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3,4-dihydroxyphenylpyruvate + NADH + H+
3-(3,4-dihydroxyphenyl)lactate + NAD+
3,4-dihydroxyphenylpyruvate + NADPH + H+
3,4-dihydroxyphenyllactate + NADP+
Coleus scutellarioides
-
-
-
?
3,4-dihydroxyphenylpyruvate + NADPH + H+
3-(3,4-dihydroxyphenyl)lactate + NADP+
Coleus scutellarioides
-
-
-
r
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH + H+
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
(R)-3-(4-hydroxyphenyl)lactate + NADP+
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
3-methoxy-4-hydroxyphenylpyruvate + NADH + H+
3-(3-methoxy-4-hydroxyphenyl)lactate + NAD+
Coleus scutellarioides
-
-
-
-
?
4-hydroxyphenylpyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
4-hydroxyphenylpyruvate + NADPH + H+
D-(4-hydroxyphenyl)lactate + NADP+
beta-phenylpyruvate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
Coleus scutellarioides
-
-
-
-
r
glyoxylate + NADPH + H+
glycolate + NADP+
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
phenylpyruvate + NADPH + H+
D-phenyllactate + NADP+
phenylpyruvate + NADPH + H+
phenyllactate + NADP+
additional information
?
-
3,4-dihydroxyphenylpyruvate + NADH + H+
3-(3,4-dihydroxyphenyl)lactate + NAD+
Coleus scutellarioides
-
-
-
?
3,4-dihydroxyphenylpyruvate + NADH + H+
3-(3,4-dihydroxyphenyl)lactate + NAD+
Coleus scutellarioides
-
-
-
r
3,4-dihydroxyphenylpyruvate + NADH + H+
3-(3,4-dihydroxyphenyl)lactate + NAD+
Coleus scutellarioides
-
-
-
r
3,4-dihydroxyphenylpyruvate + NADH + H+
3-(3,4-dihydroxyphenyl)lactate + NAD+
Coleus scutellarioides
-
-
-
r
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH + H+
Coleus scutellarioides
-
-
-
-
?
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH + H+
Coleus scutellarioides
-
biosynthesis of rosmarinic acid
-
?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Coleus scutellarioides
-
-
-
?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Coleus scutellarioides
-
-
-
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+
(R)-3-(4-hydroxyphenyl)lactate + NADP+
-
-
-
r
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
(R)-3-(4-hydroxyphenyl)lactate + NADP+
best substrate
-
-
r
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
(R)-3-(4-hydroxyphenyl)lactate + NADP+
-
-
-
r
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
(R)-3-(4-hydroxyphenyl)lactate + NADP+
best substrate
-
-
r
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
Coleus scutellarioides
-
-
-
?
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
Coleus scutellarioides
substrate bindiing structure, docking study, overview
-
-
r
4-hydroxyphenylpyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Coleus scutellarioides
-
-
-
?
4-hydroxyphenylpyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Coleus scutellarioides
-
-
-
r
4-hydroxyphenylpyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Coleus scutellarioides
-
-
-
r
4-hydroxyphenylpyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
-
-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
-
-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
Coleus scutellarioides
-
-
-
-
r
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
Coleus scutellarioides
-
-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
Coleus scutellarioides
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+
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
reaction of EC 1.1.1.81
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
reaction of EC 1.1.1.81
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
?
phenylpyruvate + NADPH + H+
D-phenyllactate + NADP+
-
-
-
?
phenylpyruvate + NADPH + H+
D-phenyllactate + 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
-
-
?
phenylpyruvate + NADPH + H+
phenyllactate + NADP+
-
-
-
?
phenylpyruvate + NADPH + H+
phenyllactate + NADP+
-
-
-
?
additional information
?
-
isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
-
-
-
additional information
?
-
isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
-
-
-
additional information
?
-
isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
-
-
-
additional information
?
-
-
isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
-
-
-
additional information
?
-
isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
-
-
-
additional information
?
-
Coleus scutellarioides
-
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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3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH + H+
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
(R)-3-(4-hydroxyphenyl)lactate + NADP+
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
Coleus scutellarioides
-
-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH + H+
Coleus scutellarioides
-
-
-
-
?
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH + H+
Coleus scutellarioides
-
biosynthesis of rosmarinic acid
-
?
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
Coleus scutellarioides
-
-
-
?
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+
(R)-3-(4-hydroxyphenyl)lactate + NADP+
-
-
-
r
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
(R)-3-(4-hydroxyphenyl)lactate + NADP+
-
-
-
r
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
Coleus scutellarioides
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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evolution
Coleus scutellarioides
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
Coleus scutellarioides
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
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
Coleus scutellarioides
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
Coleus scutellarioides
-
the key enzyme is involved in rosmarinic acid biosynthesis
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
-
Wickerhamia fluorescens efficiently converts phenylalanine and phenylpyruvate to D-phenyllactate. These compounds up-regulate the transcription of enzyme gene pprA
-
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
-
additional information
Coleus scutellarioides
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
homology-based structural modeling
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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
Coleus scutellarioides
-
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
Coleus scutellarioides
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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expression in Escherichia coli
expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS
Coleus scutellarioides
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
Coleus scutellarioides
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
expression in Escherichia coli
Coleus scutellarioides
expression in Escherichia coli
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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
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