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Literature summary for 1.4.3.21 extracted from

  • Mills, S.A.; Goto, Y.; Su, Q.; Plastino, J.; Klinman, J.P.
    Mechanistic comparison of the cobalt-substituted and wild-type copper amine oxidase from Hansenula polymorpha (2002), Biochemistry, 41, 10577-10584.
    View publication on PubMed
Search for more literature for 1.4.3.21

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information the Km-value for O2 of the cobalt-substituted enzyme form is approximately 70fold higher than that of the copper-containing wild-type enzyme Ogataea angusta

Metals/Ions

Metals/Ions Comment Organism Structure
Cobalt the Km-value for O2 of the cobalt-substituted enzyme form is approximately 70fold higher than that of the copper-containing wild-type enzyme Ogataea angusta
copper copper protein Ogataea angusta

Organism

Organism UniProt Comment Textmining
Ogataea angusta
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methylamine + H2O + O2
-
 Ogataea angusta methanal + NH3 + H2O2
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1
-
 O2 Co-substituted enzyme Ogataea angusta
7.8
-
 O2 wild-type enzyme Ogataea angusta