Enzymes
| UniProtKB help_outline | 1,483 proteins |
| Enzyme class help_outline |
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- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; 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 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N4-acetyl-2'-deoxycytidine Identifier CHEBI:146133 Charge 0 Formula C11H15N3O5 InChIKeyhelp_outline RWYFZABPLDFELM-QXFUBDJGSA-N SMILEShelp_outline O1[C@@H](N2C=CC(=NC2=O)NC(=O)C)C[C@H](O)[C@H]1CO 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 2'-deoxycytidine Identifier CHEBI:15698 (Beilstein: 87567; CAS: 951-77-9) help_outline Charge 0 Formula C9H13N3O4 InChIKeyhelp_outline CKTSBUTUHBMZGZ-SHYZEUOFSA-N SMILEShelp_outline Nc1ccn([C@H]2C[C@H](O)[C@@H](CO)O2)c(=O)n1 2D coordinates Mol file for the small molecule Search links Involved in 9 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline acetate Identifier CHEBI:30089 (Beilstein: 1901470; CAS: 71-50-1) help_outline Charge -1 Formula C2H3O2 InChIKeyhelp_outline QTBSBXVTEAMEQO-UHFFFAOYSA-M SMILEShelp_outline CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 174 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 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:62936 | RHEA:62937 | RHEA:62938 | RHEA:62939 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| EC numbers help_outline |
Publications
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YqfB protein from Escherichia coli: an atypical amidohydrolase active towards N4-acylcytosine derivatives.
Stanislauskiene R., Laurynenas A., Rutkiene R., Aucynaite A., Tauraite D., Meskiene R., Urbeliene N., Kaupinis A., Valius M., Kaliniene L., Meskys R.
Human activating signal cointegrator homology (ASCH) domain-containing proteins are widespread and diverse but, at present, the vast majority of those proteins have no function assigned to them. This study demonstrates that the 103-amino acid Escherichia coli protein YqfB, previously identified as ... >> More
Human activating signal cointegrator homology (ASCH) domain-containing proteins are widespread and diverse but, at present, the vast majority of those proteins have no function assigned to them. This study demonstrates that the 103-amino acid Escherichia coli protein YqfB, previously identified as hypothetical, is a unique ASCH domain-containing amidohydrolase responsible for the catabolism of N<sup>4</sup>-acetylcytidine (ac4C). YqfB has several interesting and unique features: i) it is the smallest monomeric amidohydrolase described to date, ii) it is active towards structurally different N<sup>4</sup>-acylated cytosines/cytidines, and iii) it has a high specificity for these substrates (k<sub>cat</sub>/K<sub>m</sub> up to 2.8 × 10<sup>6</sup> M<sup>-1</sup> s<sup>-1</sup>). Moreover, our results suggest that YqfB contains a unique Thr-Lys-Glu catalytic triad, and Arg acting as an oxyanion hole. The mutant lacking the yqfB gene retains the ability to grow, albeit poorly, on N<sup>4</sup>-acetylcytosine as a source of uracil, suggesting that an alternative route for the utilization of this compound exists in E. coli. Overall, YqfB ability to hydrolyse various N<sup>4</sup>-acylated cytosines and cytidines not only sheds light on the long-standing mystery of how ac4C is catabolized in bacteria, but also expands our knowledge of the structural diversity within the active sites of amidohydrolases. << Less
Sci. Rep. 10:788-788(2020) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.