EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.4.3.21 | 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 | |
1.4.3.21 | 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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.4.3.21 | Ogataea angusta | - |
expressed in Saccharomyces cerevisiae | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.3.21 | methylamine + H2O + O2 | - |
Ogataea angusta | methanal + NH3 + H2O2 | - |
? |