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Ligand cyclo-D-Trp-L-Pro

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (6 results)

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Show Substrate (6 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.106

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

721814

-

2.5.1.106

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

737520

-

2.5.1.106

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

723120, 721814

-

2.5.1.109

dimethylallyl diphosphate + cyclo-D-Trp-L-Pro = ?

758707

-

2.5.1.109

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

737541

-

2.5.1.109

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

721391

-

2.5.1.106

3 entries

2.5.1.109

3 entries

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

2.5.1.106

0.21

-

mutant Y205N, pH 7.5, 37°C

737520

2.5.1.106

0.41

-

mutant Y205L, pH 7.5, 37°C

737520

2.5.1.109

0.027

-

37°C, pH 7.5

721391

2.5.1.109

0.027

-

pH 7.5, 37°C

721391

2.5.1.106

2 entries

2.5.1.109

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

2.5.1.106

0.4

-

mutant Y205N, pH 7.5, 37°C

737520

2.5.1.106

0.46

-

mutant Y205L, pH 7.5, 37°C

737520

2.5.1.109

2.906

-

37°C, pH 7.5

721391

2.5.1.109

2.906

-

pH 7.5, 37°C

721391

2.5.1.106

2 entries

2.5.1.109

2 entries

References & Links

Literature References (6)

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Show Reference (6 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

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

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

737520

27311563

Saturation mutagenesis on Tyr205 of the cyclic dipeptide C2-prenyltransferase FtmPT1 results in mutants with strongly increased C3-prenylating activity

2016

Zhou, K.; Zhao, W.; Liu, X.; Li, S.

Appl. Microbiol. Biotechnol.

100

943-9953

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

758707

32185409

Reinvestigation of the substrate specificity of a reverse prenyltransferase NotF from Aspergillus sp. MF297-2

2020

Yang, K.; Li, S.M.; Liu, X.; Fan, A.

Arch. Microbiol.

202

1419-1424

Links to other databases for cyclo-D-Trp-L-Pro

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Show Links (1 entry)

ChEBI

PubChem

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