print visible entries

print all entries

Ligand dimethylallyl phosphate

Basic Ligand Information

Molecular Structure

close all tables

open all tables

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

top print hide

Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.129

dimethylallyl phosphate + FMNH2 = prenylated FMNH2 + phosphate

734780, 758698, 759056

6qli, 3D-view

2.5.1.129

dimethylallyl phosphate + FMNH2 = prenylated FMNH2 + phosphate

734780, 758698, 759056

6qll, 3D-view

2.5.1.129

dimethylallyl phosphate + FMNH2 = prenylated FMNH2 + phosphate

734780, 758698, 759056

7km3, 3D-view

2.5.1.129

3 entries

2.7.4.26

ATP + dimethylallyl phosphate = ADP + dimethylallyl diphosphate

739681, 739544

-

Substrate in Enzyme-catalyzed Reactions (5 results)

top print hide

Show Substrate (5 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.106

dimethylallylphosphate + cyclo-L-5-hydroxytryptophan-L-proline = diphosphate + (3S,8aS)-3-[[5-hydroxy-4-(3-methylbut-2-en-1-yl)-2,3-dihydro-1H-indol-3-yl]methyl]hexahydropyrrolo[1,2-a]pyrazine-1,4-dione

724761

-

2.5.1.129

dimethylallyl phosphate + FMNH2 = prenylated FMNH2 + phosphate

734780, 758698, 759056

6qli, 3D-view

2.5.1.129

dimethylallyl phosphate + FMNH2 = prenylated FMNH2 + phosphate

734780, 758698, 759056

6qll, 3D-view

2.5.1.129

dimethylallyl phosphate + FMNH2 = prenylated FMNH2 + phosphate

734780, 758698, 759056

7km3, 3D-view

2.5.1.129

3 entries

2.7.4.26

ATP + dimethylallyl phosphate = ADP + dimethylallyl diphosphate

760886, 739681, 739544, 717243

-

Product in Enzyme-catalyzed Reactions (2 results)

top print hide

Show Product (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.4.26

ATP + dimethyl allylalcohol = ADP + dimethylallyl phosphate

0

-

2.7.4.26

ATP + dimethylallyl alcohol = ADP + dimethylallyl phosphate

0

-

2.7.4.26

2 entries

3D Structure of Enzyme-Ligand-Complex (PDB) (6 results)

top print hide

Show 3D Structure of Enzyme-Ligand-Complex (PDB) (6 entries)

EC NUMBER

ENZYME 3D STRUCTURE

2.5.1.129

6qli, 3D-view

2.5.1.129

6qll, 3D-view

2.5.1.129

7km3, 3D-view

2.5.1.129

6qli, 3D-view

2.5.1.129

6qll, 3D-view

2.5.1.129

7km3, 3D-view

2.5.1.129

6 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (4 results)

top print hide

Show Turnover Number (4 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.7.4.26

2.7

-

pH and temperature not specified in the publication

739544

2.7.4.26

11.3

-

pH 7.5, 37°C

717243

2.7.4.26

32

-

pH 8.0, 30°C

760886

2.7.4.26

34

-

pH 7.5, 37°C

717243

2.7.4.26

4 entries

K_M Value (4 results)

top print hide

Show KM Value (4 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.7.4.26

0.033

-

pH and temperature not specified in the publication

739544

2.7.4.26

0.0432

-

pH 7.5, 37°C

717243

2.7.4.26

0.14

-

pH 8.0, 30°C

760886

2.7.4.26

0.174

-

pH 7.5, 37°C

717243

2.7.4.26

4 entries

References & Links

Literature References (8)

top print hide

Show Reference (8 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

717243

19928876

Characterization of thermophilic archaeal isopentenyl phosphate kinases.

2010

Chen, M.; Poulter, C.D.

Biochemistry

49

207-217

724761

24014462

Potential rearrangements in the reaction catalyzed by the indole prenyltransferase FtmPT1

2013

Mahmoodi, N.; Tanner, M.E.

ChemBioChem

14

2029-2037

734780

26083743

UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis

2015

White, M.D.; Payne, K.A.; Fisher, K.; Marshall, S.A.; Parker, D.; Rattray, N.J.; Trivedi, D.K.; Goodacre, R.; Rigby, S.E.; Scrutton, N.S.; Hay, S.; Leys, D.

Nature

522

502-506

739544

26216978

Orthologs of the archaeal isopentenyl phosphate kinase regulate terpenoid production in plants

2015

Henry, L.K.; Gutensohn, M.; Thomas, S.T.; Noel, J.P.; Dudareva, N.

Proc. Natl. Acad. Sci. USA

112

10050-10055

739681

27052337

Improving the catalytic activity of isopentenyl phosphate kinase through protein coevolution analysis

2016

Liu, Y.; Yan, Z.; Lu, X.; Xiao, D.; Jiang, H.

Sci. Rep.

6

24117

758698

28754323

The UbiX-UbiD system The biosynthesis and use of prenylated flavin (prFMN)

2017

Marshall, S.A.; Payne, K.A.P.; Leys, D.

Arch. Biochem. Biophys.

632

209-221

759056

30136768

Ligand-driven conformational dynamics influences selectivity of UbiX

2018

Zaczek, S.; Kowalska, J.; Dybala-Defratyka, A.

ChemBioChem

19

2403-2409

760886

30998839

Probing the substrate promiscuity of isopentenyl phosphate kinase as a platform for hemiterpene analogue production

2019

Lund, S.; Courtney, T.; Williams, G.J.

ChemBioChem

20

2217-2221

Links to other databases for dimethylallyl phosphate

top print hide

Show Links (1 entry)

ChEBI

PubChem