ENZYME entry: EC 184.108.40.206
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|ATP + a [protein]-(L-amino acyl-L-cysteine) <=> ADP + phosphate + a [protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline|
- Requires Mg(2+).
- The enzyme, which participates in the biosynthesis of some ribosomal
peptide natural products (RiPPs) such as the trunkamides, converts
L-cysteine residues to thiazoline rings.
- The enzyme requires two domains - a cyclodehydratase domain, known as
a YcaO domain, and a substrate recognition domain (RRE domain) that
controls the regiospecificity of the enzyme.
- The RRE domain can either be fused to the YcaO domain or occur as a
separate protein; however both domains are required for activity.
- The enzyme can process multiple L-cysteine residues within the same
substrate peptide, and all enzymes characterized so far follow a
defined order, starting with the L-cysteine closest to the
- The reaction involves phosphorylation of the preceding ribosomal
peptide backbone amide bond, forming ADP and a phosphorylated
intermediate, followed by release of the phosphate group.
- In some cases the enzyme catalyzes a side reaction in which the
phosphorylated intermediate reacts with ADP to form AMP and
- This activity is also catalyzed by the related enzyme EC 220.127.116.11.
- That enzyme differs by having an RRE domain that also recognizes
L-serine and L-threonine residues, which are converted to oxazoline
and methyloxazoline rings, respectively.
|PRIAM enzyme-specific profiles||18.104.22.168|
|KEGG Ligand Database for Enzyme Nomenclature||22.214.171.124|
|IUBMB Enzyme Nomenclature||126.96.36.199|
|MEDLINE||Find literature relating to 188.8.131.52|
|Rhea expert-curated reactions||184.108.40.206|
entries corresponding to 6.2.2.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 6.2.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 6.-.-.-