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Literature summary for 2.1.3.3 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
Search for more literature for 2.1.3.3

Inhibitors

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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
90000
-
 dimeric aggregation state, sucrose density gradient centrifugation Bacillus subtilis
167000
-
 tetrameric aggregation state, sucrose density gradient centrifugation Bacillus subtilis
236000
-
 hexameric aggregation state, sucrose density gradient centrifugation Bacillus subtilis
260000
-
 gel filtration Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis 168
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Storage Stability

Storage Stability Organism
-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)

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

Subunits

Subunits Comment Organism
? 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

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

pH Range

pH Minimum pH Maximum Comment Organism
6 8.3 approx. 50% of maximal activity at pH 6.0 Bacillus subtilis
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

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

Ki Value [mM]

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