Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline D-ribitol 1-phosphate Identifier CHEBI:87817 Charge -2 Formula C5H11O8P InChIKeyhelp_outline VJDOAZKNBQCAGE-MROZADKFSA-L SMILEShelp_outline OC[C@H]([C@H]([C@H](COP(=O)([O-])[O-])O)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 (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 phosphate Identifier CHEBI:43474 Charge -2 Formula HO4P InChIKeyhelp_outline NBIIXXVUZAFLBC-UHFFFAOYSA-L SMILEShelp_outline OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 992 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ribitol Identifier CHEBI:15963 (Beilstein: 1720524; CAS: 488-81-3) help_outline Charge 0 Formula C5H12O5 InChIKeyhelp_outline HEBKCHPVOIAQTA-ZXFHETKHSA-N SMILEShelp_outline OC[C@H](O)[C@H](O)[C@H](O)CO 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:47652 | RHEA:47653 | RHEA:47654 | RHEA:47655 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Covalent docking predicts substrates for haloalkanoate dehalogenase superfamily phosphatases.
London N., Farelli J.D., Brown S.D., Liu C., Huang H., Korczynska M., Al-Obaidi N.F., Babbitt P.C., Almo S.C., Allen K.N., Shoichet B.K.
Enzyme function prediction remains an important open problem. Though structure-based modeling, such as metabolite docking, can identify substrates of some enzymes, it is ill-suited to reactions that progress through a covalent intermediate. Here we investigated the ability of covalent docking to i ... >> More
Enzyme function prediction remains an important open problem. Though structure-based modeling, such as metabolite docking, can identify substrates of some enzymes, it is ill-suited to reactions that progress through a covalent intermediate. Here we investigated the ability of covalent docking to identify substrates that pass through such a covalent intermediate, focusing particularly on the haloalkanoate dehalogenase superfamily. In retrospective assessments, covalent docking recapitulated substrate binding modes of known cocrystal structures and identified experimental substrates from a set of putative phosphorylated metabolites. In comparison, noncovalent docking of high-energy intermediates yielded nonproductive poses. In prospective predictions against seven enzymes, a substrate was identified for five. For one of those cases, a covalent docking prediction, confirmed by empirical screening, and combined with genomic context analysis, suggested the identity of the enzyme that catalyzes the orphan phosphatase reaction in the riboflavin biosynthetic pathway of Bacteroides. << Less
Biochemistry 54:528-537(2015) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.