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Your query returned 1 entry. 
Printable version
| EC | 6.2.1.70 | ||||
| Accepted name: | L-threonine—[L-threonyl-carrier protein] ligase | ||||
| Reaction: | ATP + L-threonine + holo-[L-threonyl-carrier protein] = AMP + diphosphate + L-threonyl-[L-threonyl-carrier protein] (overall reaction) (1a) ATP + L-threonine = diphosphate + (L-threonyl)adenylate (1b) (L-threonyl)adenylate + holo-[L-threonyl-carrier protein] = AMP + L-threonyl-[L-threonyl-carrier protein] |
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| Other name(s): | dhbF (gene name); pmsD (gene name); syrB1 (gene name) | ||||
| Systematic name: | L-threonine:[L-threonyl-carrier protein] ligase (AMP-forming) | ||||
| 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. | ||||
| Links to other databases: | BRENDA, EXPASY, Gene, KEGG, MetaCyc | ||||
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