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ENZYME entry: EC

Accepted Name
Thiazoline synthase.
Reaction catalysed
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 C-terminus.
  • 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 diphosphate.
  • This activity is also catalyzed by the related enzyme EC
  • 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 profiles6.2.2.3
KEGG Ligand Database for Enzyme Nomenclature6.2.2.3
IUBMB Enzyme Nomenclature6.2.2.3
MEDLINEFind literature relating to
Rhea expert-curated reactions6.2.2.3

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