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Information on EC 1.1.1.237 - hydroxyphenylpyruvate reductase
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1.1.1.237 hydroxyphenylpyruvate reductaseIUBMB 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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Word Map
- 1.1.1.237
-
rosmarinic
-
coronary
- clopidogrel
-
post-treatment
- miltiorrhiza
-
adp-induced
- salvia
-
percutaneous
-
aggregometry
- aspirin
-
verifynow
-
antiplatelet
- lamiaceae
-
p-selectin
-
coleus
-
4-hydroxyphenyllactic
- blumei
- cilostazol
-
lithospermic
- bunge
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
hppr, hydroxyphenylpyruvate reductase, 4-hydroxyphenylpyruvate reductase, hydroxy(phenyl)pyruvate reductase, h(p)pr, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-hydroxyphenylpyruvate reductase
HPPR
Ppr
pprA
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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)
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
KEGG
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxyphenylpyruvate + NADH + H+
3-(3,4-dihydroxyphenyl)lactate + NAD+
-
-
r
3,4-dihydroxyphenylpyruvate + NADPH + H+
3,4-dihydroxyphenyllactate + NADP+
-
-
?
3,4-dihydroxyphenylpyruvate + NADPH + H+
3-(3,4-dihydroxyphenyl)lactate + NADP+
-
-
r
3-methoxy-4-hydroxyphenylpyruvate + NADH
3-(3-methoxy-4-hydroxyphenyl)lactate + NAD+
-
-
-
?
5-hydroxyphenylpyruvate + NADPH + H+
5-hydroxyphenyllactate + NADP+
-
-
-
r
3,4-dihydroxyphenylpyruvate + NADH
3-(3,4-dihydroxyphenyl)lactate + NAD+
-
-
-
?
3,4-dihydroxyphenylpyruvate + NADH
3-(3,4-dihydroxyphenyl)lactate + NAD+
-
-
-
r
3,4-dihydroxyphenylpyruvate + NADH
3-(3,4-dihydroxyphenyl)lactate + NAD+
-
-
-
r
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH
-
-
-
?
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH
-
biosynthesis of rosmarinic acid
-
?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
-
-
?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
-
-
r
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
-
-
?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
-
-
r
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
-
-
?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
-
-
?
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
-
-
?
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
substrate bindiing structure, docking study, overview
-
r
4-hydroxyphenylpyruvate + NADH
3-(4-hydroxyphenyl)lactate + NAD+
-
-
-
?
4-hydroxyphenylpyruvate + NADH
3-(4-hydroxyphenyl)lactate + NAD+
-
-
-
r
4-hydroxyphenylpyruvate + NADH
3-(4-hydroxyphenyl)lactate + NAD+
-
-
-
r
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
-
-
-
r
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
the enzyme is involved in L-serine biosynthesis and rosmarinic acid biosynthesis
-
?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
-
part of the metabolic pathway leading to rosmarinic acid and lithospermic acid B
-
?
4-hydroxyphenylpyruvate + NADPH + H+
D-(4-hydroxyphenyl)lactate + NADP+
-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
D-(4-hydroxyphenyl)lactate + NADP+
-
-
?
phenylpyruvate + NADPH + H+
D-phenyllactate + NADP+
more than 99.9% D-isomer, L-isomer below limits of detection
-
?
phenylpyruvate + NADPH + H+
D-phenyllactate + NADP+
more than 99.9% D-isomer, L-isomer below limits of detection
-
?
additional information
?
-
-
rosmarinic acid biosynthetic pathway is regulated by interactions of several enzymes necessary for biosynthesis including HPPR
-
?
additional information
?
-
no substrates: pyruvate, oxaloacetate or benzoylformate
-
?
additional information
?
-
no substrates: pyruvate, oxaloacetate or benzoylformate
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
-
-
-
?
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH
-
-
-
-
?
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH
-
biosynthesis of rosmarinic acid
-
?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
-
-
-
?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
-
-
-
r
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
-
-
-
?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
-
-
-
?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
-
-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
the enzyme is involved in L-serine biosynthesis and rosmarinic acid biosynthesis
-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
-
part of the metabolic pathway leading to rosmarinic acid and lithospermic acid B
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
NADH as well as NADPH can serve as the electron donor
-
additional information
-
NADH as well as NADPH can serve as the electron donor
-
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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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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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
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
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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
metabolism
HPPR is a key enzyme involved in the rosmarinic acid biosynthesis via the tyrosine-dependent pahtway
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 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
the key enzyme is involved in biosynthesis of rosmarinic acid via the tyrosine-derived pathway
metabolism
-
the key enzyme is involved in biosynthesis of rosmarinic acid via the tyrosine-derived pathway, overview
metabolism
-
the key enzyme is involved in rosmarinic acid biosynthesis
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
-
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
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)
A0A2G9FWG3_9LAMI
316
0
34584
TrEMBL
Mitochondrion (Reliability: 5)
A0A2R4SEK7_MENSP
313
0
34156
TrEMBL
other Location (Reliability: 3)
A0A2R4SEI0_MENAQ
313
0
34150
TrEMBL
other Location (Reliability: 3)
A0A2S1B6P7_MENLO
313
0
34056
TrEMBL
other Location (Reliability: 2)
A0A5B7BD14_DAVIN
123
0
13769
TrEMBL
Mitochondrion (Reliability: 5)
A0A0A7RFJ3_SALMI
313
0
34228
TrEMBL
other Location (Reliability: 3)
A0A2R4SEK0_MENPI
313
0
34156
TrEMBL
other Location (Reliability: 3)
A0A5B7C2F6_DAVIN
313
0
34174
TrEMBL
other Location (Reliability: 2)
A0A0A7DW92_OCIBA
204
0
22055
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34113
34113
2 * 34113, sequence calculation and crystal structure
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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
-
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 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
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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
Plectranthus scutellarioides
-
brenda
Häusler, E.; Petersen, M.; Alfermann, A.W.
Hydroxyphenylpyruvate reductase from cell suspension cultures of Coleus blumei Benth
Z. Naturforsch. C
46
371-376
1991
Plectranthus scutellarioides
-
brenda
Petersen, M.; Häusler 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
Plectranthus scutellarioides
-
brenda
Petersen, M.; Häusler E.; Karwatzki, B.; Meinhard J.
Proposed biosynthetic pathway for rosmarinic acid in cell cultures of Coleus blumei benth
Planta
189
10-14
1993
Plectranthus scutellarioides
-
brenda
Kim, K.H.; Janiak, V.; Petersen, M.
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Plectranthus scutellarioides (Q65CJ7), Plectranthus scutellarioides
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Qian, J.; Guiping, L.; Xiujun, L.; Xincai, H.; Hongmei, L.
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Plectranthus scutellarioides
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Xiao, Y.; Gao, S.; Di, P.; Chen, J.; Chen, W.; Zhang, L.
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Salvia miltiorrhiza
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Plectranthus scutellarioides (Q65CJ7), Plectranthus scutellarioides
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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
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Wickerhamia fluorescens (F1T2J9), Wickerhamia fluorescens TK1 (F1T2J9)
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Kim, Y.B.; Uddina, M.R.; Kim, Y.; Park, C.G.; Park, S.U.
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Salvia miltiorrhiza (A0A0A7RFJ3), Salvia miltiorrhiza
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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
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Ocimum basilicum var. purpurascens (A0A0A7DW92)
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Dewanjee, S.; Gangopadhyay, M.; Das, U.; Sahu, R.; Khanra, R.
Enhanced rosmarinic acid biosynthesis in Solenostemon scutellarioides culture: a precursor-feeding strategy
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Plectranthus scutellarioides
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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.
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Plectranthus scutellarioides (Q65CJ7)
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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
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Salvia officinalis (M1H6F7)
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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
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Perilla frutescens (F8RGR8)
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