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Literature summary for 4.2.1.40 extracted from

  • Gulick, A.M.; Hubbard, B.K.; Gerlt, J.A.; Rayment, I.
    Evolution of enzymatic activities in the enolase superfamily: identification of the general acid catalyst in the active site of D-glucarate dehydratase from Escherichia coli (2001), Biochemistry, 40, 10054-10062.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method Escherichia coli

Protein Variants

Protein Variants Comment Organism
N341D do not catalyze the dehydrofluorination of 4-deoxy-4-fluoro-D-glucarate Escherichia coli
N341L catalyzes the dehydrofluorination of 4-deoxy-4-fluoro-D-glucarate Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AES2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-deoxy-4-fluoro-D-glucarate
-
Escherichia coli ?
-
?
D-glucarate
-
Escherichia coli 3-deoxy-L-threo-2-hexulosarate + H2O
-
?
L-idarate
-
Escherichia coli 3-deoxy-L-threo-2-hexulosarate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.004
-
D-glucarate pH 7.5, 22°C, N341L mutant Escherichia coli
0.022
-
D-glucarate pH 7.5, 22°C, N341D mutant Escherichia coli
0.036
-
L-idarate pH 7.5, 22°C, N341L mutant Escherichia coli
0.099
-
L-idarate pH 7.5, 22°C, N341D mutant Escherichia coli
0.28
-
4-deoxy-4-fluoro-D-glucarate pH 7.5, 22°C, N341D mutant Escherichia coli
2.7
-
4-deoxy-4-fluoro-D-glucarate pH 7.5, 22°C, N341L mutant Escherichia coli
35
-
D-glucarate pH 7.5, 22°C, wild-type enzyme Escherichia coli
35
-
L-idarate pH 7.5, 22°C, wild-type enzyme Escherichia coli
44
-
4-deoxy-4-fluoro-D-glucarate pH 7.5, 22°C, wild-type enzyme Escherichia coli