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Enzyme Nomenclature
Information on EC 1.1.1.237 - hydroxyphenylpyruvate reductase
for references in articles please use BRENDA:EC1.1.1.237
Word Map on EC 1.1.1.237
- 1.1.1.237
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coronary
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rosmarinic
- clopidogrel
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post-treatment
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adp-induced
- salvia
- miltiorrhiza
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percutaneous
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aggregometry
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antiplatelet
- aspirin
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verifynow
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p-selectin
- lamiaceae
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4-hydroxylase
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lithospermic
- blumei
- cilostazol
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stenting
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coleus
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.1.1.237
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RECOMMENDED NAME
GeneOntology No.
hydroxyphenylpyruvate reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-(4-hydroxyphenyl)lactate + NAD+ = 3-(4-hydroxyphenyl)pyruvate + NADH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
117590-77-9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv. Tigullio, a commercial cultivar of sweet basil
UniProt
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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
HPPR 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
metabolism
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the key enzyme is involved in biosynthesis of rosmarinic acid via the tyrosine-derived pathway, 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
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the key enzyme is involved in rosmarinic acid biosynthesis
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
hydroxyphenylpyruvate reductase is involved in rosmarinic acid biosynthesis via the tyrosine pathway
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
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Wickerhamia fluorescens efficiently converts phenylalanine and phenylpyruvate to D-phenyllactate. These compounds up-regulate the transcription of enzyme gene pprA
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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
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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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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+
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r
3,4-dihydroxyphenylpyruvate + NADPH + H+
3,4-dihydroxyphenyllactate + NADP+
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-
?
3,4-dihydroxyphenylpyruvate + NADPH + H+
3-(3,4-dihydroxyphenyl)lactate + NADP+
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-
-
r
3-methoxy-4-hydroxyphenylpyruvate + NADH
3-(3-methoxy-4-hydroxyphenyl)lactate + NAD+
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-
-
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?
3,4-dihydroxyphenylpyruvate + NADH
3-(3,4-dihydroxyphenyl)lactate + NAD+
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?
3,4-dihydroxyphenylpyruvate + NADH
3-(3,4-dihydroxyphenyl)lactate + NAD+
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-
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r
3,4-dihydroxyphenylpyruvate + NADH
3-(3,4-dihydroxyphenyl)lactate + NAD+
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r
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH
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?
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH
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biosynthesis of rosmarinic acid
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?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
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?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
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r
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
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?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
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?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
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?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
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r
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
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?
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
substrate bindiing structure, docking study, overview
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r
4-hydroxyphenylpyruvate + NADH
3-(4-hydroxyphenyl)lactate + NAD+
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?
4-hydroxyphenylpyruvate + NADH
3-(4-hydroxyphenyl)lactate + NAD+
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r
4-hydroxyphenylpyruvate + NADH
3-(4-hydroxyphenyl)lactate + NAD+
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r
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
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part of the metabolic pathway leading to rosmarinic acid and lithospermic acid B
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?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
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?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
the enzyme is involved in L-serine biosynthesis and rosmarinic acid biosynthesis
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?
4-hydroxyphenylpyruvate + NADPH + H+
D-(4-hydroxyphenyl)lactate + NADP+
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?
4-hydroxyphenylpyruvate + NADPH + H+
D-(4-hydroxyphenyl)lactate + NADP+
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?
phenylpyruvate + NADPH + H+
D-phenyllactate + NADP+
more than 99.9% D-isomer, L-isomer below limits of detection
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?
phenylpyruvate + NADPH + H+
D-phenyllactate + NADP+
more than 99.9% D-isomer, L-isomer below limits of detection
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?
additional information
?
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rosmarinic acid biosynthetic pathway is regulated by interactions of several enzymes necessary for biosynthesis including HPPR
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additional information
?
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no substrates: pyruvate, oxaloacetate or benzoylformate
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additional information
?
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no substrates: pyruvate, oxaloacetate or benzoylformate
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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+
Q65CJ7
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?
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH
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?
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH
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biosynthesis of rosmarinic acid
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?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
A0A0A7DW92
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?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
F8RGR8
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r
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
A0A0A7RFJ3
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?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
M1H6F7
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?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Q65CJ7
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?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
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part of the metabolic pathway leading to rosmarinic acid and lithospermic acid B
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?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
Q65CJ7
the enzyme is involved in L-serine biosynthesis and rosmarinic acid biosynthesis
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?
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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
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additional information
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NADH as well as NADPH can serve as the electron donor
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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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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additional information
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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
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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
hig enzyme activity and rosmarinic acid content, transcript expression level during cell suspension culture
additional information
plants inoculated with bacteria, and mycorrhizal plants
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
additional information
the enzyme gene expression is the highest in stem, the second in root, and lowest in leaf
additional information
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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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34113
34113
2 * 34113, sequence calculation and crystal structure
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SUBUNITS
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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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
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.237)
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