1.14.11.B17: S-(L-glutamyl)-[peptidyl-carrier protein]-3-hydroxylase (3-hydroxylating, S-(threo-3-hydroxy-L-glutamyl)-[peptidyl-carrier-protein]-forming)
This is an abbreviated version!
For detailed information about S-(L-glutamyl)-[peptidyl-carrier protein]-3-hydroxylase (3-hydroxylating, S-(threo-3-hydroxy-L-glutamyl)-[peptidyl-carrier-protein]-forming), go to the full flat file.
Reaction
Synonyms
KtzO
ECTree
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Substrates Products
Substrates Products on EC 1.14.11.B17 - S-(L-glutamyl)-[peptidyl-carrier protein]-3-hydroxylase (3-hydroxylating, S-(threo-3-hydroxy-L-glutamyl)-[peptidyl-carrier-protein]-forming)
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REACTION DIAGRAM
S-(L-glutamyl)-[peptidyl-carrier protein of nonribosomal peptide synthetase KtzH] + 2-oxoglutarate + O2
S-(threo-3-hydroxy-L-glutamyl)-[peptidyl-carrier-protein of nonribosomal peptide synthetase KtzH] + succinate + CO2
additional information
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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 KtzO-catalyzed hydroxylation of glutamic acid bound to the carrier protein. To determine the kinetic parameters of KtzO 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
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S-(L-glutamyl)-[peptidyl-carrier protein of nonribosomal peptide synthetase KtzH] + 2-oxoglutarate + O2
S-(threo-3-hydroxy-L-glutamyl)-[peptidyl-carrier-protein of nonribosomal peptide synthetase KtzH] + succinate + CO2
the enzyme is involved in the biosynthesis of L-threo-3-hydroxy-glutamate, prior to incorporation into kutznerides (antifungal nonribosomal hexadepsipeptides)
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S-(L-glutamyl)-[peptidyl-carrier protein of nonribosomal peptide synthetase KtzH] + 2-oxoglutarate + O2
S-(threo-3-hydroxy-L-glutamyl)-[peptidyl-carrier-protein of nonribosomal peptide synthetase KtzH] + succinate + CO2
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 KtzO. Both A* and a hydroxylase KtzO are required for Glu-AMP transfer. Subsequently, the PCP-bound glutamic acid is hydroxylated by KtzO to afford L-threo-3-hydroxyglutamic acid
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