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show all sequences of 1.1.1.237

Structure and substrate docking of a hydroxy(phenyl)pyruvate reductase from the higher plant Coleus blumei Benth

Janiak, V.; Petersen, M.; Zentgraf, M.; Klebe, G.; Heine, A.; Acta Crystallogr. Sect. D 66, 593-603 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS
Solenostemon scutellarioides
Crystallization (Commentary)
Crystallization
Organism
apoenzyme and enzyme in complex with NADP+, sitting drop vapour diffusion method, mixing of 0.001 ml of 6 mg/ml protein or 15 mg/ml protein with 2 mM NADP+ in 50 mM Tris-HCl, pH 7.0, with 0.001 ml of well solution containing 30% 2-methyl-2,4-pentanediol, 0.2 M NaCl, 0.1 M Tris-HCl, pH 7.5 at 4°C, or 20% PEG 1000, 0.1 M imidazole, pH 7.5, 4 mM 4-hydroxyphenylpyruvate, 0.2 mM DTT at 26°C, leading to one-crystal clusters or tetragonal bipyramid-shaped crystals, X-ray diffraction structure determination and analysis at 1.47 A and 2.2 A, respectively, modeling
Solenostemon scutellarioides
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34113
-
2 * 34113, sequence calculation and crystal structure
Solenostemon scutellarioides
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
Solenostemon scutellarioides
-
3-(4-hydroxyphenyl)lactate + NADP+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Solenostemon scutellarioides
Q65CJ7
-
-
Purification (Commentary)
Commentary
Organism
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity and 2',5'-ADP affinity chromatography and dialysis
Solenostemon scutellarioides
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cell suspension culture
-
Solenostemon scutellarioides
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3,4-dihydroxyphenylpyruvate + NADH + H+
-
723825
Solenostemon scutellarioides
3-(3,4-dihydroxyphenyl)lactate + NAD+
-
-
-
r
3,4-dihydroxyphenylpyruvate + NADPH + H+
-
723825
Solenostemon scutellarioides
3-(3,4-dihydroxyphenyl)lactate + NADP+
-
-
-
r
3-(4-hydroxyphenyl)pyruvate + NADH + H+
-
723825
Solenostemon scutellarioides
3-(4-hydroxyphenyl)lactate + NAD+
-
-
-
r
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
-
723825
Solenostemon scutellarioides
3-(4-hydroxyphenyl)lactate + NADP+
-
-
-
?
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
substrate bindiing structure, docking study, overview
723825
Solenostemon scutellarioides
3-(4-hydroxyphenyl)lactate + NADP+
-
-
-
r
Subunits
Subunits
Commentary
Organism
homodimer
2 * 34113, sequence calculation and crystal structure
Solenostemon scutellarioides
More
molecular docking study, overview
Solenostemon scutellarioides
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
NADH as well as NADPH can serve as the electron donor
Solenostemon scutellarioides
NADP+
-
Solenostemon scutellarioides
NADPH
preferred cofactor compared to NAD+, forms three hydrogen bonds to the protein via N41 to Asp256 OD2 and Ile230 O and O40 to His279 NE2
Solenostemon scutellarioides
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS
Solenostemon scutellarioides
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
NADH as well as NADPH can serve as the electron donor
Solenostemon scutellarioides
NADP+
-
Solenostemon scutellarioides
NADPH
preferred cofactor compared to NAD+, forms three hydrogen bonds to the protein via N41 to Asp256 OD2 and Ile230 O and O40 to His279 NE2
Solenostemon scutellarioides
Crystallization (Commentary) (protein specific)
Crystallization
Organism
apoenzyme and enzyme in complex with NADP+, sitting drop vapour diffusion method, mixing of 0.001 ml of 6 mg/ml protein or 15 mg/ml protein with 2 mM NADP+ in 50 mM Tris-HCl, pH 7.0, with 0.001 ml of well solution containing 30% 2-methyl-2,4-pentanediol, 0.2 M NaCl, 0.1 M Tris-HCl, pH 7.5 at 4°C, or 20% PEG 1000, 0.1 M imidazole, pH 7.5, 4 mM 4-hydroxyphenylpyruvate, 0.2 mM DTT at 26°C, leading to one-crystal clusters or tetragonal bipyramid-shaped crystals, X-ray diffraction structure determination and analysis at 1.47 A and 2.2 A, respectively, modeling
Solenostemon scutellarioides
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34113
-
2 * 34113, sequence calculation and crystal structure
Solenostemon scutellarioides
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
Solenostemon scutellarioides
-
3-(4-hydroxyphenyl)lactate + NADP+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity and 2',5'-ADP affinity chromatography and dialysis
Solenostemon scutellarioides
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cell suspension culture
-
Solenostemon scutellarioides
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3,4-dihydroxyphenylpyruvate + NADH + H+
-
723825
Solenostemon scutellarioides
3-(3,4-dihydroxyphenyl)lactate + NAD+
-
-
-
r
3,4-dihydroxyphenylpyruvate + NADPH + H+
-
723825
Solenostemon scutellarioides
3-(3,4-dihydroxyphenyl)lactate + NADP+
-
-
-
r
3-(4-hydroxyphenyl)pyruvate + NADH + H+
-
723825
Solenostemon scutellarioides
3-(4-hydroxyphenyl)lactate + NAD+
-
-
-
r
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
-
723825
Solenostemon scutellarioides
3-(4-hydroxyphenyl)lactate + NADP+
-
-
-
?
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
substrate bindiing structure, docking study, overview
723825
Solenostemon scutellarioides
3-(4-hydroxyphenyl)lactate + NADP+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 34113, sequence calculation and crystal structure
Solenostemon scutellarioides
More
molecular docking study, overview
Solenostemon scutellarioides
General Information
General Information
Commentary
Organism
evolution
the enzyme belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases
Solenostemon scutellarioides
additional information
movement of the two domains after cosubstrate binding in order to close the inter-domain cleft for catalysis. The amino acids participating in the contacts are Leu205, Arg232 and His279 from the cosubstrate-binding domain and Ser53, Gly77 and Asp79 from the substrate-binding domain. The active site of H(P)PR is formed by the amino-acid residues Arg232 and His279, active site structure, overview
Solenostemon scutellarioides
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases
Solenostemon scutellarioides
additional information
movement of the two domains after cosubstrate binding in order to close the inter-domain cleft for catalysis. The amino acids participating in the contacts are Leu205, Arg232 and His279 from the cosubstrate-binding domain and Ser53, Gly77 and Asp79 from the substrate-binding domain. The active site of H(P)PR is formed by the amino-acid residues Arg232 and His279, active site structure, overview
Solenostemon scutellarioides
Other publictions for EC 1.1.1.237
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)
724428
Fujii
Novel fungal phenylpyruvate re ...
Wickerhamia fluorescens, Wickerhamia fluorescens TK1
Biochim. Biophys. Acta
1814
1669-1676
2011
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1
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5
6
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3
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2
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1
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10
1
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6
1
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4
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1
4
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5
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6
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3
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1
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10
1
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6
1
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1
1
1
1
6
6
723825
Janiak
Structure and substrate dockin ...
Solenostemon scutellarioides
Acta Crystallogr. Sect. D
66
593-603
2010
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1
1
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1
1
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3
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1
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1
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5
2
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3
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1
3
1
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1
1
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1
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1
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5
2
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2
2
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700368
Qian
Influence of growth regulators ...
Solenostemon scutellarioides
Nat. Prod. Res.
23
127-137
2009
1
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3
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1
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4
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1
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700648
Xiao
Methyl jasmonate dramatically ...
Salvia miltiorrhiza
Physiol. Plant.
137
1-9
2009
1
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1
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2
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657023
Kim
Purification, cloning and func ...
Solenostemon scutellarioides
Plant Mol. Biol.
54
311-323
2004
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1
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1
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3
1
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5
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1
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1
1
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3
1
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1
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1
1
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1
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3
1
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1
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1
1
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3
1
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286351
Petersen
-
The biosynthesis of rosmarinic ...
Solenostemon scutellarioides
Plant Cell Tissue Organ Cult.
38
171 - 179
1994
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4
4
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1
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1
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1
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3
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1
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2
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4
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4
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1
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3
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1
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286352
Petersen
-
Proposed biosynthetic pathway ...
Solenostemon scutellarioides
Planta
189
10-14
1993
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1
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1
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286350
Häusler
-
Hydroxyphenylpyruvate reductas ...
Solenostemon scutellarioides
Z. Naturforsch. C
46
371-376
1991
-
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5
5
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1
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1
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2
4
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1
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1
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5
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5
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4
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1
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1
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286349
Petersen
-
Two new enzymes of rosmarinic ...
Solenostemon scutellarioides
Z. Naturforsch. C
43
501-504
1988
2
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