Reaction participants Show >> << Hide
- Name help_outline N-carbamoyl-L-glutamate Identifier CHEBI:229697 Charge -2 Formula C6H8N2O5 InChIKeyhelp_outline LCQLHJZYVOQKHU-VKHMYHEASA-L SMILEShelp_outline [O-]C(=O)[C@@H](NC(N)=O)CCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 10,232 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-glutamate Identifier CHEBI:29985 (CAS: 11070-68-1) help_outline Charge -1 Formula C5H8NO4 InChIKeyhelp_outline WHUUTDBJXJRKMK-VKHMYHEASA-M SMILEShelp_outline [NH3+][C@@H](CCC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 249 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NH4+ Identifier CHEBI:28938 (CAS: 14798-03-9) help_outline Charge 1 Formula H4N InChIKeyhelp_outline QGZKDVFQNNGYKY-UHFFFAOYSA-O SMILEShelp_outline [H][N+]([H])([H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 544 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CO2 Identifier CHEBI:16526 (CAS: 124-38-9) help_outline Charge 0 Formula CO2 InChIKeyhelp_outline CURLTUGMZLYLDI-UHFFFAOYSA-N SMILEShelp_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 1,073 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:84011 | RHEA:84012 | RHEA:84013 | RHEA:84014 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Two amino acid amidohydrolase genes encoding L-stereospecific carbamoylase and aminoacylase are organized in a common operon in Bacillus stearothermophilus.
Batisse N., Weigel P., Lecocq M., Sakanyan V.
The L-carbamoylase gene (amaB) upstream of the previously detected L-aminoacylase gene (amaA) in the Bacillus stearothermophilus NCIB8224 strain was identified in this study. The amaB and amaA genes are cotranscribed as a single mRNA from the same transcriptional start. The two-ama-gene operon is ... >> More
The L-carbamoylase gene (amaB) upstream of the previously detected L-aminoacylase gene (amaA) in the Bacillus stearothermophilus NCIB8224 strain was identified in this study. The amaB and amaA genes are cotranscribed as a single mRNA from the same transcriptional start. The two-ama-gene operon is conserved in B. stearothermophilus strains. A cross-activity of L-carbamoylase towards respective substrates for L-aminoacylase supports the hypothesis of a common ancestor for both amino acid amidohydrolase genes. << Less
Appl. Environ. Microbiol. 63:763-766(1997) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.
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Gene cloning and characterization of N-carbamyl-l-glutamic acid amidohydrolase involved in ergothioneine utilization in Burkholderia sp. HME13.
Muramatsu H., Yamada M., Maguchi H., Kato S.I.
Burkholderia sp. HME13 utilizes ergothioneine, a strong antioxidant, as the nitrogen source. We have previously shown that ergothionase, thiourocanate hydratase, 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase, and hydantoin-5-propionic acid amidohydrolase may be involved in ergot ... >> More
Burkholderia sp. HME13 utilizes ergothioneine, a strong antioxidant, as the nitrogen source. We have previously shown that ergothionase, thiourocanate hydratase, 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase, and hydantoin-5-propionic acid amidohydrolase may be involved in ergothioneine utilization in this strain. In this study, we identified the ertE gene in Burkholderia sp. HME13, which encodes a bivalent metal-dependent N-carbamyl-l-glutamic acid amidohydrolase (ErtE). ErtE showed maximum activity at 60 °C and pH 7.0 and was stable at temperatures up to 55 °C and pH 6.5-8.0. The Km and Vmax values of ErtE for N-carbamyl-l-glutamic acid were 0.74 m m and 140 U/mg, respectively. Ethylenediaminetetraacetic acid-treated ErtE showed no enzymatic activity, which was restored upon the addition of Co2+, Mn2+, Ni2+, and Fe2+. Expression analyses and enzymatic assays suggested that ErtE is involved in ergothioneine utilization in this strain. Finally, we propose a mechanism for ergothioneine utilization in Burkholderia sp. HME13. << Less
Biosci. Biotechnol. Biochem. 89:255-262(2025) [PubMed] [EuropePMC]