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

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

Synonyms

KtzO

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
                1.14.11.B17 S-(L-glutamyl)-[peptidyl-carrier protein]-3-hydroxylase (3-hydroxylating, S-(threo-3-hydroxy-L-glutamyl)-[peptidyl-carrier-protein]-forming)

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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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
show the reaction diagram
additional information
?
-
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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