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Enzyme Nomenclature
Information on EC 1.14.11.45 - L-isoleucine 4-hydroxylase
Word Map on EC 1.14.11.45
- 1.14.11.45
-
stereoselective
- thuringiensis
-
4-hydroxyisoleucine
- l-ethionine
-
biocatalyst
-
sulfoxidation
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.11.45
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RECOMMENDED NAME
GeneOntology No.
L-isoleucine 4-hydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-isoleucine + 2-oxoglutarate + O2 = (4S)-4-hydroxy-L-isoleucine + succinate + CO2
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dehydrogenation
hydroxylation
sulfoxidation
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SYSTEMATIC NAME
IUBMB Comments
L-isoleucine,2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating)
The enzyme, characterized from the bacterium Bacillus thuringiensis, can also catalyse the hydroxylation of L-leucine, L-norvaline, L-norleucine, and L-allo-isoleucine, as well as the sulfoxidation of L-methionine, L-ethionine, S-methyl-L-cysteine, S-ethyl-L-cysteine, and S-allyl-L-cysteine.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S,3R,4S)-4-hydroxy-L-isoleucine + 2-oxoglutarate + O2
(2S,3R)-2-amino-3-methyl-4-ketopentanoate + succinate + CO2
(S)-allyl-L-cysteine + 2-oxoglutarate + O2
S-allyl-L-cysteine (S)-sulfoxide + succinate + CO2
(S)-ethyl-L-cysteine + 2-oxoglutarate + O2
S-ethyl-L-cysteine (S)-sulfoxide + succinate + CO2
(S)-methyl-L-cysteine + 2-oxoglutarate + O2
S-methyl-L-cysteine (S)-sulfoxide + succinate + CO2
L-allo-isoleucine + 2-oxoglutarate + O2
(S)-3-hydroxy-L-allo-isoleucine + succinate + CO2
-
-
-
-
?
L-ethionine + 2-oxoglutarate + O2
L-ethionine sulfoxide + succinate + CO2
-
-
-
-
?
L-leucine + 2-oxoglutarate + O2
4-hydroxy-L-leucine + succinate + CO2
-
-
-
-
?
L-methionine + 2-oxoglutarate + O2
L-methionine (S)-sulfoxide + succinate + CO2
-
-
-
-
?
L-methionine + 2-oxoglutarate + O2
L-methionine sulfoxide + succinate + CO2
-
-
-
-
?
L-norleucine + 2-oxoglutarate + O2
4-hydroxy-L-norleucine + succinate + CO2
-
-
-
-
?
L-norvaline + 2-oxoglutarate + O2
(S)-4-hydroxy-L-norvaline + succinate + CO2
-
-
-
-
?
(2S,3R,4S)-4-hydroxy-L-isoleucine + 2-oxoglutarate + O2
(2S,3R)-2-amino-3-methyl-4-ketopentanoate + succinate + CO2
-
-
-
-
?
(2S,3R,4S)-4-hydroxy-L-isoleucine + 2-oxoglutarate + O2
(2S,3R)-2-amino-3-methyl-4-ketopentanoate + succinate + CO2
-
-
-
-
?
(S)-allyl-L-cysteine + 2-oxoglutarate + O2
S-allyl-L-cysteine (S)-sulfoxide + succinate + CO2
-
-
-
-
?
(S)-allyl-L-cysteine + 2-oxoglutarate + O2
S-allyl-L-cysteine (S)-sulfoxide + succinate + CO2
-
-
-
-
?
(S)-ethyl-L-cysteine + 2-oxoglutarate + O2
S-ethyl-L-cysteine (S)-sulfoxide + succinate + CO2
-
-
-
-
?
(S)-ethyl-L-cysteine + 2-oxoglutarate + O2
S-ethyl-L-cysteine (S)-sulfoxide + succinate + CO2
-
-
-
-
?
(S)-methyl-L-cysteine + 2-oxoglutarate + O2
S-methyl-L-cysteine (S)-sulfoxide + succinate + CO2
-
-
-
-
?
(S)-methyl-L-cysteine + 2-oxoglutarate + O2
S-methyl-L-cysteine (S)-sulfoxide + succinate + CO2
-
-
-
-
?
L-ethionine + 2-oxoglutarate + O2
L-ethionine (S)-sulfoxide + succinate + CO2
-
-
-
-
?
L-ethionine + 2-oxoglutarate + O2
L-ethionine (S)-sulfoxide + succinate + CO2
-
-
-
-
?
L-isoleucine + 2-oxoglutarate + O2
(2S,3R,4S)-4-hydroxy-isoleucine + succinate + CO2
-
-
-
-
?
L-isoleucine + 2-oxoglutarate + O2
(2S,3R,4S)-4-hydroxy-isoleucine + succinate + CO2
-
-
-
-
?
L-isoleucine + 2-oxoglutarate + O2
(2S,3R,4S)-4-hydroxy-L-isoleucine + succinate + CO2
-
-
-
-
?
L-isoleucine + 2-oxoglutarate + O2
(2S,3R,4S)-4-hydroxy-L-isoleucine + succinate + CO2
-
best substrate
-
-
?
L-isoleucine + 2-oxoglutarate + O2
(2S,3R,4S)-4-hydroxy-L-isoleucine + succinate + CO2
-
best substrate
-
-
?
L-isoleucine + 2-oxoglutarate + O2
(2S,3R,4S)-4-hydroxy-L-isoleucine + succinate + CO2
-
-
-
-
?
L-isoleucine + 2-oxoglutarate + O2
(4S)-4-hydroxy-L-isoleucine + succinate + CO2
-
-
-
?
L-isoleucine + 2-oxoglutarate + O2
(4S)-4-hydroxy-L-isoleucine + succinate + CO2
-
-
-
?
L-isoleucine + 2-oxoglutarate + O2
N,N-dihydroxy-L-isoleucine + succinate + CO2
-
-
-
-
?
L-isoleucine + 2-oxoglutarate + O2
N,N-dihydroxy-L-isoleucine + succinate + CO2
-
-
-
-
?
additional information
?
-
-
the enzyme does not react with D-Ile, D-allo-Ile, tert-butoxycarbonyl-L-Ile, 9-fluorenylmethoxycarbonyl-L-Ile,N-carbamoyl-L-Ile, L-Ile methyl ester, and N-acetyl-L-Ile methyl ester
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-
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additional information
?
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no activity with L-threonine
-
-
-
additional information
?
-
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the enzyme does not react with D-Ile, D-allo-Ile, tert-butoxycarbonyl-L-Ile, 9-fluorenylmethoxycarbonyl-L-Ile,N-carbamoyl-L-Ile, L-Ile methyl ester, and N-acetyl-L-Ile methyl ester
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-
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additional information
?
-
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L-isoleucine, 2-oxoglutarate: oxygen oxidoreductase HilA and L-isoleucine-4'-dioxygenase HilB catalyze the consecutive hydroxylation of L-isoleucine at the C-4' and C-4 positions, respectively, to synthesize L-4',4-dihydroxyisoleucine. When expressed without HilA, HilB acts as a minimally effective L-isoleucine-4-dioxygenase
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-
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additional information
?
-
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L-isoleucine, 2-oxoglutarate: oxygen oxidoreductase HilA and L-isoleucine-4'-dioxygenase HilB catalyze the consecutive hydroxylation of L-isoleucine at the C-4' and C-4 positions, respectively, to synthesize L-4',4-dihydroxyisoleucine. When expressed without HilA, HilB acts as a minimally effective L-isoleucine-4-dioxygenase
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S,3R,4S)-4-hydroxy-L-isoleucine + 2-oxoglutarate + O2
(2S,3R)-2-amino-3-methyl-4-ketopentanoate + succinate + CO2
(2S,3R,4S)-4-hydroxy-L-isoleucine + 2-oxoglutarate + O2
(2S,3R)-2-amino-3-methyl-4-ketopentanoate + succinate + CO2
-
-
-
-
?
(2S,3R,4S)-4-hydroxy-L-isoleucine + 2-oxoglutarate + O2
(2S,3R)-2-amino-3-methyl-4-ketopentanoate + succinate + CO2
-
-
-
-
?
L-isoleucine + 2-oxoglutarate + O2
(2S,3R,4S)-4-hydroxy-isoleucine + succinate + CO2
-
-
-
-
?
L-isoleucine + 2-oxoglutarate + O2
(2S,3R,4S)-4-hydroxy-isoleucine + succinate + CO2
-
-
-
-
?
L-isoleucine + 2-oxoglutarate + O2
(2S,3R,4S)-4-hydroxy-L-isoleucine + succinate + CO2
-
-
-
-
?
L-isoleucine + 2-oxoglutarate + O2
(2S,3R,4S)-4-hydroxy-L-isoleucine + succinate + CO2
-
best substrate
-
-
?
L-isoleucine + 2-oxoglutarate + O2
(2S,3R,4S)-4-hydroxy-L-isoleucine + succinate + CO2
-
best substrate
-
-
?
L-isoleucine + 2-oxoglutarate + O2
(2S,3R,4S)-4-hydroxy-L-isoleucine + succinate + CO2
-
-
-
-
?
L-isoleucine + 2-oxoglutarate + O2
(4S)-4-hydroxy-L-isoleucine + succinate + CO2
E2GIN1
-
-
-
?
L-isoleucine + 2-oxoglutarate + O2
(4S)-4-hydroxy-L-isoleucine + succinate + CO2
E2GIN1
-
-
-
?
L-isoleucine + 2-oxoglutarate + O2
N,N-dihydroxy-L-isoleucine + succinate + CO2
-
-
-
-
?
L-isoleucine + 2-oxoglutarate + O2
N,N-dihydroxy-L-isoleucine + succinate + CO2
-
-
-
-
?
additional information
?
-
-
L-isoleucine, 2-oxoglutarate: oxygen oxidoreductase HilA and L-isoleucine-4'-dioxygenase HilB catalyze the consecutive hydroxylation of L-isoleucine at the C-4' and C-4 positions, respectively, to synthesize L-4',4-dihydroxyisoleucine. When expressed without HilA, HilB acts as a minimally effective L-isoleucine-4-dioxygenase
-
-
-
additional information
?
-
-
L-isoleucine, 2-oxoglutarate: oxygen oxidoreductase HilA and L-isoleucine-4'-dioxygenase HilB catalyze the consecutive hydroxylation of L-isoleucine at the C-4' and C-4 positions, respectively, to synthesize L-4',4-dihydroxyisoleucine. When expressed without HilA, HilB acts as a minimally effective L-isoleucine-4-dioxygenase
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-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbic acid
-
ascorbic acid is not necessarily required for the reaction, however, in the presence of ascorbic acid, the reaction rate is greatly stimulated
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
-
the enzyme retains over 90% activity after 1 h of incubation at pH 7.0-9.0
730987
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 28
-
the enzyme retains over 80% of its activity after 1 h incubation at 20-28°C
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HiPrep DEAE column chromatography, Mono S column chromatography, Resource PHE column chromatography, and Superdex 75 gel filtration
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.11.45)
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