| Accepted Name |
|---|
| thiazoline synthase
|
| Reaction catalysed |
|---|
| ATP + L-amino acyl-L-cysteinyl-[protein] = (1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline-[protein] + ADP + H(+) + phosphate |
| Comment(s) |
|---|
- 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 6.2.2.2.
- 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.
|
| Cross-references |
|---|
| BRENDA | 6.2.2.3 |
| EC2PDB | 6.2.2.3 |
| ExplorEnz | 6.2.2.3 |
| PRIAM enzyme-specific profiles | 6.2.2.3 |
| KEGG Ligand Database for Enzyme Nomenclature | 6.2.2.3 |
| IUBMB Enzyme Nomenclature | 6.2.2.3 |
| IntEnz | 6.2.2.3 |
| MEDLINE | Find literature relating to 6.2.2.3 |
| MetaCyc | 6.2.2.3 |
| Rhea expert-curated reactions | 6.2.2.3 |
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ENZYME /
UniProtKB/Swiss-Prot 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.-.-.-
