Enzymes
| UniProtKB help_outline | 19 proteins |
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- Name help_outline 5-deoxy-α-D-ribose 1-phosphate Identifier CHEBI:58749 Charge -2 Formula C5H9O7P InChIKeyhelp_outline XXQFKXPJJNBLSU-TXICZTDVSA-L SMILEShelp_outline C[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 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 5-deoxy-D-ribulose 1-phosphate Identifier CHEBI:144504 Charge -2 Formula C5H9O7P InChIKeyhelp_outline AVEHMJVDRGMBHD-NQXXGFSBSA-L SMILEShelp_outline O[C@@H]([C@H](C(COP(=O)([O-])[O-])=O)O)C 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:61296 | RHEA:61297 | RHEA:61298 | RHEA:61299 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Salvage of the 5-deoxyribose byproduct of radical SAM enzymes.
Beaudoin G.A.W., Li Q., Folz J., Fiehn O., Goodsell J.L., Angerhofer A., Bruner S.D., Hanson A.D.
5-Deoxyribose is formed from 5'-deoxyadenosine, a toxic byproduct of radical S-adenosylmethionine (SAM) enzymes. The degradative fate of 5-deoxyribose is unknown. Here, we define a salvage pathway for 5-deoxyribose in bacteria, consisting of phosphorylation, isomerization, and aldol cleavage steps ... >> More
5-Deoxyribose is formed from 5'-deoxyadenosine, a toxic byproduct of radical S-adenosylmethionine (SAM) enzymes. The degradative fate of 5-deoxyribose is unknown. Here, we define a salvage pathway for 5-deoxyribose in bacteria, consisting of phosphorylation, isomerization, and aldol cleavage steps. Analysis of bacterial genomes uncovers widespread, unassigned three-gene clusters specifying a putative kinase, isomerase, and sugar phosphate aldolase. We show that the enzymes encoded by the Bacillus thuringiensis cluster, acting together in vitro, convert 5-deoxyribose successively to 5-deoxyribose 1-phosphate, 5-deoxyribulose 1-phosphate, and dihydroxyacetone phosphate plus acetaldehyde. Deleting the isomerase decreases the 5-deoxyribulose 1-phosphate pool size, and deleting either the isomerase or the aldolase increases susceptibility to 5-deoxyribose. The substrate preference of the aldolase is unique among family members, and the X-ray structure reveals an unusual manganese-dependent enzyme. This work defines a salvage pathway for 5-deoxyribose, a near-universal metabolite. << Less
Nat. Commun. 9:3105-3105(2018) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.