Information 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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The expected taxonomic range for this enzyme is: Kutzneria sp. 744

EC NUMBER
COMMENTARY hide
1.14.11.B17
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
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
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
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SYSTEMATIC NAME
IUBMB Comments
S-(L-glutamyl)-[peptidyl-carrier protein of nonribosomal peptide synthetase KtzH],2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating, S-(threo-3-hydroxy-L-glutamyl)-[peptidyl-carrier-protein of nonribosomal peptide synthetase KtzH]-forming)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in the biosynthesis of L-threo-3-hydroxy-glutamate, prior to incorporation into kutznerides (antifungal nonribosomal hexadepsipeptides)
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
?
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
A8CF77
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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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
putative non-heme iron oxygenase, exhibit the conserved HXD/E_H iron(II)-binding motif, in the assay (NH4)2FeSO4 is used as source of the ferrous iron cofactor (0.5 mM)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Kutzneria sp. 744
A8CF77
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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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Kutzneria sp. 744
A8CF77
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
2
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40100
x * 40100, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40100, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overproduced in Escherichia coli as His7-tagged fusions