Information on EC 1.14.11.57 - L-proline trans-4-hydroxylase

for references in articles please use BRENDA:EC1.14.11.57
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.11.57
-
RECOMMENDED NAME
GeneOntology No.
L-proline trans-4-hydroxylase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-proline + 2-oxoglutarate + O2 = trans-4-hydroxy-L-proline + succinate + CO2
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-proline,2-oxoglutarate:oxygen oxidoreductase (trans-4-hydroxylating)
Requires Fe2+ and ascorbate. The enzyme, isolated from multiple bacterial species, only produces trans-4-hydroxy-L-proline (cf. EC 1.14.11.56, L-proline cis-4-hydroxylase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-proline + 2-oxoglutarate + O2
trans-4-hydroxy-L-proline + succinate + CO2
show the reaction diagram
additional information
?
-
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
L-proline + 2-oxoglutarate + O2
trans-4-hydroxy-L-proline + succinate + CO2
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
about 10-15% of the activity with iron
Iron
-
strict requirements for ferrous ion and 2-oxoglutarate, maximum activity at 0.03 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
inhibitory above 0.5 mM
3,4-dihydroxybenzoate
-
-
Co2+
-
0.5 mM, complete inhibition
diethyl dicarbonate
-
complete inhibition. Inactivation can be partially prevented by the inclusion of L-proline and 2-oxoglutarate in the preincubation mixture
L-ascorbate
-
ascorbate causes a time-dependent inhibition of L-proline hydroxylation. The addition of ascorbate does not stimulate L-proline-coupled turnover of 2-oxoglutarate, but does stimulate L-proline-uncoupled turnover
Pyridine-2,4-dicarboxylate
-
competitive with respect to 2-oxoglutarate
Pyridine-2,5-dicarboxylate
-
-
Zn2+
-
0.5 mM, complete inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
catalase
-
presence of catalase causes 20-30% increase in the turnover of L-proline
-
pyridine-2,6-dicarboxylate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.032
2-oxoglutarate
-
pH 7.5, 35°C
0.445
L-proline
-
pH 7.5, 35°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.032
3,4-dihydroxybenzoate
Streptomyces griseoviridis
-
pH 7.5, 35°C
0.005
Pyridine-2,4-dicarboxylate
Streptomyces griseoviridis
-
pH 7.5, 35°C
0.049
Pyridine-2,5-dicarboxylate
Streptomyces griseoviridis
-
pH 7.5, 35°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
907
-
pH 7.5, 26°C
2080
-
pH 6.5, 35°C
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
-
gel filtration
38000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, about 30% loss of activity by freezing and thawing
-
4°C, 4-5 h, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-