print visible entries

print all entries

Ligand 3-(4-hydroxyphenyl)lactate

Basic Ligand Information

Molecular Structure

close all tables

open all tables

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (3 results)

top print hide

Show Natural Substrate (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.237

3-(4-hydroxyphenyl)lactate + NAD+ = 4-hydroxyphenylpyruvate + NADH

286350, 286351, 286349

-

2.3.1.140

4-coumaroyl-CoA + 3-(4-hydroxyphenyl)lactate = CoA + 2-O-(4-coumaroyl)-3-(4-hydroxyphenyl)lactate

720636

-

2.3.1.140

caffeoyl-CoA + 3-(4-hydroxyphenyl)lactate = CoA + 2-O-caffeoyl-3-(4-hydroxyphenyl)lactate

720636

-

2.3.1.140

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (3 results)

top print hide

Show Natural Product (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.237

3-(4-hydroxyphenyl)pyruvate + NADH + H+ = 3-(4-hydroxyphenyl)lactate + NAD+

-

-

1.1.1.237

3-(4-hydroxyphenyl)pyruvate + NADPH + H+ = 3-(4-hydroxyphenyl)lactate + NADP+

-

-

1.1.1.237

4-hydroxyphenylpyruvate + NADPH + H+ = 4-hydroxyphenyllactate + NADP+

-

-

1.1.1.237

3 entries

Substrate in Enzyme-catalyzed Reactions (11 results)

top print hide

Show Substrate (11 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.110

p-hydroxyphenyllactate + NAD+ = p-hydroxyphenylpyruvate + NADH

285756

-

1.1.1.237

3-(4-hydroxyphenyl)lactate + NAD+ = 4-hydroxyphenylpyruvate + NADH

286350, 286351, 286349

-

1.1.3.15

DL-p-hydroxy-beta-phenyllactate + 2,6-dichlorophenolindophenol = (4-hydroxyphenyl)pyruvate + reduced 2,6-dichlorophenolindophenol

389701

-

2.3.1.140

3,4-dihydroxyphenylpropanoyl-CoA + 3-(4-hydroxyphenyl)lactate = CoA + 2-O-(3,4-dihydroxyphenylpropanoyl)-3-(4-hydroxyphenyl)lactate

756266

-

2.3.1.140

4-coumaroyl-CoA + 3-(4-hydroxyphenyl)lactate = CoA + 2-O-(4-coumaroyl)-3-(4-hydroxyphenyl)lactate

486321, 720787, 756266, 720636, 720789, 676710

-

2.3.1.140

4-hydroxyphenylpropanoyl-CoA + 3-(4-hydroxyphenyl)lactate = CoA + 2-O-(4-hydroxyphenylpropanoyl)-3-(4-hydroxyphenyl)lactate

756266

-

2.3.1.140

caffeoyl-CoA + 3-(4-hydroxyphenyl)lactate = CoA + 2-O-caffeoyl-3-(3,4-dihydroxyphenyl)lactate

720636

-

2.3.1.140

caffeoyl-CoA + 3-(4-hydroxyphenyl)lactate = CoA + 2-O-caffeoyl-3-(4-hydroxyphenyl)lactate

286352, 486319, 486321, 676710, 720787, 756266, 720636, 720789

-

2.3.1.140

cinnamoyl-CoA + 3-(4-hydroxyphenyl)lactate = CoA + 2-O-cinnamoyl-3-(4-hydroxyphenyl)lactate

720787, 720789

-

2.3.1.140

feruloyl-CoA + 3-(4-hydroxyphenyl)lactate = CoA + 2-O-feruloyl-3-(4-hydroxyphenyl)lactate

720787, 756266, 720789

-

2.3.1.140

sinapoyl-CoA + 3-(4-hydroxyphenyl)lactate = CoA + 2-O-sinapoyl-3-(4-hydroxyphenyl)lactate

720787

-

2.3.1.140

8 entries

Product in Enzyme-catalyzed Reactions (9 results)

top print hide

Show Product (9 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.237

3-(4-hydroxyphenyl)pyruvate + NADH + H+ = 3-(4-hydroxyphenyl)lactate + NAD+

-

-

1.1.1.237

3-(4-hydroxyphenyl)pyruvate + NADPH + H+ = 3-(4-hydroxyphenyl)lactate + NADP+

-

-

1.1.1.237

4-hydroxyphenylpyruvate + NADH = 3-(4-hydroxyphenyl)lactate + NAD+

286349, 286350, 286351

-

1.1.1.237

4-hydroxyphenylpyruvate + NADPH + H+ = 3-(4-hydroxyphenyl)lactate + NADP+

-

-

1.1.1.237

4-hydroxyphenylpyruvate + NADPH + H+ = 4-hydroxyphenyllactate + NADP+

-

-

1.1.1.237

5 entries

1.1.1.345

3-(4-hydroxyphenyl)-2-oxopropanoate + NADH + H+ = 2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD+

-

-

1.1.1.37

p-hydroxyphenylpyruvate + NADH + H+ = 2-hydroxy-3-(4-hydroxyphenyl)propanoate

-

-

1.1.1.81

4-hydroxyphenylpyruvate + NADPH + H+ = 3-(4-hydroxyphenyl)lactate + NADP+

-

-

1.1.1.96

4-hydroxyphenylpyruvate + NADH = 4-hydroxyphenyllactate + NAD+

287552, 287554

-

Inhibitor in Enzyme-catalyzed Reactions (6 results)

top print hide

Show Inhibitors (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.27

50% inhibition above 10 mM, competitive

395375

-

1.3.1.43

-

390802

-

1.5.1.34

0.058 mM, 50% inhibition

484979

-

1.5.1.34

0.071 mM, 50% inhibition

484979

-

1.5.1.34

2 entries

2.6.1.24

weak

639936

-

2.7.11.4

weak

640578

-

Enzyme Kinetic Parameters

K_M Value (15 results)

top print hide

Show KM Value (15 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.110

0.076

-

-

286312

1.1.1.110

1.77

-

-

285756

2.3.1.140

0.0169

-

with 4-coumaroyl-CoA, pH 7.0, 30°C, native crude enzyme

720636

2.3.1.140

0.0189

-

with 4-coumaroyl-CoA, pH 7.0, 30°C, crude recombinant His-tagged enzyme

720636

2.3.1.140

0.021

-

with 4-coumaroyl-CoA, pH 7.5, 30°C, recombinant AAT1

720789

2.3.1.140

0.025

-

pH 7.0, 30°C, with 4-coumaroyl-CoA, recombinant RAS

720787

2.3.1.140

0.049

-

with caffeoyl-CoA, pH 7.5, 30°C, recombinant AAT1

720789

2.3.1.140

0.074

-

with caffeoyl-CoA, pH 7.0, 30°C, native crude enzyme

720636

2.3.1.140

0.1565

-

with caffeoyl-CoA, pH 7.0, 30°C, crude recombinant His-tagged enzyme

720636

2.3.1.140

0.163

-

pH 7.0, 30°C, with caffeoyl-CoA, recombinant RAS

720787

2.3.1.140

0.17

-

-

486321

2.3.1.140

0.55

-

pH 7.0, 30°C, with cinnamoyl-CoA, recombinant RAS

720787

2.3.1.140

0.652

-

with cinnamoyl-CoA, pH 7.5, 30°C, recombinant AAT1

720789

2.3.1.140

0.672

-

with feruloyl-CoA, pH 7.5, 30°C, recombinant AAT1

720789

2.3.1.140

1.425

-

pH 7.0, 30°C, with feroyl-CoA, recombinant RAS

720787

1.1.1.110

2 entries

2.3.1.140

13 entries

References & Links

Literature References (21)

top print hide

Show Reference (21 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

285756

4384683

Indolelactate dehydrogenase from Clostridium sporogenes

1968

Jean, M.; DeMoss, R.D.

Can. J. Microbiol.

14

429-435

286312

-

Purification and properties of D-aromatic lactate dehydrogenase, an enzyme involved in the catabolism of the aromatic amino acids of Candida maltosa

1986

Bode, R.; Lippoldt, A.; Birnbaum, D.

Biochem. Physiol. Pflanz.

181

189-198

286349

-

Two new enzymes of rosmarinic acid biosyntheses from cell cultures of Coleus blumei: hydroxyphenylpyruvate reductase and rosmarinic acid synthase

1988

Petersen, M.; Alfermann, A.W.

Z. Naturforsch. C

43

501-504

286350

-

Hydroxyphenylpyruvate reductase from cell suspension cultures of Coleus blumei Benth

1991

Häusler, E.; Petersen, M.; Alfermann, A.W.

Z. Naturforsch. C

46

371-376

286351

-

The biosynthesis of rosmarinic acid in suspension cultures of Coleus blumei

1994

Petersen, M.; Häusler E.; Meinhard J.; Karwatzki, B.; Gertlowski C.

Plant Cell Tissue Organ Cult.

38

171 - 179

286352

-

Proposed biosynthetic pathway for rosmarinic acid in cell cultures of Coleus blumei benth

1993

Petersen, M.; Häusler E.; Karwatzki, B.; Meinhard J.

Planta

189

10-14

287552

6760790

A description of human aromatic alpha-keto acid reductase

1982

Donald, L.J.

Ann. Hum. Genet.

46

299-306

287554

5935348

Isolation and properties of aromatic alpha-keto acid reductase

1966

Zannoni, V.G.; Weber, W.W.

J. Biol. Chem.

241

1340-1344

389701

14492912

L-alpha-Hydroxy acid oxidases of hog renal cortex

1962

Robinson, J.C.; Keay, L.; Molinari, R.; Sizer, I.W.

J. Biol. Chem.

237

2001-2010

390802

11790331

Cyclohexadienyl dehydrogenase from Pseudomonas stutzeri exemplifies a widespread type of tyrosine-pathway dehydrogenase in the TyrA protein family

2000

Xie, G.; Bonner, C.A.; Jensen, R.A.

Comp. Biochem. Physiol. C

125

65-83

395375

7118918

Blue color, metal content, and substrate binding in 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874

1982

Lindstedt, S.; Rundgren, M.

J. Biol. Chem.

257

11922-11931

484979

6422988

Potent inhibitory effects of tyrosine metabolites on dihydropteridine reductase from human and sheep liver

1984

Shen, R.S.

Biochim. Biophys. Acta

785

181-185

486319

-

Two new enzymes of rosmarinic acid biosynthesis from cell cultures of Coleus blumei: Hydroxyphenylpyruvate reductase and rosmarinic acid synthase

1988

Petersen, M.; Alfermann, A.W.

Z. Naturforsch. C

43c

501-504

486321

-

Characterization of rosmarinic acid synthase from cell cultures of Coleus blumei

1991

Petersen, M.S.

Phytochemistry

30

2877-2881

639936

4381052

Purification and properties of halogenated tyrosine and thyroid hormone transaminase from rat kidney mitochondria

1967

Nakano, M.

J. Biol. Chem.

242

73-81

640578

6721502

Clofibric acid, phenylpyruvate, and dichloroacetate inhibition of branched-chain alpha-ketoacid dehydrogenase kinase in vitro and in perfused rat heart

1984

Paxton, R.; Harris, R.A.

Arch. Biochem. Biophys.

231

58-66

676710

17047986

Rosmarinic acid synthase is a new member of the superfamily of BAHD acyltransferases

2006

Berger, A.; Meinhard, J.; Petersen, M.

Planta

224

1503-1510

720636

21354582

Cloning and characterisation of rosmarinic acid synthase from Melissa officinalis L.

2011

Weitzel, C.; Petersen, M.

Phytochemistry

72

572-578

720787

21318289

Distinct substrate specificities and unusual substrate flexibilities of two hydroxycinnamoyltransferases, rosmarinic acid synthase and hydroxycinnamoyl-CoA:shikimate hydroxycinnamoyl-transferase, from Coleus blumei Benth.

2011

Sander, M.; Petersen, M.

Planta

233

1157-1171

720789

21424826

Substrate promiscuity of a rosmarinic acid synthase from lavender (Lavandula angustifolia L.)

2011

Landmann, C.; Huecherig, S.; Fink, B.; Hoffmann, T.; Dittlein, D.; Coiner, H.A.; Schwab, W.

Planta

234

305-320

756266

26667131

Synthesis of rosmarinic acid analogues in Escherichia coli

2016

Zhuang, Y.; Jiang, J.; Bi, H.; Yin, H.; Liu, S.; Liu, T.

Biotechnol. Lett.

38

619-627

Links to other databases for 3-(4-hydroxyphenyl)lactate

top print hide

Show Links (1 entry)

ChEBI

PubChem

-