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Literature summary for 2.1.3.2 extracted from

  • Etchian, O.A.; Pellerin, J.
    Characterization of aspartate transcarbamylase activity from gonads of the soft shell clam, Mya arenaria (2003), Comp. Biochem. Physiol. B, 134, 615-629.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
dimethylformamide
-
Mya arenaria
dimethylsulfamide
-
Mya arenaria

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2
-
Carbamoyl phosphate pH 8.23, 37°C Mya arenaria
3.93
-
Carbamoyl phosphate pH 9.4, 37°C Mya arenaria
6.25
-
L-aspartate pH 8.23, 37°C Mya arenaria
7.35
-
L-aspartate pH 9.4, 37°C Mya arenaria

Organism

Organism UniProt Comment Textmining
Mya arenaria
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
gonad
-
Mya arenaria
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
highest activity in Tris-HCl buffer, followed by Tris-acetate EDTA, glycine sodium and cacodylate buffer Mya arenaria

Storage Stability

Storage Stability Organism
-20°C, 35 days, loss of 50% activity Mya arenaria
-80°C, 35 days, stable Mya arenaria

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
carbamoyl phosphate + L-aspartate
-
Mya arenaria phosphate + N-carbamoyl-L-aspartate
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Mya arenaria

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
10 min, 50% residual activity Mya arenaria

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.2
-
-
Mya arenaria