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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
BRENDA6.2.1.70
EC2PDB6.2.1.70
ExplorEnz6.2.1.70
PRIAM enzyme-specific profiles6.2.1.70
KEGG Ligand Database for Enzyme Nomenclature6.2.1.70
IUBMB Enzyme Nomenclature6.2.1.70
IntEnz6.2.1.70
MEDLINEFind literature relating to 6.2.1.70
MetaCyc6.2.1.70
Rhea expert-curated reactions6.2.1.70
UniProtKB/Swiss-Prot
P45745, DHBF_BACSU;  Q1IAL0, PMSD_PSEE4;  Q52400, SYRB1_PSESY;  

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