Enzymes
| UniProtKB help_outline | 1 proteins |
Reaction participants Show >> << Hide
- Name help_outline 3-oxocapnine Identifier CHEBI:231947 Charge 0 Formula C17H35NO4S InChIKeyhelp_outline ACSXFFQLIILPJM-INIZCTEOSA-N SMILEShelp_outline CC(CCCCCCCCCCCC([C@@H]([NH3+])CS(=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
- Name help_outline NADPH Identifier CHEBI:57783 (Beilstein: 10411862) help_outline Charge -4 Formula C21H26N7O17P3 InChIKeyhelp_outline ACFIXJIJDZMPPO-NNYOXOHSSA-J SMILEShelp_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](OP([O-])([O-])=O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,329 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 9,932 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline capnine Identifier CHEBI:231953 Charge 0 Formula C17H37NO4S InChIKeyhelp_outline XMTQSVIYISYLNK-BHWOMJMDSA-N SMILEShelp_outline CC(CCCCCCCCCCCC([C@@H]([NH3+])CS(=O)(=O)[O-])O)C 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 NADP+ Identifier CHEBI:58349 Charge -3 Formula C21H25N7O17P3 InChIKeyhelp_outline XJLXINKUBYWONI-NNYOXOHSSA-K SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](OP([O-])([O-])=O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,335 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:81575 | RHEA:81576 | RHEA:81577 | RHEA:81578 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Identification and Characterization of the Biosynthetic Pathway of the Sulfonolipid Capnine.
Liu Y., Wei Y., Teh T.M., Liu D., Zhou Y., Zhao S., Ang E.L., Zhao H., Zhang Y.
Capnine (2-amino-3-hydroxy-15-methylhexadecane-1-sulfonate) and capnoids (<i>N</i>-fatty acylated capnine derivatives) are sulfonolipids present in the outer membrane of gliding bacteria in the phylum Bacteroidetes and play a role in their unique gliding motility. They are structurally similar to ... >> More
Capnine (2-amino-3-hydroxy-15-methylhexadecane-1-sulfonate) and capnoids (<i>N</i>-fatty acylated capnine derivatives) are sulfonolipids present in the outer membrane of gliding bacteria in the phylum Bacteroidetes and play a role in their unique gliding motility. They are structurally similar to sphingolipids and are thought to be biosynthesized via a similar pathway. Here we report the identification and biochemical characterization of the capnine biosynthetic enzymes cysteate synthase (CapA) and cysteate-C-fatty acyltransferase (CapB) from the pathogenic gliding bacterium <i>Capnocytophaga ochracea</i> and NAD(P)H-dependent dehydrocapnine reductase CapC from the avian pathogen <i>Ornithobacterium rhinotracheale</i>. CapA catalyzes the formation of cysteate from <i>O</i>-phospho-l-serine and sulfite, and CapB catalyzes the formation of dehydrocapnine from cysteate and 13-methyl-myristoyl-CoA, followed by reduction by CapC. CapA is closely related to cystathionine-β-synthase but distantly related to the archaeal cysteate synthase. Close homologues of CapA, CapB, and the CapA isozyme archaeal cysteate synthase are present in many Bacteroidetes bacteria, including environmental, pathogenic, and human oral and intestinal microbiome bacteria, suggesting the widespread ability of these bacteria to biosynthesize capnine and related sulfonolipids. << Less
Biochemistry 61:2861-2869(2022) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.