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Literature summary extracted from

  • Lee, M.; Maher, M.J.; Christopherson, R.I.; Guss, J.M.
    Kinetic and structural analysis of mutant Escherichia coli dihydroorotases: a flexible loop stabilizes the transition state (2007), Biochemistry, 46, 10538-10550.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.2.3 hanging drop vapour diffusion method with 15-20% polyethylene glycol 3350, 0.1 M MES, pH 6.0-6.5, 75 mM MgCl2, and 150 mM KCl Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.5.2.3 additional information deletion mutant DELTA107-116 DHOase shows negligible activity Escherichia coli
3.5.2.3 T109A decreased activity Escherichia coli
3.5.2.3 T109G negligible activity Escherichia coli
3.5.2.3 T109S strongly decreased activity Escherichia coli
3.5.2.3 T109V strongly decreased activity Escherichia coli
3.5.2.3 T110A negligible activity Escherichia coli
3.5.2.3 T110S strongly decreased activity Escherichia coli
3.5.2.3 T110V negligible activity Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.2.3 1.5
-
 N-(aminocarbonyl)-L-aspartic acid wild type enzyme, at pH 5.8 Escherichia coli
3.5.2.3 3
-
 N-(aminocarbonyl)-L-aspartic acid mutant enzyme T110S, at pH 5.8 Escherichia coli
3.5.2.3 4
-
 N-(aminocarbonyl)-L-aspartic acid mutant enzyme T110A, at pH 5.8 Escherichia coli
3.5.2.3 6
-
 N-(aminocarbonyl)-L-aspartic acid mutant enzyme T109S, at pH 5.8 Escherichia coli
3.5.2.3 6
-
 N-(aminocarbonyl)-L-aspartic acid mutant enzyme T110V, at pH 5.8 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.2.3 Zn2+ binuclear zinc center Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.5.2.3 Escherichia coli P05020
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.2.3 Mono Q column chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.2.3 L-dihydroorotate + H2O
-
 Escherichia coli N-carbamoyl-L-aspartate
-
 r
3.5.2.3 N-carbamoyl-L-aspartate
-
 Escherichia coli L-dihydroorotate + H2O
-
 r

Synonyms

EC Number Synonyms Comment Organism
3.5.2.3 DHOase
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.2.3 11.5
-
 N-(aminocarbonyl)-L-aspartic acid mutant enzyme T110A, at pH 5.8 Escherichia coli
3.5.2.3 49.8
-
 N-(aminocarbonyl)-L-aspartic acid mutant enzyme T109S, at pH 5.8 Escherichia coli
3.5.2.3 59.7
-
 N-(aminocarbonyl)-L-aspartic acid mutant enzyme T110S, at pH 5.8 Escherichia coli
3.5.2.3 145.5
-
 N-(aminocarbonyl)-L-aspartic acid mutant enzyme T110V, at pH 5.8 Escherichia coli
3.5.2.3 181.1
-
 N-(aminocarbonyl)-L-aspartic acid wild type enzyme, at pH 5.8 Escherichia coli