Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.4.3.21 extracted from

  • Takahashi, K.; Klinman, J.P.
    Relationship of stopped flow to steady state parameters in the dimeric copper amine oxidase from Hansenula polymorpha and the role of zinc in inhibiting activity at alternate copper-containing subunits (2006), Biochemistry, 45, 4683-4694.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Cu only the copper-containing homodimer is capable of rapid reoxidation and the zinc-copper heterodimers are incapable of rapid turnover at either subunit Ogataea angusta
Zn the presence of substantial amount of zinc results in two distinctive enzyme species, designated as the fast and slow enzymes. Both forms are rapidly reduced by substrate methylamine with a rate constant of 199/s but behave differently in their oxidation rates. The fast enzyme is oxidized by dioxygen at a rate of 22.1/s, whereas the slow enzyme reacts at a rate of 0.00018/s. An investigation of the relationship between the copper content and the extent of the fast enzyme shows that only the copper-containing homodimer is capable of rapid reoxidation and the zinc-copper heterodimers are incapable of rapid turnover at either subunit Ogataea angusta

Organism

Organism UniProt Comment Textmining
Ogataea angusta
-
expressed in Saccharomyces cerevisiae
-

Substrates and Products (Substrate)

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