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Literature summary for 4.3.2.1 extracted from

  • Murakami-Murofushi, K.; Rainer, S.
    Argininosuccinase from bovine brain: isolation and comparison of catalytic, physical, and chemical properties with the enzymes from liver and kidney (1979), Anal. Biochem., 95, 139-155.
    View publication on PubMed
Search for more literature for 4.3.2.1

General Stability

General Stability Organism
Arg or phosphate ions protect from cold inactivation Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
additional information the antibody of the liver enzyme is an effective inhibitor of brain enzyme Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 4 * 50000, SDS-PAGE Bos taurus
202000
-
 gel filtration Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
brain Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Bos taurus

Storage Stability

Storage Stability Organism
0°C, Tris buffer, pH 8.5, 50% loss of activity after 2.5 h Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
argininosuccinate
-
 Bos taurus fumarate + L-Arg
-
 ?

Subunits

Subunits Comment Organism
tetramer 4 * 50000, SDS-PAGE Bos taurus