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Information on EC 6.2.1.70 - L-threonine-[L-threonyl-carrier protein] ligase

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.70 L-threonine-[L-threonyl-carrier protein] ligase
IUBMB Comments
The adenylation domain of the enzyme catalyses 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.
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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holo-[L-threonyl-carrier protein]
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L-threonyl-[L-threonyl-carrier protein]
Synonyms
syrb1, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(L-threonyl)adenylate + holo-[L-threonyl-carrier protein] = AMP + L-threonyl-[L-threonyl-carrier protein]
show the reaction diagram
(1b)
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ATP + L-threonine + holo-[L-threonyl-carrier protein] = AMP + diphosphate + L-threonyl-[L-threonyl-carrier protein]
show the reaction diagram
overall reaction
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ATP + L-threonine = diphosphate + (L-threonyl)adenylate
show the reaction diagram
(1a)
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PATHWAY SOURCE
PATHWAYS
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