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Literature summary extracted from

  • Neway, J.O.; Switzer, R.L.
    Purification, characterization, and physiological function of Bacillus subtilis ornithine transcarbamylase (1983), J. Bacteriol., 155, 512-521.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.3 Delta-N-Phosphonoacetyl-L-ornithine
-
 Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.3.3 44000
-
 x * 44000, SDS-PAGE, enzyme exists as a mixture of dimeric, tetrameric and hexameric forms, enzyme is converted to a dimer in presence of 2-mercaptoethanol Bacillus subtilis
2.1.3.3 90000
-
 dimeric aggregation state, sucrose density gradient centrifugation Bacillus subtilis
2.1.3.3 167000
-
 tetrameric aggregation state, sucrose density gradient centrifugation Bacillus subtilis
2.1.3.3 236000
-
 hexameric aggregation state, sucrose density gradient centrifugation Bacillus subtilis
2.1.3.3 260000
-
 gel filtration Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.3 Bacillus subtilis
-
-
-
2.1.3.3 Bacillus subtilis 168
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.3.3 heat, ammonium sulfate, DEAE-cellulose, hydroxylapatite, DEAE-Sephacel, Bio-Gel A 1.5 Bacillus subtilis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.3.3 265
-
-
 Bacillus subtilis

Storage Stability

EC Number Storage Stability Organism
2.1.3.3 -20°C, protein concentration 1-2 mg/ml, several months, no loss of activity after repeated freezing and thawing Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.3.3 carbamoyl phosphate + L-ornithine
-
 Bacillus subtilis phosphate + L-citrulline
-
 ?
2.1.3.3 carbamoyl phosphate + L-ornithine
-
 Bacillus subtilis 168 phosphate + L-citrulline
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.3.3 ? x * 44000, SDS-PAGE, enzyme exists as a mixture of dimeric, tetrameric and hexameric forms, enzyme is converted to a dimer in presence of 2-mercaptoethanol Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.3.3 8.3
-
 bicine-NaOH buffer Bacillus subtilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.1.3.3 6 8.3 approx. 50% of maximal activity at pH 6.0 Bacillus subtilis
2.1.3.3 7.5 10 nearly constant activity in this range, half-maximal activity at pH 7.0, negliable activity at pH 6.0 Bacillus subtilis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.1.3.3 8.3
-
 highest stability, bicine-NaOH buffer Bacillus subtilis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.1.3.3 0.01
-
 phosphonacetyl-L-ornithine between pH 7.5-9.0 Bacillus subtilis