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Information on EC 1.1.1.237 - hydroxyphenylpyruvate reductase
for references in articles please use BRENDA:EC1.1.1.237
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.237 hydroxyphenylpyruvate reductase
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.
The enzyme appears in viruses and cellular organisms
- 1.1.1.237
-
rosmarinic
- coronary
- clopidogrel
-
post-treatment
- salvia
- miltiorrhiza
-
adp-induced
-
percutaneous
-
aggregometry
-
verifynow
-
antiplatelet
- lamiaceae
-
p-selectin
- cilostazol
- bunge
-
coleus
-
4-hydroxyphenyllactic
-
lithospermic
- blumei
Reaction Schemes
showSynonyms
hppr, hydroxyphenylpyruvate reductase, 4-hydroxyphenylpyruvate reductase, hppr2, hppr3, h(p)pr, hydroxy(phenyl)pyruvate reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-hydroxyphenylpyruvate reductase
At1g79870
HPPR
HPPR2
HPPR3
HPR2
HPRP
-
-
-
-
hydroxyphenylpyruvic acid reductase
-
-
-
-
Ppr
pprA
HPPR
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-3-(3,4-dihydroxyphenyl)lactate + NAD(P)+ = 3-(3,4-dihydroxyphenyl)pyruvate + NAD(P)H + H+
(2)
-
-
-
(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+ = 3-(4-hydroxyphenyl)pyruvate + NAD(P)H + H+
(1)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
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redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
rosmarinic acid biosynthesis I, rosmarinic acid biosynthesis II
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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.
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CAS REGISTRY NUMBER
COMMENTARY
117590-77-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxyphenylpyruvate + NADPH + H+
3,4-dihydroxyphenyllactate + NADP+
Substrates: -
Products: -
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?
3,4-dihydroxyphenylpyruvate + NADPH + H+
3-(3,4-dihydroxyphenyl)lactate + NADP+
Substrates: -
Products: -
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r
3-methoxy-4-hydroxyphenylpyruvate + NADH + H+
3-(3-methoxy-4-hydroxyphenyl)lactate + NAD+
-
Substrates: -
Products: -
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?
beta-phenylpyruvate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
-
Substrates: -
Products: -
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r
3,4-dihydroxyphenylpyruvate + NADH + H+
3-(3,4-dihydroxyphenyl)lactate + NAD+
-
Substrates: -
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3,4-dihydroxyphenylpyruvate + NADH + H+
3-(3,4-dihydroxyphenyl)lactate + NAD+
-
Substrates: -
Products: -
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?
3,4-dihydroxyphenylpyruvate + NADH + H+
3-(3,4-dihydroxyphenyl)lactate + NAD+
Substrates: -
Products: -
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r
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH + H+
-
Substrates: biosynthesis of rosmarinic acid
Products: -
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?
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH + H+
-
Substrates: -
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3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Substrates: -
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r
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Substrates: -
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?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Substrates: -
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3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Substrates: -
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r
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Substrates: -
Products: -
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?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Substrates: -
Products: -
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?
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
(R)-3-(4-hydroxyphenyl)lactate + NADP+
Substrates: -
Products: -
Products: -
r
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
(R)-3-(4-hydroxyphenyl)lactate + NADP+
Substrates: best substrate
Products: -
Products: -
r
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
(R)-3-(4-hydroxyphenyl)lactate + NADP+
Substrates: -
Products: -
Products: -
r
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
(R)-3-(4-hydroxyphenyl)lactate + NADP+
Substrates: best substrate
Products: -
Products: -
r
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
Substrates: -
Products: -
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?
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
Substrates: substrate bindiing structure, docking study, overview
Products: -
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r
4-hydroxyphenylpyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
-
Substrates: -
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r
4-hydroxyphenylpyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
-
Substrates: -
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4-hydroxyphenylpyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
Substrates: -
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?
4-hydroxyphenylpyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
Substrates: -
Products: -
Products: -
?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
Substrates: the enzyme is involved in L-serine biosynthesis and rosmarinic acid biosynthesis
Products: -
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?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
Substrates: -
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?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
-
Substrates: -
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r
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
-
Substrates: part of the metabolic pathway leading to rosmarinic acid and lithospermic acid B
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?
4-hydroxyphenylpyruvate + NADPH + H+
D-(4-hydroxyphenyl)lactate + NADP+
Substrates: -
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?
4-hydroxyphenylpyruvate + NADPH + H+
D-(4-hydroxyphenyl)lactate + NADP+
Substrates: -
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glyoxylate + NADPH + H+
glycolate + NADP+
Substrates: -
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glyoxylate + NADPH + H+
glycolate + NADP+
Substrates: -
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hydroxypyruvate + NADH + H+
D-glycerate + NAD+
Substrates: -
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hydroxypyruvate + NADH + H+
D-glycerate + NAD+
Substrates: -
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hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
Substrates: reaction of EC 1.1.1.81
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hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
Substrates: -
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hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
Substrates: -
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?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
Substrates: reaction of EC 1.1.1.81
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phenylpyruvate + NADPH + H+
D-phenyllactate + NADP+
Substrates: -
Products: -
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phenylpyruvate + NADPH + H+
D-phenyllactate + NADP+
Substrates: -
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phenylpyruvate + NADPH + H+
D-phenyllactate + NADP+
Substrates: more than 99.9% D-isomer, L-isomer below limits of detection
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phenylpyruvate + NADPH + H+
D-phenyllactate + NADP+
Substrates: more than 99.9% D-isomer, L-isomer below limits of detection
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phenylpyruvate + NADPH + H+
phenyllactate + NADP+
Substrates: -
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phenylpyruvate + NADPH + H+
phenyllactate + NADP+
Substrates: -
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?
additional information
?
-
Substrates: isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
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?
additional information
?
-
Substrates: isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
Products: -
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?
additional information
?
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Substrates: isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
Products: -
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?
additional information
?
-
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Substrates: isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
Products: -
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?
additional information
?
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Substrates: isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
Products: -
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?
additional information
?
-
-
Substrates: rosmarinic acid biosynthetic pathway is regulated by interactions of several enzymes necessary for biosynthesis including HPPR
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additional information
?
-
Substrates: no substrates: pyruvate, oxaloacetate or benzoylformate
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additional information
?
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Substrates: no substrates: pyruvate, oxaloacetate or benzoylformate
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
Substrates: -
Products: -
Products: -
?
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH + H+
-
Substrates: biosynthesis of rosmarinic acid
Products: -
Products: -
?
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH + H+
-
Substrates: -
Products: -
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?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Substrates: -
Products: -
Products: -
?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Substrates: -
Products: -
Products: -
?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Substrates: -
Products: -
Products: -
r
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Substrates: -
Products: -
Products: -
?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Substrates: -
Products: -
Products: -
?
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
(R)-3-(4-hydroxyphenyl)lactate + NADP+
Substrates: -
Products: -
Products: -
r
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
(R)-3-(4-hydroxyphenyl)lactate + NADP+
Substrates: -
Products: -
Products: -
r
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
Substrates: the enzyme is involved in L-serine biosynthesis and rosmarinic acid biosynthesis
Products: -
Products: -
?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
-
Substrates: part of the metabolic pathway leading to rosmarinic acid and lithospermic acid B
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
NADH as well as NADPH can serve as the electron donor
-
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Coronary Artery Disease
Impact of chronic kidney disease on platelet function profiles in diabetes mellitus patients with coronary artery disease taking dual antiplatelet therapy.
Diabetes Mellitus
Clinical Predictors of High Posttreatment Platelet Reactivity to Clopidogrel in Koreans.
Myocardial Infarction
High post-treatment platelet reactivity is associated with a high incidence of myonecrosis after stenting for non-ST elevation acute coronary syndromes.
Renal Insufficiency, Chronic
Clinical Predictors of High Posttreatment Platelet Reactivity to Clopidogrel in Koreans.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.37
3-(4-hydroxyphenyl)pyruvate
pH 7.0, 30°C, recombinant enzyme
3.57
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
1.5 - 2
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.285
3-(4-hydroxyphenyl)pyruvate
pH 7.0, 30°C, recombinant enzyme
0.052
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
0.611
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.77
3-(4-hydroxyphenyl)pyruvate
pH 7.0, 30°C, recombinant enzyme
0.402
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv. Tigullio, a commercial cultivar of sweet basil
UniProt
brenda
catalyzes reactions of EC 1.1.1.237 and EC 1.1.1.81
UniProt
brenda
catalyzes reactions of EC 1.1.1.79, EC 1.1.1.81, EC 1.1.1.237
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
hig enzyme activity and rosmarinic acid content, transcript expression level during cell suspension culture
brenda
additional information
high overall expression in seedling
brenda
additional information
high overall expression in seedling
brenda
additional information
high overall expression in seedling
brenda
additional information
quantitative reverse transcription PCR enzyme expression analysis
brenda
additional information
quantitative reverse transcription PCR enzyme expression analysis
brenda
additional information
quantitative reverse transcription PCR enzyme expression analysis
brenda
additional information
-
quantitative reverse transcription PCR enzyme expression analysis
brenda
additional information
plants inoculated with bacteria, and mycorrhizal plants
brenda
additional information
quantitative real-time PCR analysis of the transcription pattern indicates that the PfHPPR expresses constitutively in all examined tissues but most highly in leaves
brenda
additional information
the enzyme gene expression is the highest in stem, the second in root, and lowest in leaf
brenda
additional information
-
the enzyme gene expression is the highest in stem, the second in root, and lowest in leaf
brenda
additional information
-
transcript levels of SbHPPR in the flowers are higher than those in other organs. The amount of accumulated rosmarinic acid in the flowers is 28.7times higher than that in the roots. No rosmarinic acid is detected in the leaves and stems
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases
evolution
comparison of HPPR gene sequences from Perilla frutescens and other species reveals that the HPPR genes are structurally conserved and might possess similar functions
evolution
HPPR belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases
evolution
no hydroxyphenylpyruvate reductase (HPPR) activity by isozyme HPPR4 from Arabidopsis thaliana. Isozyme HPPR2 mainly shows hydroxypyruvate reductase (HPR) activity (EC 1.1.1.81), while isozyme HPPR3 mainly shows 4-hydroxyphenylpyruvate reductase activity. Enzyme HPPR3 belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases, group II
evolution
-
no hydroxyphenylpyruvate reductase (HPPR) activity by isozyme HPPR4 from Arabidopsis thaliana. Isozyme HPPR2 mainly shows hydroxypyruvate reductase (HPR) activity (EC 1.1.1.81), while isozyme HPPR3 mainly shows 4-hydroxyphenylpyruvate reductase activity. Enzyme HPPR3 belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases, group II
-
malfunction
Arabidopsis thaliana mutants defective in either HPPR2 or HPPR3 isozyme contain lower amounts of pHPL and are impaired in conversion of tyrosine to pHPL. Furthermore, a loss-of-function mutation in tyrosine aminotransferase (TAT) also reduces the pHPL accumulation in plants. HPR mutants show impaired growth and contain less chlorophyll, phenotypes, detailed overview
malfunction
-
Arabidopsis thaliana mutants defective in either HPPR2 or HPPR3 isozyme contain lower amounts of pHPL and are impaired in conversion of tyrosine to pHPL. Furthermore, a loss-of-function mutation in tyrosine aminotransferase (TAT) also reduces the pHPL accumulation in plants. HPR mutants show impaired growth and contain less chlorophyll, phenotypes, detailed overview
-
metabolism
the enzyme is involved in biosynthesis of rosmarinic acid via the tyrosine-derived pathway, tyrosine is metabolized to 4-hydroxyphenyllactate by tyrosine aminotransferase (TAT, EC 2.6.1.5) and 4-hydroxyphenylpyruvate reductase (HPPR, EC 1.1.1.237), pathway overview. 4-Hydroxyphenylpyruvated dioxygenase transforms 4-hydroxyphenylpyruvate acid to homogentisic acid, therefore competing for the same substrate with HPPR in the tyrosine-derived pathway. Regulation of water-soluble phenolic acid biosynthesis in Salvia miltiorrhiza via regulators at molecular level, such as the phenylalanine ammonia-lyase gene (PAL), cinnamic acid 4-hydroxylase gene (C4H), 4-coumarate-CoA ligase gene (4CL), tyrosine aminotransferase gene (TAT), 4-hydroxyphenylpyruvate reductase gene (HPPR), 4-hydroxyphenylpyruvated dioxygenase gene (HPPD), hydroxycinnamoyl-CoA:hydroxyphenyllactate hydroxycinnamoyl transferase-like gene (RAS-like), and v-myb avian myeloblastosis viral oncogene homolog 4 gene (MYB4), and production of anthocyanin pigmentation 1 gene (AtPAP1), and via regulators at cell level, such as methyl jasmonate, salicylic acid, abscisic acid, polyamines, metal ions, hydrogen peroxide (H2O2), ultraviolet-B radiation, and yeast elicitor, overview
metabolism
HPPR is a key enzyme involved in the rosmarinic acid biosynthesis via the tyrosine-dependent pahtway
metabolism
-
the key enzyme is involved in rosmarinic acid biosynthesis
metabolism
-
the key enzyme is involved in biosynthesis of rosmarinic acid via the tyrosine-derived pathway, overview
metabolism
hydroxyphenylpyruvate reductase is involved in rosmarinic acid biosynthesis via the tyrosine pathway
metabolism
the enzyme is involved in biosynthesis of rosmarinic acid via the tyrosine-derived pathway, overview. Activity of HPPR seems to be a arte-limiting point in rosmarinic acid biosynthesis
metabolism
the key enzyme is involved in biosynthesis of rosmarinic acid via the tyrosine-derived pathway
metabolism
in vitro characterization of the recombinant proteins reveals that HPPR2 has both hydroxypyruvate reductase (HPR EC 1.1.1.81) and hydroxyphenylpyruvate reductase (HPPR) activities, whereas HPPR3 has a strong preference for pHPP, and both enzymes are localized in the cytosol. In Arabidopsis thaliana, HPPR2 and HPPR3, together with tyrosine aminotransferase 1 (TAT1), constitute to a probably conserved biosynthetic pathway from tyrosine to 4-hydroxyphenyllactic acid (pHPL), from which some specialized metabolites, such as rosmarinic acid (RA), can be generated in specific groups of plants. Role of HPPR in the tyrosine conversion pathway, overview
metabolism
-
in vitro characterization of the recombinant proteins reveals that HPPR2 has both hydroxypyruvate reductase (HPR EC 1.1.1.81) and hydroxyphenylpyruvate reductase (HPPR) activities, whereas HPPR3 has a strong preference for pHPP, and both enzymes are localized in the cytosol. In Arabidopsis thaliana, HPPR2 and HPPR3, together with tyrosine aminotransferase 1 (TAT1), constitute to a probably conserved biosynthetic pathway from tyrosine to 4-hydroxyphenyllactic acid (pHPL), from which some specialized metabolites, such as rosmarinic acid (RA), can be generated in specific groups of plants. Role of HPPR in the tyrosine conversion pathway, overview
-
physiological function
Wickerhamia fluorescens efficiently converts phenylalanine and phenylpyruvate to D-phenyllactate. These compounds up-regulate the transcription of enzyme gene pprA
physiological function
enzyme HPPR catalyzes the first specific biosynthetic step in the biosynthesis of rosmarinic acid from the aromatic amino acids phenylalanine and tyrosine
physiological function
Arabidopsis mutants defective in either isoform HPPR2 or HPPR3 contain lower amounts of 4-hydroxyphenyllactic acid and are impaired in conversion of tyrosine to 4-hydroxyphenyllactic acid
physiological function
hydroxyphenylpyruvate reductase (HPPR), which catalyzes the reduction of 4-hydroxyphenylpyruvic acid (pHPP) to 4-hydroxyphenyllactic acid (pHPL), is the key enzyme in the biosynthesis of rosmarinic acid (RA) from tyrosine and, so far, HPPR activity is reported only from the RA-accumulating plants
physiological function
-
hydroxyphenylpyruvate reductase (HPPR), which catalyzes the reduction of 4-hydroxyphenylpyruvic acid (pHPP) to 4-hydroxyphenyllactic acid (pHPL), is the key enzyme in the biosynthesis of rosmarinic acid (RA) from tyrosine and, so far, HPPR activity is reported only from the RA-accumulating plants
-
physiological function
-
Arabidopsis mutants defective in either isoform HPPR2 or HPPR3 contain lower amounts of 4-hydroxyphenyllactic acid and are impaired in conversion of tyrosine to 4-hydroxyphenyllactic acid
-
physiological function
-
Wickerhamia fluorescens efficiently converts phenylalanine and phenylpyruvate to D-phenyllactate. These compounds up-regulate the transcription of enzyme gene pprA
-
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HPPR_PLESU
313
0
34128
Swiss-Prot
other Location (Reliability: 3)
A0A0A7DW92_OCIBA
204
0
22055
TrEMBL
Secretory Pathway (Reliability: 1)
F1T2J9_9ASCO
364
0
40265
TrEMBL
other Location (Reliability: 5)
F8RGR8_PERFR
313
0
34423
TrEMBL
Secretory Pathway (Reliability: 1)
M1H6F7_SALOF
313
0
33939
TrEMBL
Secretory Pathway (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34113
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
homodimer
2 * 34113, sequence calculation and crystal structure
additional information
secondary structure, and homology-based structural modeling
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
expression analysis of HPPR2, HPPR3, and other pathway-related enzymes in mutant strains, HPPR3 mutant phenotype, overview
additional information
expression analysis of HPPR2, HPPR3, and other pathway-related enzymes in mutant strains, HPPR3 mutant phenotype, overview
additional information
expression analysis of HPPR2, HPPR3, and other pathway-related enzymes in mutant strains, HPPR3 mutant phenotype, overview
additional information
-
expression analysis of HPPR2, HPPR3, and other pathway-related enzymes in mutant strains, HPPR3 mutant phenotype, overview
additional information
-
expression analysis of HPPR2, HPPR3, and other pathway-related enzymes in mutant strains, HPPR3 mutant phenotype, overview
-
additional information
-
cultures fed with precursors, namely L-Phe, L-Tyr, and cucumber juice, at different concentrations show Phe an 1.5, 2.1, and 1.6fold increase in rosmarinic acid accumulation within 48-72 h, respectively. In this study, we focused on the function of individual precursor on key enzymes involved in RA biosynthesis. The phenylalanine ammonia lyase activity was significantly upregulated after Phe feeding, while tyrosine aminotransferase and hydroxyphenylpyruvate reductase activities are improved with Tyr treatment. Rosmarinic acid synthase activity is significantly enhanced by all three precursors, overview
additional information
hairy root lines of Coleus blumei carrying HPPR or rosmarinic acid synthase (RAS) RNAi suppression and overexpression constructs are established using Agrobacterium rhizogenes-mediated transformation. Hairy root lines showing undetectable HPPR or RAS mRNA levels displayed strongly reduced rosmarinic acid contents with reduction of up to 92% compared to control hairy root lines. An increase of rosmarinic acid levels up to 176% occurs in overexpression hairy root lines with equally increased HPPR transcript levels while RAS overexpression results in co-suppression effects with reduced rosmarinic acid levels
additional information
overexpression of HPPR does not lead to the enhancement of phenolic acid production in comparison with control. Single HPPR transgenic lines and TAT-HPPR co-transgenic lines present much higher rosmarinic acid and lithospermic acid B accumulation. Although possessing a relatively low TAT and HPPR transcript level compared with the single-gene transgenic lines, the TAT-HPPR co-transgenic lines produce over 16.1times rosmarinic acid and 18.8times lithospermic acid B than that in control lines. TAT-HPPR co-transgenic lines possess the lowest accumulation level of homogentisic acid, a compound involved in the competitive branch of rosmarinic acid biosynthesis and produced by HPPD from 4-hydroxyphenylpyruvic acid precursor. This most likely suggested a metabolic flux shift from the homogentisic acid branch to the rosmarinic acid pathway
additional information
-
overexpression of HPPR does not lead to the enhancement of phenolic acid production in comparison with control. Single HPPR transgenic lines and TAT-HPPR co-transgenic lines present much higher rosmarinic acid and lithospermic acid B accumulation. Although possessing a relatively low TAT and HPPR transcript level compared with the single-gene transgenic lines, the TAT-HPPR co-transgenic lines produce over 16.1times rosmarinic acid and 18.8times lithospermic acid B than that in control lines. TAT-HPPR co-transgenic lines possess the lowest accumulation level of homogentisic acid, a compound involved in the competitive branch of rosmarinic acid biosynthesis and produced by HPPD from 4-hydroxyphenylpyruvic acid precursor. This most likely suggested a metabolic flux shift from the homogentisic acid branch to the rosmarinic acid pathway
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain Rose-gami B (DE3) by nickel affinity chromatography and desalting gel filtration
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity and 2',5'-ADP affinity chromatography and dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS
gene CbHPPR, DNA and amino acid sequence determination and analysis, hairy root lines of Coleus blumei carrying HPPR RNAi suppression and overexpression constructs are established using Agrobacterium rhizogenes strain LBA15834-mediated transformation, HPPR is overexpressed under control of the constitutive CaMV 35S-promoter
gene HPPR, quantitative real-time reverse transcription PCR enzyme expression analysis
gene PfHPPR, DNA and amino acid sequence determination and analysis, sequence comparisons, quantitative real-time PCR enzyme expression analysis
gene SbHPPR, DNA and amino acid sequence determination and analysis, sequence comparisons, quantitative real-time PCR enzyme expression analysis
-
gene SmHPPR, semiquantitative RT-PCR enzyme expression analysis
gene SoHPPR, DNA and amino acid sequence determination and analysis, sequence comparisons, quantitative RT-PCR enzyme expression analysis
isozyme HPPR3, sequence comparisons and phylogenetic analysis, quantitative reverse transcription PCR enzyme expression analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rose-gami B (DE3). Recombinant expression of GFP-tagged enzyme in Arabidopsis thaliana protoplasts
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
basil plant inoculation with either the arbuscular mycorrhizal fungus (AMF) species Rhizophagus intraradices or a combination of two plant growth-promoting (PGP) isolated from its sporosphere, Sinorhizobium meliloti TSA41 and Streptomyces sp. W43N, triggers the overexpression hydroxyphenylpyruvate reductase (HPPR) and other genes encoding enzymes in volved in the rosmiarinic acid biosynthesis, overview. Levels of HPPR downstream of TAT are upregulated 2fold in leaves produced by plants inoculated with bacteria, while in mycorrhizal plants, they are downregulated
expression of PfHPPR can be induced by several factors such as abscisic acid (ABA), salicylic acid (SA), and ultraviolet-B radiation (UV-B)
levels of HPPR downstream of TAT are upregulated 2fold in leaves produced by plants inoculated with bacteria, while in mycorrhizal plants, they are downregulated
methyljasmonate, salicylic acid, gibberellic acid 3, and abscisic acid treatments upregulate SmHPPR transcription level
presence of phenylalanine results in up to 40fold increase in transcripts
UV-B radiation and hydrogen peroxide treatments downregulate SmHPPR transcription level
presence of phenylalanine results in up to 40fold increase in transcripts
presence of phenylalanine results in up to 40fold increase in transcripts
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Petersen, M.; Alfermann, A.W.
Two new enzymes of rosmarinic acid biosyntheses from cell cultures of Coleus blumei: hydroxyphenylpyruvate reductase and rosmarinic acid synthase
Z. Naturforsch. C
43
501-504
1988
Coleus scutellarioides
-
brenda
Husler, E.; Petersen, M.; Alfermann, A.W.
Hydroxyphenylpyruvate reductase from cell suspension cultures of Coleus blumei Benth
Z. Naturforsch. C
46
371-376
1991
Coleus scutellarioides
-
brenda
Petersen, M.; Husler E.; Meinhard J.; Karwatzki, B.; Gertlowski C.
The biosynthesis of rosmarinic acid in suspension cultures of Coleus blumei
Plant Cell Tissue Organ Cult.
38
171 - 179
1994
Coleus scutellarioides
-
brenda
Petersen, M.; Husler E.; Karwatzki, B.; Meinhard J.
Proposed biosynthetic pathway for rosmarinic acid in cell cultures of Coleus blumei benth
Planta
189
10-14
1993
Coleus scutellarioides
-
brenda
Kim, K.H.; Janiak, V.; Petersen, M.
Purification, cloning and functional expression of hydroxyphenylpyruvate reductase involved in rosmarinic acid biosynthesis in cell cultures of Coleus blumei
Plant Mol. Biol.
54
311-323
2004
Coleus scutellarioides (Q65CJ7)
brenda
Qian, J.; Guiping, L.; Xiujun, L.; Xincai, H.; Hongmei, L.
Influence of growth regulators and sucrose concentrations on growth and rosmarinic acid production in calli and suspension cultures of Coleus blumei
Nat. Prod. Res.
23
127-137
2009
Coleus scutellarioides
brenda
Xiao, Y.; Gao, S.; Di, P.; Chen, J.; Chen, W.; Zhang, L.
Methyl jasmonate dramatically enhances the accumulation of phenolic acids in Salvia miltiorrhiza hairy root cultures
Physiol. Plant.
137
1-9
2009
Salvia miltiorrhiza
brenda
Janiak, V.; Petersen, M.; Zentgraf, M.; Klebe, G.; Heine, A.
Structure and substrate docking of a hydroxy(phenyl)pyruvate reductase from the higher plant Coleus blumei Benth
Acta Crystallogr. Sect. D
66
593-603
2010
Coleus scutellarioides (Q65CJ7)
brenda
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)
brenda
Kim, Y.B.; Uddina, M.R.; Kim, Y.; Park, C.G.; Park, S.U.
Molecular cloning and characterization of tyrosine aminotransferase and hydroxyphenylpyruvate reductase, and rosmarinic acid accumulation in Scutellaria baicalensis
Nat. Prod. Commun.
9
1311-1314
2014
Scutellaria baicalensis
brenda
Ma, P.; Liu, J.; Zhang, C.; Liang, Z.
Regulation of water-soluble phenolic acid biosynthesis in Salvia miltiorrhiza Bunge
Appl. Biochem. Biotechnol.
170
1253-1262
2013
Salvia miltiorrhiza (A0A0A7RFJ3), Salvia miltiorrhiza
brenda
Battini, F.; Bernardi, R.; Turrini, A.; Agnolucci, M.; Giovannetti, M.
Rhizophagus intraradices or its associated bacteria affect gene expression of key enzymes involved in the rosmarinic acid biosynthetic pathway of basil
Mycorrhiza
26
699-707
2016
Ocimum basilicum var. purpurascens (A0A0A7DW92)
brenda
Dewanjee, S.; Gangopadhyay, M.; Das, U.; Sahu, R.; Khanra, R.
Enhanced rosmarinic acid biosynthesis in Solenostemon scutellarioides culture: a precursor-feeding strategy
Nat. Prod. Res.
28
1691-1698
2014
Coleus scutellarioides
brenda
Huecherig, S.; Petersen, M.
RNAi suppression and overexpression studies of hydroxyphenylpyruvate reductase (HPPR) and rosmarinic acid synthase (RAS) genes related to rosmarinic acid biosynthesis in hairy root cultures of Coleus blumei
Plant Cell Tissue Organ Cult.
113
375-385
2013
Coleus scutellarioides (Q65CJ7)
-
brenda
Barberini, S.; Savona, M.; Raffi, D.; Leonardi, M.; Pistelli, L.; Stochmal, A.; Vainstein, A.; Pistelli, L.; Ruffoni, B.
Molecular cloning of SoHPPR encoding a hydroxyphenylpyruvate reductase, and its expression in cell suspension cultures of Salvia officinalis
Plant Cell Tissue Organ Cult.
114
131-138
2013
Salvia officinalis (M1H6F7)
-
brenda
Lu, X.; Hao, L.; Wang, F.; Huang, C.
Molecular cloning, characterization and expression analysis of a gene encoding hydroxyphenylpyruvate reductase involved in rosmarinic acid biosynthesis pathway from Perilla frutescens
Proc. 2012 Int. Conf. Appl. Biotechnol.
251 LNEE
1807-1820
2014
Perilla frutescens (F8RGR8)
-
brenda
Xu, J.; Fang, X.; Li, C.; Zhao, Q.; Martin, C.; Chen, X.; Yang, L.
Characterization of Arabidopsis thaliana hydroxyphenylpyruvate reductases in the tyrosine conversion pathway
Front. Plant Sci.
9
1305
2018
Arabidopsis thaliana (Q9CA90), Arabidopsis thaliana (Q9LE33), Arabidopsis thaliana (A0A178WMD4), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q9LE33)
brenda
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