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Enzyme Nomenclature
Information on EC 1.14.11.B3 - L-proline cis-4-hydroxylase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.11.B3
preliminary BRENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
L-proline cis-4-hydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-proline + 2-oxoglutarate + O2 = cis-4-hydroxy-L-proline + succinate + CO2
reaction mechanism
L-proline + 2-oxoglutarate + O2 = cis-4-hydroxy-L-proline + succinate + CO2
reaction mechanism
L-proline + 2-oxoglutarate + O2 = cis-4-hydroxy-L-proline + succinate + CO2
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SYSTEMATIC NAME
IUBMB Comments
L-proline,2-oxoglutarate:oxygen oxidoreductase (4-cis-hydroxylating)
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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
L-proline + 2-oxoglutarate + O2
cis-4-hydroxy-L-proline + succinate + CO2
the enzyme reacts in a regio- and stereoselective manner
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-
?
L-proline + 2-oxoglutarate + O2
cis-4-hydroxy-L-proline + succinate + CO2
the enzyme reacts in a regio- and stereoselective manner
cis-4-hydroxy-L-proline is clinically evaluated as an anticancer drug
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?
L-proline + 2-oxoglutarate + O2
cis-4-hydroxy-L-proline + succinate + CO2
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-
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-
?
L-proline + 2-oxoglutarate + O2
cis-4-hydroxy-L-proline + succinate + CO2
the enzyme reacts in a regio- and stereoselective manner
cis-4-hydroxy-L-proline is clinically evaluated as an anticancer drug
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?
additional information
?
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the enzymes possess a His-1 motif consisting of histidine-X-aspartate and a basic amino acid residue, lysine or arginine, serving as a 2-oxoglutarate C-5 stabilizator
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additional information
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the enzymes possess a His-1 motif consisting of histidine-X-aspartate and a basic amino acid residue, lysine or arginine, serving as a 2-oxoglutarate C-5 stabilizator
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additional information
?
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the enzymes possess a His-1 motif consisting of histidine-X-aspartate and a basic amino acid residue, lysine or arginine, serving as a 2-oxoglutarate C-5 stabilizator
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-
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additional information
?
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the enzymes possess a His-1 motif consisting of histidine-X-aspartate and a basic amino acid residue, lysine or arginine, serving as a 2-oxoglutarate C-5 stabilizator
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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
L-proline + 2-oxoglutarate + O2
cis-4-hydroxy-L-proline + succinate + CO2
Q989T9
the enzyme reacts in a regio- and stereoselective manner
cis-4-hydroxy-L-proline is clinically evaluated as an anticancer drug
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?
L-proline + 2-oxoglutarate + O2
cis-4-hydroxy-L-proline + succinate + CO2
Q92LF6
the enzyme reacts in a regio- and stereoselective manner
cis-4-hydroxy-L-proline is clinically evaluated as an anticancer drug
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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
additional information
no inhibition by hydroxylamine, Mg2+, Mn2+, and Fe3+ at 2 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbic acid
stimulates, but is not necessarily required for the reaction
ascorbic acid
stimulates, but is not necessarily required for the reaction
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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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
6 - 8
pH 6.0: about 60% of maximal activity, pH 8.0: about 55% of maximal activity
6 - 8
pH 6.0: about 30% of maximal activity, pH 6.5: about 80% of maximal activity, about 40% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 35
15 - 35
15°C: about 70% of maximal activity, 35°C: about 60% of maximal activity
15 - 35
15°C: about 90% of maximal activity, 30°C: about 75% of maximal activity, 50°C: about 30% of maximal activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli by affinity chromatography
recombinant enzyme from Escherichia coli by affinity chromatography
recombinant enzyme from Escherichia coli by affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene MlP4H, DNA and amino acid sequence determination, analysis and comparison, expression in Escherichia coli JM109
gene SmP4H, DNA and amino acid sequence determination, analysis and comparison, expression in Escherichia coli JM109
in order to develop a microbial production system for N-acetyl CHOP from L-proline, a coexpression plasmid harboring the genes encoding SmP4H and Mpr1 from Sinorhizobium meliloti and Saccharomyces cerevisiae, respectively is constructed, and introduced into Escherichia coli BL21 DELTAputA strain in which the L-proline degradation pathway is blocked
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
the enzyme is used for industrial production of cis-4-hydroxy-L-proline. cis-4-Hydroxy-L-proline is clinically evaluated as an anticancer drug
synthesis
the enzyme is used for industrial production of cis-4-hydroxy-L-proline. cis-4-Hydroxy-L-proline is clinically evaluated as an anticancer drug
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.11.B3)
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