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Literature summary extracted from

  • Macheroux, P.; Seth, O.; Bollschweiler, C.; Schwarz, M.; Kurfurst, M.; Au, L.C.; Ghisla, S.
    L-Amino-acid oxidase from the Malayan pit viper Calloselasma rhodostoma: comparative sequence analysis and characterization of active and inactive forms of the enzyme (2001), Eur. J. Biochem., 268, 1679-1686.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.3.2
-
 Calloselasma rhodostoma

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.3.2 anthranilate competitive Calloselasma rhodostoma

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.2 0.56
-
 L-leucine
-
 Calloselasma rhodostoma

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.2 Calloselasma rhodostoma
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.2
-
 Calloselasma rhodostoma

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.2 L-amino acid + H2O + O2
-
 Calloselasma rhodostoma 2-oxo acid + NH3 + H2O2
-
 ?
1.4.3.2 L-leucine + H2O + O2
-
 Calloselasma rhodostoma 4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.4.3.2 additional information
-
 freezing causes reversible inactivation Calloselasma rhodostoma

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.4.3.2 7
-
 at pH above neutrality reversible inactivation Calloselasma rhodostoma

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.2 FAD
-
 Calloselasma rhodostoma