EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
  1.14.11.B15 | more |
able to hydroxylate glutamic acid bound to a noncognate peptidyl-carrier-protein, e.g. the ninth peptidyl-carrier-protein domain of the CDA NRPS assembly line (CDA-T9). Nonhydrolyzable coenzyme A analogs are developed and used to determine the kinetic parameters for KtzP-catalyzed hydroxylation of glutamic acid bound to the carrier protein. To determine the kinetic parameters of KtzP catalyzed hydroxylation, the problem of the labile thioester bond is circumvented by using synthetic coenzyme A analogs coupled to glutamic acid where the thioester is replaced by a hydrolytically stable amide bond |
Kutzneria sp. 744 |
? |
- |
? |
| 1.14.11.B15 | S-(L-glutamyl)-[peptidyl-carrier protein of nonribosomal peptide synthetase KtzH] + 2-oxoglutarate + O2 |
the enzyme is involved in the biosynthesis of L-erythro-3-hydroxy-glutamate, a component of kutznerides (antifungal nonribosomal hexadepsipeptides) |
Kutzneria sp. 744 |
S-(erythro-3-hydroxy-L-glutamyl)-[peptidyl-carrier-protein of nonribosomal peptide synthetase KtzH] + succinate + CO2 |
- |
? |
| 1.14.11.B15 | S-(L-glutamyl)-[peptidyl-carrier protein of nonribosomal peptide synthetase KtzH] + 2-oxoglutarate + O2 |
D-Glu, L-Glu and [peptidyl-carrier-protein]-D-glutamyl thioester are not accepted as substrates. Proposed reaction mechanism: the stand-alone adenylation domain KtzN first activates L-glutamic acid as amino acyl adenylate, which then can be transferred site-specifically to the third peptidyl-carrier-protein domain of KtzH. The specificity of this interaction is mediated by the presence of the truncated A domain (A') as well as hydroxylase KtzP. Both A' and a hydroxylase KtzP are required for Glu-AMP transfer. Subsequently, the PCP-bound glutamic acid is hydroxylated by KtzP to afford L-erythro-3-hydroxyglutamic acid |
Kutzneria sp. 744 |
S-(erythro-3-hydroxy-L-glutamyl)-[peptidyl-carrier-protein of nonribosomal peptide synthetase KtzH] + succinate + CO2 |
- |
? |
