Information on EC 1.14.11.41 - L-arginine hydroxylase

for references in articles please use BRENDA:EC1.14.11.41
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The expected taxonomic range for this enzyme is: Streptomyces

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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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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.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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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
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.4
L-arginine
pH 8.0, 30°C
1.16
L-canavanine
pH 8.0, 30°C
7.05
L-homoarginine
pH 8.0, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
43.5
L-arginine
pH 8.0, 30°C
1.22
L-canavanine
pH 8.0, 30°C
13.85
L-homoarginine
pH 8.0, 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.8
L-arginine
pH 8.0, 30°C
1.05
L-canavanine
pH 8.0, 30°C
1.96
L-homoarginine
pH 8.0, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41600
x * 41600, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 41600, SDS-PAGE
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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 1.1–1.3 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a fusion protein with an N-terminal hexahistidine tag in Escherichia coli BL21(DE3)
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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.11.41)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)