| Accepted Name |
|---|
| oxazoline synthase
|
| Alternative Name(s) |
|---|
| cyanobactin cyclodehydratase |
| cyanobactin heterocyclase |
| Reaction catalysed |
|---|
- ATP + L-amino acyl-L-seryl-[protein] <=> (S,S)-2-(C-substituted-aminomethyl)-4-acyl-2-oxazoline-[protein] + ADP + H(+) + phosphate
- ATP + L-amino acyl-L-threonyl-[protein] <=> (S,S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-2-oxazoline-[protein] + ADP + H(+) + phosphate
- 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 ribosomal
peptide natural products (RiPPs), converts L-cysteine, L-serine and
L-threonine residues to thiazoline, oxazoline, and methyloxazoline
rings, respectively.
- 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 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.
|
| Cross-references |
|---|
| BRENDA | 6.2.2.2 |
| EC2PDB | 6.2.2.2 |
| ExplorEnz | 6.2.2.2 |
| PRIAM enzyme-specific profiles | 6.2.2.2 |
| KEGG Ligand Database for Enzyme Nomenclature | 6.2.2.2 |
| IUBMB Enzyme Nomenclature | 6.2.2.2 |
| IntEnz | 6.2.2.2 |
| MEDLINE | Find literature relating to 6.2.2.2 |
| MetaCyc | 6.2.2.2 |
| Rhea expert-curated reactions | 6.2.2.2 |
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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.-.-.-
