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Literature summary 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

Crystallization (Commentary)

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

Protein Variants

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.40 4-deoxy-D-glucarate
-
 Escherichia coli
4.2.1.40 xylarohydroxamate
-
 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.40 Mg2+ located at the active site Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.40 Escherichia coli P0AES2
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.40 4-deoxy-4-fluoro-D-glucarate
-
 Escherichia coli ?
-
 ?
4.2.1.40 D-glucarate
-
 Escherichia coli 3-deoxy-L-threo-2-hexulosarate + H2O
-
 ?
4.2.1.40 L-idarate
-
 Escherichia coli 3-deoxy-L-threo-2-hexulosarate
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.1.40 0.00025
-
 L-idarate H339N mutant, pH 7.5, 22°C Escherichia coli
4.2.1.40 0.00033
-
 D-glucarate H339N mutant, pH 7.5, 22°C Escherichia coli
4.2.1.40 0.001
-
 D-glucarate K207R mutant, pH 7.5, 22°C Escherichia coli
4.2.1.40 0.0015
-
 L-idarate K207Q mutant, pH 7.5, 22°C Escherichia coli
4.2.1.40 0.0015
-
 L-idarate K207R mutant, pH 7.5, 22°C Escherichia coli
4.2.1.40 0.005
-
 D-glucarate K207Q mutant, pH 7.5, 22°C Escherichia coli
4.2.1.40 0.0051
-
 L-idarate H339A mutant, pH 7.5, 22°C Escherichia coli
4.2.1.40 0.016
-
 D-glucarate H339A mutant, pH 7.5, 22°C Escherichia coli
4.2.1.40 0.02
-
 D-glucarate H339Q mutant, pH 7.5, 22°C Escherichia coli
4.2.1.40 0.02
-
 L-idarate H339Q mutant, pH 7.5, 22°C Escherichia coli
4.2.1.40 0.08
-
 L-idarate Y150F mutant, pH 7.5, 22°C Escherichia coli
4.2.1.40 0.19
-
 D-glucarate Y150F mutant, pH 7.5, 22°C Escherichia coli
4.2.1.40 1
-
 D-glucarate D366A mutant, pH 7.5, 22°C Escherichia coli
4.2.1.40 1.5
-
 L-idarate D366A mutant, pH 7.5, 22°C Escherichia coli
4.2.1.40 1.8
-
 D-glucarate D366N mutant, pH 7.5, 22°C Escherichia coli
4.2.1.40 8
-
 L-idarate D366N mutant, pH 7.5, 22°C Escherichia coli
4.2.1.40 34
-
 L-idarate pH 7.5, 22°C, wild-type enzyme Escherichia coli
4.2.1.40 35
-
 D-glucarate pH 7.5, 22°C, wild-type enzyme Escherichia coli