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Literature summary for 1.4.3.2 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)

Cloned (Comment) Organism
-
Calloselasma rhodostoma

Inhibitors

Inhibitors Comment Organism Structure
anthranilate competitive Calloselasma rhodostoma

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Calloselasma rhodostoma
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Calloselasma rhodostoma

Substrates and Products (Substrate)

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

Temperature Stability [°C]

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

pH Stability

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

Cofactor

Cofactor Comment Organism Structure
FAD
-
Calloselasma rhodostoma