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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: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli (2000), Biochemistry, 39, 4590-4602.
    View publication on PubMed
Search for more literature for 4.2.1.40

Crystallization (Commentary)

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

Protein Variants

Protein Variants Comment Organism
D366A reduced kcat for D-glucarate and L-idarate Escherichia coli
D366N reduced kcat for D-glucarate and 3fold reduced kcat for L-idarate Escherichia coli
H339A reduced kcat for D-glucarate and L-idarate Escherichia coli
H339N reduced kcat for D-glucarate and L-idarate Escherichia coli
H339Q reduced kcat for D-glucarate and L-idarate Escherichia coli
K207Q reduced kcat for D-glucarate and L-idarate Escherichia coli
K207R reduced kcat for D-glucarate and L-idarate Escherichia coli
Y150F significant reduction of kcat for D-glucarate and L-idarate Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
4-deoxy-D-glucarate
-
 Escherichia coli
xylarohydroxamate
-
 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ located at the active site 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
0.00025
-
 L-idarate H339N mutant, pH 7.5, 22°C Escherichia coli
0.00033
-
 D-glucarate H339N mutant, pH 7.5, 22°C Escherichia coli
0.001
-
 D-glucarate K207R mutant, pH 7.5, 22°C Escherichia coli
0.0015
-
 L-idarate K207Q mutant, pH 7.5, 22°C Escherichia coli
0.0015
-
 L-idarate K207R mutant, pH 7.5, 22°C Escherichia coli
0.005
-
 D-glucarate K207Q mutant, pH 7.5, 22°C Escherichia coli
0.0051
-
 L-idarate H339A mutant, pH 7.5, 22°C Escherichia coli
0.016
-
 D-glucarate H339A mutant, pH 7.5, 22°C Escherichia coli
0.02
-
 D-glucarate H339Q mutant, pH 7.5, 22°C Escherichia coli
0.02
-
 L-idarate H339Q mutant, pH 7.5, 22°C Escherichia coli
0.08
-
 L-idarate Y150F mutant, pH 7.5, 22°C Escherichia coli
0.19
-
 D-glucarate Y150F mutant, pH 7.5, 22°C Escherichia coli
1
-
 D-glucarate D366A mutant, pH 7.5, 22°C Escherichia coli
1.5
-
 L-idarate D366A mutant, pH 7.5, 22°C Escherichia coli
1.8
-
 D-glucarate D366N mutant, pH 7.5, 22°C Escherichia coli
8
-
 L-idarate D366N mutant, pH 7.5, 22°C Escherichia coli
34
-
 L-idarate pH 7.5, 22°C, wild-type enzyme Escherichia coli
35
-
 D-glucarate pH 7.5, 22°C, wild-type enzyme Escherichia coli