BRENDA - Enzyme Database show
show all sequences of 1.14.11.28

Hydroxylation of L-proline to cis-3-hydroxy-L-proline by recombinant Escherichia coli expressing a synthetic L-proline-3-hydroxylase gene

Johnston, R.; Chu, L.; Liu, M.; Goldberg, S.; Goswami, A.; Patel, R.; Enzyme Microb. Technol. 45, 484-490 (2009)
No PubMed abstract available

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene P3H, DNA and amino acid sequence determination and analysis, preparation of a synthetic gene encoding proline 3-hydroxylase and cloning and overexpression of proline 3-hydroxylase protein in Escherichia coli strain BL21(DE3) resulting in strain SC16497, biotransformation rates, overview
Streptomyces sp.
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
activates, required
Streptomyces sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33154
-
x * 33154, sequence calculation
Streptomyces sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-proline + 2-oxoglutarate + O2
Streptomyces sp.
-
cis-3-hydroxy-L-proline + succinate + CO2
-
-
?
L-proline + 2-oxoglutarate + O2
Streptomyces sp. TH1
-
cis-3-hydroxy-L-proline + succinate + CO2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces sp.
-
-
-
Streptomyces sp. TH1
-
-
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
recombinant biotransformation of L-proline to cis-3-hydroxy-L-proline in Escherichia coli cells transformed with a synthetic P3H gene, overview
Streptomyces sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-proline + 2-oxoglutarate + O2
-
697667
Streptomyces sp.
cis-3-hydroxy-L-proline + succinate + CO2
-
-
-
?
L-proline + 2-oxoglutarate + O2
-
697667
Streptomyces sp.
cis-3-hydroxy-L-proline + succinate + CO2
product identification and analysis by NMR spectroscopy
-
-
?
L-proline + 2-oxoglutarate + O2
-
697667
Streptomyces sp. TH1
cis-3-hydroxy-L-proline + succinate + CO2
-
-
-
?
L-proline + 2-oxoglutarate + O2
-
697667
Streptomyces sp. TH1
cis-3-hydroxy-L-proline + succinate + CO2
product identification and analysis by NMR spectroscopy
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 33154, sequence calculation
Streptomyces sp.
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
28
30
assay at
Streptomyces sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
7.9
assay at
Streptomyces sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
gene P3H, DNA and amino acid sequence determination and analysis, preparation of a synthetic gene encoding proline 3-hydroxylase and cloning and overexpression of proline 3-hydroxylase protein in Escherichia coli strain BL21(DE3) resulting in strain SC16497, biotransformation rates, overview
Streptomyces sp.
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
activates, required
Streptomyces sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33154
-
x * 33154, sequence calculation
Streptomyces sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-proline + 2-oxoglutarate + O2
Streptomyces sp.
-
cis-3-hydroxy-L-proline + succinate + CO2
-
-
?
L-proline + 2-oxoglutarate + O2
Streptomyces sp. TH1
-
cis-3-hydroxy-L-proline + succinate + CO2
-
-
?
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
recombinant biotransformation of L-proline to cis-3-hydroxy-L-proline in Escherichia coli cells transformed with a synthetic P3H gene, overview
Streptomyces sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-proline + 2-oxoglutarate + O2
-
697667
Streptomyces sp.
cis-3-hydroxy-L-proline + succinate + CO2
-
-
-
?
L-proline + 2-oxoglutarate + O2
-
697667
Streptomyces sp.
cis-3-hydroxy-L-proline + succinate + CO2
product identification and analysis by NMR spectroscopy
-
-
?
L-proline + 2-oxoglutarate + O2
-
697667
Streptomyces sp. TH1
cis-3-hydroxy-L-proline + succinate + CO2
-
-
-
?
L-proline + 2-oxoglutarate + O2
-
697667
Streptomyces sp. TH1
cis-3-hydroxy-L-proline + succinate + CO2
product identification and analysis by NMR spectroscopy
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 33154, sequence calculation
Streptomyces sp.
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
28
30
assay at
Streptomyces sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
7.9
assay at
Streptomyces sp.
Other publictions for EC 1.14.11.28
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
727259
Hatzimichael
The collagen prolyl hydroxylas ...
Homo sapiens
Br. J. Cancer
107
1423-1432
2012
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
726654
Mordechai
High myopia caused by a mutati ...
Homo sapiens
Am. J. Hum. Genet.
89
438-445
2011
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
697017
Shah
The prolyl 3-hydroxylases P3H2 ...
Homo sapiens
Br. J. Cancer
100
1687-1696
2009
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
2
2
-
-
697667
Johnston
-
Hydroxylation of L-proline to ...
Streptomyces sp., Streptomyces sp. TH1
Enzyme Microb. Technol.
45
484-490
2009
-
-
1
-
-
-
-
-
-
1
1
2
-
7
-
-
-
-
-
-
1
-
4
1
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
1
2
-
-
-
-
-
-
1
-
4
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
665517
Vranka
Prolyl 3-hydroxylase 1, enzyme ...
Gallus gallus
J. Biol. Chem.
279
23615-23621
2004
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
664814
Clifton
Structure of proline 3-hydroxy ...
Streptomyces sp., Streptomyces sp. TH1
Eur. J. Biochem.
268
6625-6636
2001
-
-
-
1
-
-
-
-
-
-
-
2
-
8
-
-
1
-
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
664403
Shibasaki
-
Cloning of an isozyme of proli ...
Streptomyces sp., Streptomyces sp. TH1
Biotechnol. Lett.
22
1967-1973
2000
-
-
1
-
-
-
5
4
-
1
3
-
-
7
-
-
1
-
-
1
2
-
8
-
2
-
2
-
1
-
2
1
-
2
-
-
-
1
1
-
-
-
-
5
-
4
-
1
3
-
-
-
-
1
-
1
2
-
8
-
2
-
2
-
1
-
2
2
-
-
-
-
-
-
666959
Shibasaki
-
Substrate selectivities of pro ...
Streptomyces sp., Streptomyces sp. TH1
Tetrahedron Lett.
40
5227-5230
1999
-
-
1
-
-
-
-
6
-
-
-
-
-
7
-
-
1
-
-
1
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
1
-
1
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
665361
Mori
Purification and cloning of a ...
Streptomyces sp., Streptomyces sp. TH1
J. Bacteriol.
179
5677-5683
1997
1
-
-
-
-
-
5
2
-
1
1
-
-
10
-
-
1
-
-
1
-
-
2
-
1
-
-
1
1
-
-
1
-
1
-
1
-
-
1
-
-
-
-
5
-
2
-
1
1
-
-
-
-
1
-
1
-
-
2
-
1
-
-
1
1
-
-
1
-
-
-
-
-
-
663681
Mori
Detection of novel proline 3-h ...
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) TH2, Bacillus sp. (in: Bacteria) TH3, Streptomyces canus, Streptomyces sp., Streptomyces sp. TH1
Appl. Environ. Microbiol.
62
1903-1907
1996
-
-
-
-
-
-
4
-
-
3
-
-
-
16
-
-
-
-
-
3
4
-
6
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
-
-
-
4
-
-
-
3
-
-
-
-
-
-
-
3
4
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-