EC Number |
Activating Compound |
Reference |
---|
1.14.18.3 | Cu2+ |
pMMO, optimal at 0.3 mM |
438944 |
1.14.18.3 | Fe3+ |
pMMO, optimal at 5.0 mM |
438944 |
1.14.18.3 | methanobactin-Cu2+ complex |
stimulation by methanobactin-Cu2+ complex, no activation in absence of copper, methanobactin is isolated from Methylosinus trichosporium strain OB3b |
675831 |
1.14.18.3 | more |
pMMO with the full complement of copper ions does not require methanobactin for activity |
684114 |
1.14.18.3 | more |
the active center of pMH is located in the beta-subunit |
702501 |
1.14.18.3 | catalase |
increases pMMO activity, catalyzes decomposition of H2O2, on pMMO activity |
705192 |
1.14.18.3 | lauryl maltoside |
the stimulatory effect of lauryl maltoside is responsible for the initial increase in duroquinol-dependent activity of the pellet, but no activity with NADH is observed after this solubilization |
713934 |
1.14.18.3 | more |
no pMMO acivity is observed in the detergent-solubilized fraction in the presence of dithionite, ascorbate, or methyl viologen. No pMMO activity with duroquinol or NADH is observed after solubilization with Triton X-100, Tween 20, zwittergent 3-12, Nonidet-P40, or synperonic |
713934 |
1.14.18.3 | bacteriohemerythrin |
enhances enzyme activity. The maximum activity is observed at a enzyme to bacteriohemerythrin concentration ratio of 4:1 |
728079 |
1.14.18.3 | NDH-2 |
type 2 NADH:quinone oxidoreductase (NDH-2) is required for activity with reductants NADH or quinol as cofactors, overview |
745389 |