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Information on EC 1.1.1.237 - hydroxyphenylpyruvate reductase

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EC Tree
IUBMB Comments
The enzyme participates in the biosynthesis of rosmarinic acid. It belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases, and prefers NADPH to NADH.
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This record set is specific for:
UNIPROT: F1T2J9
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
hppr, hydroxyphenylpyruvate reductase, 4-hydroxyphenylpyruvate reductase, hppr3, hppr2, hydroxy(phenyl)pyruvate reductase, h(p)pr, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
HPPR
-
-
-
-
HPRP
-
-
-
-
hydroxyphenylpyruvic acid reductase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
(R)-3-(4-hydroxyphenyl)lactate:NAD(P)+ oxidoreductase
The enzyme participates in the biosynthesis of rosmarinic acid. It belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases, and prefers NADPH to NADH.
CAS REGISTRY NUMBER
COMMENTARY hide
117590-77-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
more than 99.9% D-isomer, L-isomer below limits of detection
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-
?
additional information
?
-
no substrates: pyruvate, oxaloacetate or benzoylformate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
NADPH is preferred over NADH
NADPH
preferred over NADH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
1 mM, less than 10% residual activity
Fe2+
1 mM, less than 10% residual activity
Hg2+
1 mM, less than 10% residual activity
WO42-
1 mM, less than 10% residual activity
Zn2+
1 mM, less than 10% residual activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
NADH
pH 6.5, 25°C
0.01
NADPH
pH 6.5, 25°C
0.4
phenylpyruvate
pH 6.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19
glyoxylate
pH 6.5, 25°C
73
hydroxyphenylpyruvate
pH 6.5, 25°C
9.1
Hydroxypyruvate
pH 6.5, 25°C
31
NADH
pH 6.5, 25°C
121
NADPH
pH 6.5, 25°C
150
phenylpyruvate
pH 6.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
glyoxylate
pH 6.5, 25°C
110
hydroxyphenylpyruvate
pH 6.5, 25°C
2.6
Hydroxypyruvate
pH 6.5, 25°C
310
NADH
pH 6.5, 25°C
12000
NADPH
pH 6.5, 25°C
380
phenylpyruvate
pH 6.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
Wickerhamia fluorescens efficiently converts phenylalanine and phenylpyruvate to D-phenyllactate. These compounds up-regulate the transcription of enzyme gene pprA
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
F1T2J9_9ASCO
364
0
40265
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
2 * 40000, SDS-PAGE, 2 * 40300, calculated
40300
2 * 40000, SDS-PAGE, 2 * 40300, calculated
75000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 40000, SDS-PAGE, 2 * 40300, calculated
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
presence of phenylalanine results in up to 40fold increase in transcripts
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujii, T.; Shimizu, M.; Doi, Y.; Fujita, T.; Ito, T.; Miura, D.; Wariishi, H.; Takaya, N.
Novel fungal phenylpyruvate reductase belongs to D-isomer-specific 2-hydroxyacid dehydrogenase family
Biochim. Biophys. Acta
1814
1669-1676
2011
Wickerhamia fluorescens (F1T2J9), Wickerhamia fluorescens TK1 (F1T2J9)
Manually annotated by BRENDA team