print visible entries

print all entries

Ligand 2,4-dinitrophenyl alpha-D-galactoside

Basic Ligand Information

Molecular Structure

close all tables

open all tables

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (1 result)

top print hide

Show Substrate (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.2.1.22

2,4-dinitrophenyl alpha-D-galactoside + H2O = 2,4-dinitrophenol + alpha-D-galactose

678262

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (3 results)

top print hide

Show Turnover Number (3 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.2.1.22

0.085

-

mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C

678262

3.2.1.22

0.41

-

wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C

678262

3.2.1.22

12.23

-

wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C

678262

3.2.1.22

3 entries

K_M Value (2 results)

top print hide

Show KM Value (2 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.2.1.22

0.037

-

wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C

678262

3.2.1.22

0.135

-

mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C

678262

3.2.1.22

2 entries

References & Links

Literature References (1)

top print hide

Show Reference (1 entry)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

678262

17323919

Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases

2007

Comfort, D.A.; Bobrov, K.S.; Ivanen, D.R.; Shabalin, K.A.; Harris, J.M.; Kulminskaya, A.A.; Brumer, H.; Kelly, R.M.

Biochemistry

46

3319-3330

Links to other databases for 2,4-dinitrophenyl alpha-D-galactoside

top print hide

Show Links (1 entry)

ChEBI

PubChem

-