Enzymes
| UniProtKB help_outline | 1 proteins |
Reaction participants Show >> << Hide
- Name help_outline (2E)-2-butenoate Identifier CHEBI:35899 Charge -1 Formula C4H5O2 InChIKeyhelp_outline LDHQCZJRKDOVOX-NSCUHMNNSA-M SMILEShelp_outline [H]\C(C)=C/C([O-])=O 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 ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,280 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
holo-[ACP]
Identifier
RHEA-COMP:9685
Reactive part
help_outline
- Name help_outline O-(pantetheine-4ʼ-phosphoryl)-L-serine residue Identifier CHEBI:64479 Charge -1 Formula C14H25N3O8PS SMILEShelp_outline C(NC(CCNC(=O)[C@@H](C(COP(OC[C@@H](C(*)=O)N*)(=O)[O-])(C)C)O)=O)CS 2D coordinates Mol file for the small molecule Search links Involved in 190 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
(2E)-butenoyl-[ACP]
Identifier
RHEA-COMP:9627
Reactive part
help_outline
- Name help_outline O-(S-2E-butenoylpantetheine-4ʼ-phosphoryl)-L-serine residue Identifier CHEBI:78453 Charge -1 Formula C18H29N3O9PS SMILEShelp_outline C\C=C\C(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP([O-])(=O)OC[C@H](N-*)C(-*)=O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline AMP Identifier CHEBI:456215 Charge -2 Formula C10H12N5O7P InChIKeyhelp_outline UDMBCSSLTHHNCD-KQYNXXCUSA-L SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 508 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline diphosphate Identifier CHEBI:33019 (Beilstein: 185088) help_outline Charge -3 Formula HO7P2 InChIKeyhelp_outline XPPKVPWEQAFLFU-UHFFFAOYSA-K SMILEShelp_outline OP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,129 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:74899 | RHEA:74900 | RHEA:74901 | RHEA:74902 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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| MetaCyc help_outline |
Related reactions help_outline
More general form(s) of this reaction
Publications
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Biosynthesis of isonitrile lipopeptides by conserved nonribosomal peptide synthetase gene clusters in Actinobacteria.
Harris N.C., Sato M., Herman N.A., Twigg F., Cai W., Liu J., Zhu X., Downey J., Khalaf R., Martin J., Koshino H., Zhang W.
A putative lipopeptide biosynthetic gene cluster is conserved in many species of Actinobacteria, including <i>Mycobacterium tuberculosis</i> and <i>M. marinum</i>, but the specific function of the encoding proteins has been elusive. Using both in vivo heterologous reconstitution and in vitro bioch ... >> More
A putative lipopeptide biosynthetic gene cluster is conserved in many species of Actinobacteria, including <i>Mycobacterium tuberculosis</i> and <i>M. marinum</i>, but the specific function of the encoding proteins has been elusive. Using both in vivo heterologous reconstitution and in vitro biochemical analyses, we have revealed that the five encoding biosynthetic enzymes are capable of synthesizing a family of isonitrile lipopeptides (INLPs) through a thio-template mechanism. The biosynthesis features the generation of isonitrile from a single precursor Gly promoted by a thioesterase and a nonheme iron(II)-dependent oxidase homolog and the acylation of both amino groups of Lys by the same isonitrile acyl chain facilitated by a single condensation domain of a nonribosomal peptide synthetase. In addition, the deletion of INLP biosynthetic genes in <i>M. marinum</i> has decreased the intracellular metal concentration, suggesting the role of this biosynthetic gene cluster in metal transport. << Less
Proc. Natl. Acad. Sci. U.S.A. 114:7025-7030(2017) [PubMed] [EuropePMC]
This publication is cited by 16 other entries.
Comments
Multi-step reaction: RHEA:74903 and RHEA:74907