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Ligand D-phenyllactate

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for D-phenyllactate

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.8.3.17

(E)-cinnamoyl-CoA + (R)-phenyllactate = (E)-cinnamate + (R)-phenyllactoyl-CoA

637243

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In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.28

phenylpyruvate + NADH + H+ = (R)-3-phenyllactate + NAD+

0

-

Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Substrate (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.140

4-coumaroyl-CoA + D-phenyllactate = CoA + (R)-2-O-(4-coumaroyl)-3-phenyllactate

720787

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2.3.1.140

caffeoyl-CoA + D-phenyllactate = CoA + (R)-2-O-caffeoyl-3-phenyllactate

720787

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2.3.1.140

cinnamoyl-CoA + D-phenyllactate = CoA + (R)-2-O-cinnamoyl-3-phenyllactate

720787

-

2.3.1.140

3 entries

2.8.3.17

(E)-cinnamoyl-CoA + (R)-phenyllactate = (E)-cinnamate + (R)-phenyllactoyl-CoA

637243

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Product in Enzyme-catalyzed Reactions (16 results)

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Show Product (16 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.110

phenylpyruvate + NAD(P)H = D-phenyllactate + NAD(P)+

286312

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1.1.1.237

phenylpyruvate + NADPH + H+ = D-phenyllactate + NADP+

0

-

1.1.1.28

phenylpyruvate + NADH + H+ = (R)-3-phenyllactate + NAD+

0

-

1.1.1.28

phenylpyruvate + NADH + H+ = D-phenyllactate + NAD+

0

-

1.1.1.28

2 entries

1.1.1.345

phenylpyruvate + NADH + H+ = phenyl-D-lactate + NAD+

0

-

1.1.1.81

phenylpyruvate + NADPH + H+ = D-phenyllactate + NADP+

0

-

1.1.99.30

phenylpyruvate + H2 = (2R)-phenyllactate

0

-

1.1.99.30

phenylpyruvate + reduced benzyl viologen = (2R)-phenyllactate + oxidized benzyl viologen

0

-

1.1.99.30

phenylpyruvate + reduced carbamoylmethyl viologen = (2R)-phenyllactate + oxidized carbamoylmethyl viologen

0

-

1.1.99.30

phenylpyruvate + reduced cobalt sepulchrate = (2R)-phenyllactate + oxidized cobalt sepulchrate

0

-

1.1.99.30

phenylpyruvate + reduced indigocarmine = (2R)-phenyllactate + oxidized indigocarmine

0

-

1.1.99.30

phenylpyruvate + reduced kresyl violet = (2R)-phenyllactate + oxidized kresyl violet

0

-

1.1.99.30

phenylpyruvate + reduced meldolablue = (2R)-phenyllactate + oxidized meldolablue

0

-

1.1.99.30

phenylpyruvate + reduced methylene blue = (2R)-phenyllactate + oxidized methylene blue

0

-

1.1.99.30

phenylpyruvate + reduced phenosafranine = (2R)-phenyllactate + oxidized phenosafranine

0

-

1.1.99.30

phenylpyruvate + reduced safranine TH = (2R)-phenyllactate + oxidized safranine TH

0

-

1.1.99.30

10 entries

Inhibitor in Enzyme-catalyzed Reactions (2 results)

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Show Inhibitors (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.4.16.4

-

683148

-

3.4.17.8

-

683148

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Enzyme Kinetic Parameters

K_M Value (4 results)

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Show KM Value (4 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.110

0.083

-

-

286312

2.3.1.140

0.49

-

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

720787

2.3.1.140

1.346

-

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

720787

2.3.1.140

17.82

-

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

720787

2.3.1.140

3 entries

K_i Value (2 results)

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Show KI Value (2 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.4.16.4

17.8

-

substrate glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]sulfanyl]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine

683148

3.4.17.8

17.8

-

pH 7.5, 25°C

683148

References & Links

Literature References (4)

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Show Reference (4 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

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

637243

10849007

The involvement of coenzyme A esters in the dehydration of (R)-phenyllactate to (E)-cinnamate by Clostridium sporogenes

2000

Dickert, S.; Pierik, A.J.; Linder, D.; Buckel, W.

Eur. J. Biochem.

267

3874-3884

683148

17059224

Deacylation transition states of a bacterial DD-peptidase

2006

Adediran, S.A.; Kumar, I.; Pratt, R.F.

Biochemistry

45

13074-13082

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

Links to other databases for D-phenyllactate

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Show Links (1 entry)

ChEBI

PubChem