Information on EC 1.14.11.41 - L-arginine hydroxylase

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The expected taxonomic range for this enzyme is: Streptomyces

EC NUMBER
COMMENTARY hide
1.14.11.41
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RECOMMENDED NAME
GeneOntology No.
L-arginine hydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-arginine + 2-oxoglutarate + O2 = (3S)-3-hydroxy-L-arginine + succinate + CO2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ethylene biosynthesis II (microbes)
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NIL
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arginine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-arginine,2-oxoglutarate:O2 oxidoreductase (3-hydroxylating)
Fe2+-dependent enzyme. The enzyme is involved in the biosynthesis of the cyclic pentapeptide antibiotic viomycin. It differs from EC 1.14.11.34, 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming), because it does not form guanidine and (S)-1-pyrroline-5-carboxylate from 3-hydroxy-L-arginine.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-arginine + 2-oxoglutarate + O2
(3S)-3-hydroxy-L-arginine + succinate + CO2
show the reaction diagram
L-canavanine + 2-oxoglutarate + O2
? + succinate + CO2
show the reaction diagram
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?
L-homoarginine + 2-oxoglutarate + O2
(3S)-N6-(diaminomethylidene)-3-hydroxy-L-lysine + succinate + CO2
show the reaction diagram
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?
additional information
?
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no activity with D-arginine, NG-methyl-L-arginine, NG-hydroxynor-L-arginine
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
Fe2+-dependent enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.4
L-arginine
pH 8.0, 30C
1.16
L-canavanine
pH 8.0, 30C
7.05
L-homoarginine
pH 8.0, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
43.5
L-arginine
Streptomyces vinaceus
Q6WZB0
pH 8.0, 30C
1.22
L-canavanine
Streptomyces vinaceus
Q6WZB0
pH 8.0, 30C
13.85
L-homoarginine
Streptomyces vinaceus
Q6WZB0
pH 8.0, 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.8
L-arginine
Streptomyces vinaceus
Q6WZB0
pH 8.0, 30C
123
1.05
L-canavanine
Streptomyces vinaceus
Q6WZB0
pH 8.0, 30C
1143
1.96
L-homoarginine
Streptomyces vinaceus
Q6WZB0
pH 8.0, 30C
2084
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41600
x * 41600, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 41600, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor-diffusion method. The crystal structures of VioC are determined in complexes with the cofactor Fe(II), the substrate L-arginine, the product (2S,3S)-hydroxyarginine and the coproduct succinate at 1.11.3 A resolution
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a fusion protein with an N-terminal hexahistidine tag in Escherichia coli BL21(DE3)
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21
overexpression in Escherichia coli with an N-terminal hexahistidine affinity tag
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