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Literature summary for 3.5.2.3 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
Search for more literature for 3.5.2.3

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

KM Value [mM]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P05020
-
-

Purification (Commentary)

Purification (Comment) Organism
Mono Q column chromatography Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
DHOase
-
 Escherichia coli

Turnover Number [1/s]

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