ENZYME entry: EC 6.2.1.70
Accepted Name |
L-threonine--[L-threonyl-carrier protein] ligase.
|
Reaction catalysed |
ATP + holo-[peptidyl-carrier protein] + L-threonine <=> AMP + diphosphate + L-threonyl-[peptidyl-carrier protein] |
Comment(s) |
- The adenylation domain of the enzyme catalyzes the activation of
L-threonine to (L-threonyl)adenylate, followed by the transfer of the
activated compound to the free thiol of a phosphopantetheine arm of a
peptidyl-carrier protein domain.
- The peptidyl-carrier protein domain may be part of the same protein
(as in the case of DhbF in bacillibactin biosynthesis), or of a
different protein (as in the case of PmsD in pseudomonine
biosynthesis).
- This activity is often found as part of a larger non-ribosomal
peptide synthase.
|
Cross-references |
BRENDA | 6.2.1.70 |
EC2PDB | 6.2.1.70 |
ExplorEnz | 6.2.1.70 |
PRIAM enzyme-specific profiles | 6.2.1.70 |
KEGG Ligand Database for Enzyme Nomenclature | 6.2.1.70 |
IUBMB Enzyme Nomenclature | 6.2.1.70 |
IntEnz | 6.2.1.70 |
MEDLINE | Find literature relating to 6.2.1.70 |
MetaCyc | 6.2.1.70 |
Rhea expert-curated reactions | 6.2.1.70 |
UniProtKB/Swiss-Prot |
|
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