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Results 1 - 10 of 10
EC Number
Activating Compound
Commentary
Reference
bacteriohemerythrin
enhances enzyme activity. The maximum activity is observed at a enzyme to bacteriohemerythrin concentration ratio of 4:1
catalase
increases pMMO activity, catalyzes decomposition of H2O2, on pMMO activity
Cu2+
pMMO, optimal at 0.3 mM
Fe3+
pMMO, optimal at 5.0 mM
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
methanobactin-Cu2+ complex
stimulation by methanobactin-Cu2+ complex, no activation in absence of copper, methanobactin is isolated from Methylosinus trichosporium strain OB3b
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
more
pMMO with the full complement of copper ions does not require methanobactin for activity
more
the active center of pMH is located in the beta-subunit
NDH-2
type 2 NADH:quinone oxidoreductase (NDH-2) is required for activity with reductants NADH or quinol as cofactors, overview
Results 1 - 10 of 10