Information on EC 1.1.1.237 - hydroxyphenylpyruvate reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.237
-
RECOMMENDED NAME
GeneOntology No.
hydroxyphenylpyruvate reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-(4-hydroxyphenyl)lactate + NAD+ = 3-(4-hydroxyphenyl)pyruvate + NADH + H+
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-hydroxybenzoate biosynthesis I (eukaryotes)
-
-
Biosynthesis of secondary metabolites
-
-
Phenylalanine metabolism
-
-
rosmarinic acid biosynthesis II
-
-
Tropane, piperidine and pyridine alkaloid biosynthesis
-
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Tyrosine metabolism
-
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Ubiquinone and other terpenoid-quinone biosynthesis
-
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suberin monomers biosynthesis
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-
SYSTEMATIC NAME
IUBMB Comments
4-hydroxyphenyllactate:NAD+ oxidoreductase
Also acts on 3-(3,4-dihydroxyphenyl)lactate. Involved with EC 2.3.1.140 rosmarinate synthase in the biosynthesis of rosmarinic acid.
CAS REGISTRY NUMBER
COMMENTARY hide
117590-77-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxyphenylpyruvate + NADH
3-(3,4-dihydroxyphenyl)lactate + NAD+
show the reaction diagram
3,4-dihydroxyphenylpyruvate + NADH + H+
3-(3,4-dihydroxyphenyl)lactate + NAD+
show the reaction diagram
-
-
-
r
3,4-dihydroxyphenylpyruvate + NADPH + H+
3,4-dihydroxyphenyllactate + NADP+
show the reaction diagram
-
-
-
?
3,4-dihydroxyphenylpyruvate + NADPH + H+
3-(3,4-dihydroxyphenyl)lactate + NADP+
show the reaction diagram
-
-
-
r
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH
show the reaction diagram
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
show the reaction diagram
-
-
-
r
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
show the reaction diagram
3-methoxy-4-hydroxyphenylpyruvate + NADH
3-(3-methoxy-4-hydroxyphenyl)lactate + NAD+
show the reaction diagram
-
-
-
-
?
4-hydroxyphenylpyruvate + NADH
3-(4-hydroxyphenyl)lactate + NAD+
show the reaction diagram
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
show the reaction diagram
4-hydroxyphenylpyruvate + NADPH + H+
D-(4-hydroxyphenyl)lactate + NADP+
show the reaction diagram
glyoxylate + NADPH + H+
glycolate + NADP+
show the reaction diagram
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
show the reaction diagram
phenylpyruvate + NADPH + H+
D-phenyllactate + NADP+
show the reaction diagram
additional information
?
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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
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH
show the reaction diagram
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
show the reaction diagram
Q65CJ7
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-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
NADPH is preferred over NADH
NADP+
NADPH
additional information
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxyphenylpyruvate
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substrate inhibition
Cu2+
1 mM, less than 10% residual activity
dihydroxyphenylpyruvate
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substrate inhibition
Fe2+
1 mM, less than 10% residual activity
Hg2+
1 mM, less than 10% residual activity
oxaloacetate
-
inhibition at 5 mM
p-Coumaroyl-CoA
pyruvate
rosmarinic acid
WO42-
1 mM, less than 10% residual activity
Zn2+
1 mM, less than 10% residual activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbic acid
-
prevents oxidation of substrates
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
130
3,4-Dihydroxyphenylpyruvate
250
3-methoxy-4-hydroxyphenylpyruvate
-
pH 7
10
4-hydroxyphenylpyruvate
18.9
glyoxylate
pH 6.5, 25°C
0.64
hydroxyphenylpyruvate
pH 6.5, 25°C
3.5
Hydroxypyruvate
pH 6.5, 25°C
0.1 - 190
NADH
0.01 - 95
NADPH
0.4
phenylpyruvate
pH 6.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19
glyoxylate
Wickerhamia fluorescens
F1T2J9
pH 6.5, 25°C
73
hydroxyphenylpyruvate
Wickerhamia fluorescens
F1T2J9
pH 6.5, 25°C
9.1
Hydroxypyruvate
Wickerhamia fluorescens
F1T2J9
pH 6.5, 25°C
31
NADH
Wickerhamia fluorescens
F1T2J9
pH 6.5, 25°C
121
NADPH
Wickerhamia fluorescens
F1T2J9
pH 6.5, 25°C
150
phenylpyruvate
Wickerhamia fluorescens
F1T2J9
pH 6.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
glyoxylate
Wickerhamia fluorescens
F1T2J9
pH 6.5, 25°C
101
110
hydroxyphenylpyruvate
Wickerhamia fluorescens
F1T2J9
pH 6.5, 25°C
3899
2.6
Hydroxypyruvate
Wickerhamia fluorescens
F1T2J9
pH 6.5, 25°C
389
310
NADH
Wickerhamia fluorescens
F1T2J9
pH 6.5, 25°C
8
12000
NADPH
Wickerhamia fluorescens
F1T2J9
pH 6.5, 25°C
5
380
phenylpyruvate
Wickerhamia fluorescens
F1T2J9
pH 6.5, 25°C
198
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34110
calculation from amino acid sequence
40000
2 * 40000, SDS-PAGE, 2 * 40300, calculated
40300
2 * 40000, SDS-PAGE, 2 * 40300, calculated
45000 - 68000
gel filtration
75000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 34113, calculation from nucleotide sequence
homodimer
2 * 34113, sequence calculation and crystal structure
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to oxidation by light and oxygen
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, loss of 30% activity after 1 month
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-20°C, loss of 85% activity after 10 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and Sephadex G25 column
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recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity and 2',5'-ADP affinity chromatography and dialysis
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
presence of phenylalanine results in up to 40fold increase in transcripts