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Ligand cyclo-L-Trp-L-Leu

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

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

2.3.2.B16

L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu = tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)

0

-

Substrate in Enzyme-catalyzed Reactions (7 results)

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Show Substrate (7 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.15.13

cyclo(L-leucyl-L-tryptophanyl) + reduced ferredoxin + O2 = ? + oxidized ferredoxin + H2O

721623

-

2.5.1.1

geranyl diphosphate + (3S,6S)-3-(1H-indol-3-ylmethyl)-6-(2-methylpropyl)piperazine-2,5-dione = (3S,6S)-3-([6-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-1H-indol-3-yl]methyl)-6-(2-methylpropyl)piperazine-2,5-dione + (3S,6S)-3-([7-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-1H-indol-3-yl]methyl)-6-(2-methylpropyl)piperazine-2,5-dione + diphosphate

738051

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2.5.1.106

dimethylallyl diphosphate + cyclo-(L-Trp-L-Leu) = diphosphate + cyclo-(D-2-dimethylallyl-Trp-L-Leu)

723120, 721814

-

2.5.1.109

dimethylallyl diphosphate + cyclo-L-Trp-L-Leu = diphosphate + 7-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Leu

737541

-

2.5.1.109

dimethylallyl diphosphate + cyclo-L-Trp-L-Leu = diphosphate + cyclo-[2-(2-methylbut-3-en-2-yl)-L-Trp]-L-Leu

721391

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2.5.1.34

dimethylallyl diphosphate + cyclo-L-Trp-L-Leu = diphosphate + 4-(3-methylbut-2-enyl)-cyclo-L-Trp-L-Leu

737544, 758673

-

2.5.1.34

dimethylallyl diphosphate + cyclo-L-tryptophan-L-leucine = diphosphate + cyclo-L-4-dimethylallyltryptophan-L-leucine

701949

-

2.5.1.109

2 entries

2.5.1.34

2 entries

Product in Enzyme-catalyzed Reactions (1 result)

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Show Product (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.2.B16

L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu = tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)

0

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (4 results)

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Show Turnover Number (4 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.5.1.109

0.014

-

37°C, pH 7.5

721391

2.5.1.109

0.014

-

pH 7.5, 37°C

721391

2.5.1.34

0.0017

-

-

701949

2.5.1.34

0.093

-

mutant enzyme R244Y, pH 7.5, 37°C

758673

2.5.1.109

2 entries

2.5.1.34

2 entries

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

2.5.1.109

0.106

-

37°C, pH 7.5

721391

2.5.1.109

0.106

-

pH 7.5, 37°C

721391

2.5.1.34

0.14

-

-

701949

2.5.1.34

0.42

-

mutant enzyme R244Y, pH 7.5, 37°C

758673

2.5.1.109

2 entries

2.5.1.34

2 entries

References & Links

Literature References (9)

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Show Reference (9 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

701949

19277607

Increasing structure diversity of prenylated diketopiperazine derivatives by using a 4-dimethylallyltryptophan synthase

2009

Steffan, N.; Li, S.M.

Arch. Microbiol.

191

461-466

721391

22660767

Identification of a brevianamide F reverse prenyltransferase BrePT from Aspergillus versicolor with a broad substrate specificity towards tryptophan-containing cyclic dipeptides

2013

Yin, S.; Yu, X.; Wang, Q.; Liu, X.Q.; Li, S.M.

Appl. Microbiol. Biotechnol.

97

1649-1660

721623

20690619

Structural and biochemical characterization of the cytochrome P450 CypX (CYP134A1) from Bacillus subtilis: a cyclo-L-leucyl-L-leucyl dipeptide oxidase

2010

Cryle, M.J.; Bell, S.G.; Schlichting, I.

Biochemistry

49

7282-7296

721814

22617493

Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides

2012

Wollinsky, B.; Ludwig, L.; Hamacher, A.; Yu, X.; Kassack, M.U.; Li, S.M.

Bioorg. Med. Chem. Lett.

22

3866-3869

723120

16000710

Overproduction, purification and characterization of FtmPT1, a brevianamide F prenyltransferase from Aspergillus fumigatus

2005

Grundmann, A.; Li, S.M.

Microbiology

151

2199-2207

737541

25125042

C7-prenylation of tryptophanyl and O-prenylation of tyrosyl residues in dipeptides by an Aspergillus terreus prenyltransferase

2015

Wunsch, C.; Zou, H.X.; Linne, U.; Li, S.M.

Appl. Microbiol. Biotechnol.

99

1719-1730

737544

26227408

Impacts and perspectives of prenyltransferases of the DMATS superfamily for use in biotechnology

2015

Fan, A.; Winkelblech, J.; Li, S.M.

Appl. Microbiol. Biotechnol.

99

7399-7415

738051

24014429

Geranylation of cyclic dipeptides by the dimethylallyl transferase AnaPT resulting in a shift of prenylation position on the indole ring

2013

Pockrandt, D.; Li, S.M.

ChemBioChem

14

2023-2028

758673

26875876

Saturation mutagenesis on Arg244 of the tryptophan C4-prenyltransferase FgaPT2 leads to enhanced catalytic ability and different preferences for tryptophan-containing cyclic dipeptides

2016

Fan, A.; Li, S.M.

Appl. Microbiol. Biotechnol.

100

5389-5399

Links to other databases for cyclo-L-Trp-L-Leu

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Show Links (1 entry)

ChEBI

PubChem

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