aniline degradation pathway. Its purpose is likely to maintain a low concentration of N5-phenyl-L-glutamine, which is potentially toxic. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Takeo, M., Ohara, A., Sakae, S., Okamoto, Y., Kitamura, C., Kato, D. and Negoro, S. Function of a glutamine synthetase-like protein in bacterial aniline oxidation via γ-glutamylanilide. J. Bacteriol. 195 (2013) 4406–4414. [DOI] [PMID: 23893114] |
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[EC 3.5.1.123 created 2016] |
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EC |
6.3.1.18 |
Accepted name: |
γ-glutamylanilide synthase |
Reaction: |
ATP + L-glutamate + aniline = ADP + phosphate + N5-phenyl-L-glutamine |
Glossary: |
γ-glutamylanilide = N5-phenyl-L-glutamine |
Other name(s): |
atdA1 (gene name); tdnQ (gene name); dcaQ (gene name) |
Systematic name: |
L-glutamate:aniline ligase (ADP-forming) |
Comments: |
Requires Mg2+. The enzyme, characterized from the bacterium Acinetobacter sp. YAA, catalyses the first step in the degradation of aniline. It can also accept chlorinated and methylated forms of aniline, preferrably in the o- and p-positions. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB |
References: |
1. |
Takeo, M., Ohara, A., Sakae, S., Okamoto, Y., Kitamura, C., Kato, D. and Negoro, S. Function of a glutamine synthetase-like protein in bacterial aniline oxidation via γ-glutamylanilide. J. Bacteriol. 195 (2013) 4406–4414. [DOI] [PMID: 23893114] |
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[EC 6.3.1.18 created 2014] |
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