Enzymes
UniProtKB help_outline | 1 proteins |
Reaction participants Show >> << Hide
- Name help_outline guanosine Identifier CHEBI:16750 (CAS: 118-00-3) help_outline Charge 0 Formula C10H13N5O5 InChIKeyhelp_outline NYHBQMYGNKIUIF-UUOKFMHZSA-N SMILEShelp_outline Nc1nc2n(cnc2c(=O)[nH]1)[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 14 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 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline D-ribose Identifier CHEBI:47013 (Beilstein: 1904878; CAS: 50-69-1,613-83-2) help_outline Charge 0 Formula C5H10O5 InChIKeyhelp_outline HMFHBZSHGGEWLO-SOOFDHNKSA-N SMILEShelp_outline OC[C@H]1OC(O)[C@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 17 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline guanine Identifier CHEBI:16235 (CAS: 73-40-5) help_outline Charge 0 Formula C5H5N5O InChIKeyhelp_outline UYTPUPDQBNUYGX-UHFFFAOYSA-N SMILEShelp_outline C12=C(N=C(NC1=O)N)NC=N2 2D coordinates Mol file for the small molecule Search links Involved in 16 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:30771 | RHEA:30772 | RHEA:30773 | RHEA:30774 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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MetaCyc help_outline |
Related reactions help_outline
More general form(s) of this reaction
Publications
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Enzyme-substrate interactions in the purine-specific nucleoside hydrolase from Trypanosoma vivax.
Versees W., Decanniere K., Van Holsbeke E., Devroede N., Steyaert J.
Nucleoside hydrolases are key enzymes in the purine salvage pathway of Trypanosomatidae and are considered as targets for drug design. We previously reported the first x-ray structure of an inosine-adenosine-guanosine preferring nucleoside hydrolase (IAG-NH) from Trypanosoma vivax (). Here we repo ... >> More
Nucleoside hydrolases are key enzymes in the purine salvage pathway of Trypanosomatidae and are considered as targets for drug design. We previously reported the first x-ray structure of an inosine-adenosine-guanosine preferring nucleoside hydrolase (IAG-NH) from Trypanosoma vivax (). Here we report the 2.0-A crystal structure of the slow D10A mutant in complex with the inhibitor 3-deaza-adenosine and the 1.6-A crystal structure of the same enzyme in complex with a genuine substrate inosine. The enzyme-substrate complex shows the substrate bound to the enzyme in a different conformation from 3-deaza-adenosine and provides a snapshot along the reaction coordinate of the enzyme-catalyzed reaction. The chemical groups on the substrate important for binding and catalysis are mapped. The 2'-OH, 3'-OH, and 5'-OH contribute 4.6, 7.5, and 5.4 kcal/mol to k(cat)/K(m), respectively. Specific interactions with the exocyclic groups on the purine ring are not required for catalysis. Site-directed mutagenesis indicates that the purine specificity of the IAG-NHs is imposed by a parallel aromatic stacking interaction involving Trp(83) and Trp(260). The pH profiles of k(cat) and k(cat)/K(m) indicate the existence of one or more proton donors, possibly involved in leaving group activation. However, mutagenesis of the active site residues around the nucleoside base and an alanine scan of a flexible loop near the active site fail to identify this general acid. The parallel aromatic stacking seems to provide the most likely alternative mechanism for leaving group activation. << Less
J Biol Chem 277:15938-15946(2002) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.