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Ligand benzyl diphosphate

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

2.5.1.122

benzyl diphosphate + 4-amino-L-phenylalanine = diphosphate + 4-(benzylamino)-L-phenylalanine

737543

-

2.5.1.122

benzyl diphosphate + L-tyrosine = diphosphate + 7-benzyl-L-tyrosine

759054

-

2.5.1.122

2 entries

2.5.1.34

benzyl diphosphate + L-tryptophan = diphosphate + 5-benzyl-L-tryptophan

737544

-

2.5.1.80

benzyl diphosphate + L-tryptophan = diphosphate + 5-benzyl-L-tryptophan

737544

-

2.5.1.B31

benzyl diphosphate + L-tryptophan = diphosphate + 5-benzyl-L-tryptophan

737406, 739221

-

2.5.1.B31

benzyl diphosphate + L-tryptophan = diphosphate + 6-benzyl-L-tryptophan

739221, 737406

-

2.5.1.B31

2 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (5 results)

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Show Turnover Number (5 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.5.1.122

0.0055

-

pH 7.5, 35°C

759054

2.5.1.122

0.016

-

cosubstrate 4-aminophenylalanine, pH 7.5, 37°C

737543

2.5.1.122

0.028

-

cosubstrate 4-aminophenylalanine, pH 7.5, 37°C

737543

2.5.1.B31

0.00028

-

pH 7.5, 37°C

737406

2.5.1.B31

0.005

-

pH 7.5, 37°C

737406

2.5.1.122

3 entries

2.5.1.B31

2 entries

K_M Value (5 results)

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Show KM Value (5 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.5.1.122

0.13

-

pH 7.5, 35°C

759054

2.5.1.122

0.52

-

cosubstrate 4-aminophenylalanine, pH 7.5, 37°C

737543

2.5.1.122

0.75

-

cosubstrate 4-aminophenylalanine, pH 7.5, 37°C

737543

2.5.1.B31

0.04

-

pH 7.5, 37°C

737406

2.5.1.B31

0.11

-

pH 7.5, 37°C

737406

2.5.1.122

3 entries

2.5.1.B31

2 entries

References & Links

Literature References (5)

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Show Reference (5 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

737406

-

Tryptophan C5-, C6- and C7-prenylating enzymes displaying a preference for C-6 of the indole ring in the presence of unnatural dimethylallyl diphosphate analogues

2015

Winkelblech, J.; Liebhold, M.; Gunera, J.; Xie, X.; Kolb, P.; Li, S.

Adv. Synth. Catal.

357

975-986

737543

25707862

Tyrosine O-prenyltransferases TyrPT and SirD displaying similar behavior toward unnatural alkyl or benzyl diphosphate as their natural prenyl donor dimethylallyl diphosphate

2015

Yu, H.; Liebhold, M.; Xie, X.; Li, S.M.

Appl. Microbiol. Biotechnol.

99

7115-7124

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

739221

26077893

Tryptophan prenyltransferases showing higher catalytic activities for Friedel-Crafts alkylation of o- and m-tyrosines than tyrosine prenyltransferases

2015

Fan, A.; Xie, X.; Li, S.M.

Org. Biomol. Chem.

13

7551-7557

759054

28960770

Determination of alkyl-donor promiscuity of tyrosine-O-prenyltransferase SirD from Leptosphaeria maculans

2017

Bandari, C.; Scull, E.M.; Masterson, J.M.; Tran, R.H.Q.; Foster, S.B.; Nicholas, K.M.; Singh, S.

ChemBioChem

18

2323-2327

Links to other databases for benzyl diphosphate

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Show Links (1 entry)

ChEBI

PubChem

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