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3,4-dihydroxyphenylpyruvate + NADH
3-(3,4-dihydroxyphenyl)lactate + NAD+
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-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
3-methoxy-4-hydroxyphenylpyruvate + NADH
3-(3-methoxy-4-hydroxyphenyl)lactate + NAD+
-
-
-
-
?
4-hydroxyphenylpyruvate + NADH
3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + NADP+
4-hydroxyphenylpyruvate + NADPH + H+
D-(4-hydroxyphenyl)lactate + NADP+
glyoxylate + NADPH + H+
glycolate + NADP+
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
phenylpyruvate + NADPH + H+
D-phenyllactate + NADP+
additional information
?
-
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+
-
-
-
?
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+
-
-
-
?
glyoxylate + NADPH + H+

glycolate + NADP+
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
hydroxypyruvate + NADH + H+

D-glycerate + NAD+
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
?
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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3-(4-hydroxyphenyl)lactate + NAD+
4-hydroxyphenylpyruvate + NADH
3-(4-hydroxyphenyl)pyruvate + NADH + H+
3-(4-hydroxyphenyl)lactate + NAD+
3-(4-hydroxyphenyl)pyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
-
-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
4-hydroxyphenyllactate + 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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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

-
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
-
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
-
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
additional information
homology-based structural modeling
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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
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.
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
Plectranthus scutellarioides, Plectranthus 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
Plectranthus 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
Plectranthus scutellarioides, Plectranthus 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
Plectranthus 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
Plectranthus 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