Purification and cloning of a proline 3-hydroxylase, a novel enzyme which hydroxylates free L-proline to cis-3-hydroxy-L-proline

Mori, H.; Shibasaki, T.; Yano, K.; Ozaki, A.; J. Bacteriol. 179, 5677-5683 (1997)

Data extracted from this reference:

Activating Compound

Commentary

Organism

Structure

L-ascorbate

2 mM, no further stimulation above 2 mM

Streptomyces sp.

Inhibitors

Commentary

Organism

Structure

Citric acid

30% inhibition at 5 mM

Streptomyces sp.

Co2+

more than 90% inhibition at 1 mM

Streptomyces sp.

Cu2+

more than 90% inhibition at 1 mM

Streptomyces sp.

EDTA

95% inhibition at 2 mM

Streptomyces sp.

Zn2+

more than 90% inhibition at 1 mM

Streptomyces sp.

KM Value [mM]

KM Value Maximum [mM]

Substrate

Commentary

Organism

Structure

0.11

-

2-oxoglutarate

100 mM N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid pH 7.0, 5 mM 2-oxoglutarate, 5 mM L-proline, 5 mM L-ascorbate, 1 mM FeSO4, 35°C

Streptomyces sp.

0.56

-

L-proline

100 mM N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid pH 7.0, 5 mM 2-oxoglutarate, 5 mM L-proline, 5 mM L-ascorbate, 1 mM FeSO4, 35°C

Streptomyces sp.

Metals/Ions

Commentary

Organism

Structure

Fe2+

strictly required, optimal stimulation at 1 mM

Streptomyces sp.

Substrates

Commentary Substrates

Literature (Substrates)

Organism

Products

Commentary (Products)

Literature (Products)

Organism (Products)

Reversibility

Substrate Product ID

L-proline + 2-oxoglutarate + O2

-

665361

Streptomyces sp.

cis-3-hydroxy-L-proline + succinate + CO2

-

-

-

?

L-proline + 2-oxoglutarate + O2

-

665361

Streptomyces sp. TH1

cis-3-hydroxy-L-proline + succinate + CO2

-

-

-

?

Turnover Number Minimum [1/s]

Turnover Number Maximum [1/s]

Substrate

Commentary

Organism

Structure

3.2

-

L-proline

100 mM N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid pH 7.0, 5 mM 2-oxoglutarate, 5 mM L-proline, 5 mM L-ascorbate, 1 mM FeSO4, 35°C

Streptomyces sp.

Cofactor

Commentary

Organism

Structure

2-oxoglutarate

strictly required, highest activity at 4 mM

Streptomyces sp.

Activating Compound

Commentary

Organism

Structure

L-ascorbate

2 mM, no further stimulation above 2 mM

Streptomyces sp.

Cofactor

Commentary

Organism

Structure

2-oxoglutarate

strictly required, highest activity at 4 mM

Streptomyces sp.

Inhibitors

Commentary

Organism

Structure

Citric acid

30% inhibition at 5 mM

Streptomyces sp.

Co2+

more than 90% inhibition at 1 mM

Streptomyces sp.

Cu2+

more than 90% inhibition at 1 mM

Streptomyces sp.

EDTA

95% inhibition at 2 mM

Streptomyces sp.

Zn2+

more than 90% inhibition at 1 mM

Streptomyces sp.

KM Value [mM]

KM Value Maximum [mM]

Substrate

Commentary

Organism

Structure

0.11

-

2-oxoglutarate

100 mM N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid pH 7.0, 5 mM 2-oxoglutarate, 5 mM L-proline, 5 mM L-ascorbate, 1 mM FeSO4, 35°C

Streptomyces sp.

0.56

-

L-proline

100 mM N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid pH 7.0, 5 mM 2-oxoglutarate, 5 mM L-proline, 5 mM L-ascorbate, 1 mM FeSO4, 35°C

Streptomyces sp.

Metals/Ions

Commentary

Organism

Structure

Fe2+

strictly required, optimal stimulation at 1 mM

Streptomyces sp.

Substrates

Commentary Substrates

Literature (Substrates)

Organism

Products

Commentary (Products)

Literature (Products)

Organism (Products)

Reversibility

ID

L-proline + 2-oxoglutarate + O2

-

665361

Streptomyces sp.

cis-3-hydroxy-L-proline + succinate + CO2

-

-

-

?

L-proline + 2-oxoglutarate + O2

-

665361

Streptomyces sp. TH1

cis-3-hydroxy-L-proline + succinate + CO2

-

-

-

?

Turnover Number Minimum [1/s]

Turnover Number Maximum [1/s]

Substrate

Commentary

Organism

Structure

3.2

-

L-proline

100 mM N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid pH 7.0, 5 mM 2-oxoglutarate, 5 mM L-proline, 5 mM L-ascorbate, 1 mM FeSO4, 35°C

Streptomyces sp.

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

Synonyms

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

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1

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1

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-

726654

Mordechai

High myopia caused by a mutati ...

Homo sapiens

Am. J. Hum. Genet.

89

438-445

2011

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1

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697017

Shah

The prolyl 3-hydroxylases P3H2 ...

Homo sapiens

Br. J. Cancer

100

1687-1696

2009

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1

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1

1

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2

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697667

Johnston

-

Hydroxylation of L-proline to ...

Streptomyces sp., Streptomyces sp. TH1

Enzyme Microb. Technol.

45

484-490

2009

-

-

1

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1

1

2

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7

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1

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665517

Vranka

Prolyl 3-hydroxylase 1, enzyme ...

Gallus gallus

J. Biol. Chem.

279

23615-23621

2004

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664814

Clifton

Structure of proline 3-hydroxy ...

Streptomyces sp., Streptomyces sp. TH1

Eur. J. Biochem.

268

6625-6636

2001

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664403

Shibasaki

-

Cloning of an isozyme of proli ...

Streptomyces sp., Streptomyces sp. TH1

Biotechnol. Lett.

22

1967-1973

2000

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1

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5

4

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7

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8

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2

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1

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2

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666959

Shibasaki

-

Substrate selectivities of pro ...

Streptomyces sp., Streptomyces sp. TH1

Tetrahedron Lett.

40

5227-5230

1999

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1

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6

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665361

Mori

Purification and cloning of a ...

Streptomyces sp., Streptomyces sp. TH1

J. Bacteriol.

179

5677-5683

1997

1

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5

2

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1

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11

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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

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4

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16

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