Reaction participants Show >> << Hide
- Name help_outline a purine D-ribonucleoside Identifier CHEBI:142355 Charge 0 Formula C10H11N4O4R2 SMILEShelp_outline C1(=*)NC(=NC2=C1N=CN2[C@@H]3O[C@H](CO)[C@@H](O)[C@H]3O)* 2D coordinates Mol file for the small molecule Search links Involved in 59 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 1,002 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a purine nucleobase Identifier CHEBI:26386 Charge 0 Formula C5H3N4R2 SMILEShelp_outline C1(NC(=NC=2NC=NC12)*)=* 2D coordinates Mol file for the small molecule Search links Involved in 70 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline α-D-ribose 1-phosphate Identifier CHEBI:57720 (Beilstein: 6893776) help_outline Charge -2 Formula C5H9O8P InChIKeyhelp_outline YXJDFQJKERBOBM-TXICZTDVSA-L SMILEShelp_outline OC[C@H]1O[C@H](OP([O-])([O-])=O)[C@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 12 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:19805 | RHEA:19806 | RHEA:19807 | RHEA:19808 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
Specific form(s) of this reaction
Publications
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Purine nucleoside phosphorylase from human erythrocytes. IV. Crystallization and some properties.
Agarwal R.P., Parks R.E. Jr.
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Nontargeted in vitro metabolomics for high-throughput identification of novel enzymes in Escherichia coli.
Sevin D.C., Fuhrer T., Zamboni N., Sauer U.
Our understanding of metabolism is limited by a lack of knowledge about the functions of many enzymes. Here, we develop a high-throughput mass spectrometry approach to comprehensively profile proteins for in vitro enzymatic activity. Overexpressed or purified proteins are incubated in a supplement ... >> More
Our understanding of metabolism is limited by a lack of knowledge about the functions of many enzymes. Here, we develop a high-throughput mass spectrometry approach to comprehensively profile proteins for in vitro enzymatic activity. Overexpressed or purified proteins are incubated in a supplemented metabolome extract containing hundreds of biologically relevant candidate substrates, and accumulating and depleting metabolites are determined by nontargeted mass spectrometry. By combining chemometrics and database approaches, we established an automated pipeline for unbiased annotation of the functions of novel enzymes. In screening all 1,275 functionally uncharacterized Escherichia coli proteins, we discovered 241 potential novel enzymes, 12 of which we experimentally validated. Our high-throughput in vitro metabolomics method is generally applicable to any purified protein or crude cell lysate of its overexpression host and enables performing up to 1,200 nontargeted enzyme assays per working day. << Less
Nat. Methods 14:187-194(2017) [PubMed] [EuropePMC]
This publication is cited by 30 other entries.