Information on EC 1.1.1.237 - hydroxyphenylpyruvate reductase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
1.1.1.237
-
RECOMMENDED NAME
GeneOntology No.
hydroxyphenylpyruvate reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-(4-hydroxyphenyl)lactate + NAD+ = 3-(4-hydroxyphenyl)pyruvate + NADH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
-
-
suberin monomers biosynthesis
-
-
Tropane, piperidine and pyridine alkaloid biosynthesis
-
-
Tyrosine metabolism
-
-
Ubiquinone and other terpenoid-quinone biosynthesis
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4-hydroxyphenylpyruvate reductase
-
-
HPPR
-
-
-
-
HPRP
-
-
-
-
hydroxy(phenyl)pyruvate reductase
Q65CJ7
-
hydroxyphenylpyruvate reductase
Q65CJ7
-
hydroxyphenylpyruvic acid reductase
-
-
-
-
Ppr
Wickerhamia fluorescens TK1
F1T2J9
-
-
pprA
F1T2J9
gene name
pprA
Wickerhamia fluorescens TK1
F1T2J9
gene name
-
CAS REGISTRY NUMBER
COMMENTARY
117590-77-9
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Coleus blumei
SwissProt
Manually annotated by BRENDA team
Wickerhamia fluorescens TK1
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
F1T2J9
Wickerhamia fluorescens efficiently converts phenylalanine and phenylpyruvate to D-phenyllactate. These compounds up-regulate the transcription of enzyme gene pprA
physiological function
Wickerhamia fluorescens TK1
-
Wickerhamia fluorescens efficiently converts phenylalanine and phenylpyruvate to D-phenyllactate. These compounds up-regulate the transcription of enzyme gene pprA
-
evolution
Q65CJ7
the enzyme belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases
additional information
Q65CJ7
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
3-(3,4-dihydroxyphenyl)lactate + NAD+
show the reaction diagram
-
-
-
r
3,4-dihydroxyphenylpyruvate + NADH
3-(3,4-dihydroxyphenyl)lactate + NAD+
show the reaction diagram
-
-
-
r
3,4-dihydroxyphenylpyruvate + NADH + H+
3-(3,4-dihydroxyphenyl)lactate + NAD+
show the reaction diagram
Q65CJ7
-
-
-
r
3,4-dihydroxyphenylpyruvate + NADPH + H+
3,4-dihydroxyphenyllactate + NADP+
show the reaction diagram
Q65CJ7
-
-
-
?
3,4-dihydroxyphenylpyruvate + NADPH + H+
3-(3,4-dihydroxyphenyl)lactate + NADP+
show the reaction diagram
Q65CJ7
-
-
-
r
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH
show the reaction diagram
-
-
-
-
?
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH
show the reaction diagram
-
biosynthesis of rosmarinic acid
-
?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
show the reaction diagram
Q65CJ7
-
-
-
r
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
show the reaction diagram
Q65CJ7
-
-
-
?
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
show the reaction diagram
Q65CJ7
substrate bindiing structure, docking study, overview
-
-
r
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 + NADH
3-(4-hydroxyphenyl)lactate + NAD+
show the reaction diagram
-
-
-
r
4-hydroxyphenylpyruvate + NADH
3-(4-hydroxyphenyl)lactate + NAD+
show the reaction diagram
-
-
-
r
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
show the reaction diagram
Q65CJ7
the enzyme is involved in L-serine biosynthesis and rosmarinic acid biosynthesis
-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
show the reaction diagram
-
part of the metabolic pathway leading to rosmarinic acid and lithospermic acid B
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
show the reaction diagram
Wickerhamia fluorescens, Wickerhamia fluorescens TK1
F1T2J9
-
-
-
?
hydroxyphenylpyruvate + NADPH + H+
D-hydroxyphenyllactate + NADP+
show the reaction diagram
Wickerhamia fluorescens, Wickerhamia fluorescens TK1
F1T2J9
-
-
-
?
phenylpyruvate + NADPH + H+
D-phenyllactate + NADP+
show the reaction diagram
Wickerhamia fluorescens, Wickerhamia fluorescens TK1
F1T2J9
more than 99.9% D-isomer, L-isomer below limits of detection
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
show the reaction diagram
Wickerhamia fluorescens, Wickerhamia fluorescens TK1
F1T2J9
-
-
-
?
additional information
?
-
-
rosmarinic acid biosynthetic pathway is regulated by interactions of several enzymes necessary for biosynthesis including HPPR
-
-
-
additional information
?
-
Wickerhamia fluorescens, Wickerhamia fluorescens TK1
F1T2J9
no substrates: pyruvate, oxaloacetate or benzoylformate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH
show the reaction diagram
-
-
-
-
?
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH
show the reaction diagram
-
biosynthesis of rosmarinic acid
-
?
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
show the reaction diagram
Q65CJ7
-
-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
show the reaction diagram
Q65CJ7
the enzyme is involved in L-serine biosynthesis and rosmarinic acid biosynthesis
-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
show the reaction diagram
-
part of the metabolic pathway leading to rosmarinic acid and lithospermic acid B
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
F1T2J9
NADPH is preferred over NADH
NADP+
-
with lower activity than NAD+
NADPH
Q65CJ7
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
NADPH
F1T2J9
preferred over NADH
additional information
Q65CJ7
NADH as well as NADPH can serve as the electron donor
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-hydroxyphenylpyruvate
-
substrate inhibition
Cu2+
F1T2J9
1 mM, less than 10% residual activity
dihydroxyphenylpyruvate
-
substrate inhibition
Fe2+
F1T2J9
1 mM, less than 10% residual activity
Hg2+
F1T2J9
1 mM, less than 10% residual activity
oxaloacetate
-
inhibition at 5 mM
p-Coumaroyl-CoA
-
50% inhibition at 0.5 mM
p-Coumaroyl-CoA
-
-
pyruvate
-
competitive inhibition
pyruvate
-
inhibition at 4 mM
rosmarinic acid
-
competitive inhibition
rosmarinic acid
-
-
WO42-
F1T2J9
1 mM, less than 10% residual activity
Zn2+
F1T2J9
1 mM, less than 10% residual activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbic acid
-
prevents oxidation of substrates
additional information
-
best result for rosmarinic acid accumulation is obtained when B5-medium supplemented is with 2.0 mg/l 6-benzyl-aminopurine, 0.5 mg/l alpha-naphthaleneacetic, 0.8 mg/L 2,4-dichlorophenxyaretic acid and 2% sucrose, and solidified with 0.8% agar. Both growth index and rosmarinic acid accumulation reach a maximum, which is 49.7 and 25.3% (dry weight), respectively. Rosmarinic acid accumulation is enhanced by the sucrose concentrations
-
additional information
-
methyl jasmonate gradually stimulates transcription value of HPPR and reaches the highest level on day 6, and then follows by a reduction, maximum mRNA transcript level reaches 8fold higher than the control. Dramatically increases the biosyntheses of rosmarinic acid and lithospermic acid B
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
130
3,4-Dihydroxyphenylpyruvate
-
pH 7
130
3,4-Dihydroxyphenylpyruvate
-
-
250
3-methoxy-4-hydroxyphenylpyruvate
-
pH 7
10
4-hydroxyphenylpyruvate
-
pH 7
10
4-hydroxyphenylpyruvate
-
-
18.9
glyoxylate
F1T2J9
pH 6.5, 25C
0.64
hydroxyphenylpyruvate
F1T2J9
pH 6.5, 25C
3.5
Hydroxypyruvate
F1T2J9
pH 6.5, 25C
0.1
NADH
F1T2J9
pH 6.5, 25C
0.01
NADPH
F1T2J9
pH 6.5, 25C
0.4
phenylpyruvate
F1T2J9
pH 6.5, 25C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19
glyoxylate
F1T2J9
pH 6.5, 25C
73
hydroxyphenylpyruvate
F1T2J9
pH 6.5, 25C
9.1
Hydroxypyruvate
F1T2J9
pH 6.5, 25C
31
NADH
F1T2J9
pH 6.5, 25C
121
NADPH
F1T2J9
pH 6.5, 25C
150
phenylpyruvate
F1T2J9
pH 6.5, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
glyoxylate
F1T2J9
pH 6.5, 25C
101
110
hydroxyphenylpyruvate
F1T2J9
pH 6.5, 25C
3899
2.6
Hydroxypyruvate
F1T2J9
pH 6.5, 25C
389
310
NADH
F1T2J9
pH 6.5, 25C
8
12000
NADPH
F1T2J9
pH 6.5, 25C
5
380
phenylpyruvate
F1T2J9
pH 6.5, 25C
198
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
727
F1T2J9
pH 6.5, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7
F1T2J9
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Plectranthus scutellarioides
Plectranthus scutellarioides
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34110
Q65CJ7
calculation from amino acid sequence
657023
45000 - 68000
Q65CJ7
gel filtration
657023
75000
F1T2J9
gel filtration
724428
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
Q65CJ7
x * 34113, calculation from nucleotide sequence
dimer
F1T2J9
2 * 40000, SDS-PAGE, 2 * 40300, calculated
dimer
Wickerhamia fluorescens TK1
-
2 * 40000, SDS-PAGE, 2 * 40300, calculated
-
homodimer
Q65CJ7
2 * 34113, sequence calculation and crystal structure
additional information
Q65CJ7
molecular docking study, overview
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 4C, or 20% PEG 1000, 0.1 M imidazole, pH 7.5, 4 mM 4-hydroxyphenylpyruvate, 0.2 mM DTT at 26C, 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
Q65CJ7
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to oxidation by light and oxygen
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, loss of 30% activity after 1 month
-
-20C, loss of 85% activity after 10 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and Sephadex G25 column
-
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity and 2',5'-ADP affinity chromatography and dialysis
Q65CJ7
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
Q65CJ7
expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS
Q65CJ7
expression in Escherichia coli
F1T2J9
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
presence of phenylalanine results in up to 40fold increase in transcripts
F1T2J9
presence of phenylalanine results in up to 40fold increase in transcripts
Wickerhamia fluorescens TK1
-
-