Cofactors

DP, Papari-Zareei M, Khan N, Sharma KK, Brandmaier A, et al. (2007) Cofactors, redox state, and directional preferences of hydroxysteroid dehydrogenases.

PLoS ONE Alerts: New Articles Matthias Negri et al. 2010

Dihydrosanguinarine 10-monooxygenase 1.14.13.56 Cofactors/prosthetic groups NADPH

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[1] Cofactors/prosthetic groups FAD [1] NADH (twice oxidized compared to NADPH [1]) [1] NADPH

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(UV-light treatment for 200 min leads to 30% inhibition of the enzyme [1]) [1] Cofactors/prosthetic groups NADH

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Methane monooxygenase 1.14.13.25 Cofactors/prosthetic groups FAD

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N-Methylcoclaurine 3'-monooxygenase 1.14.13.71 Cofactors/prosthetic groups NADPH

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[1, 4, 6] Inhibitors cytochrome c [1] Cofactors/prosthetic groups FAD

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[1] N-ethylmaleimide (80-90% inhibition at 0.008 mmol per g protein, irreversible by dilution, inhibition does not affect enzyme activity, but retards translocation of the substrate into the cytoplasm [3]) [3] Cofactors/prosthetic groups FAD

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< 1, 2 > [1-3] Cofactors/prosthetic groups NADPH < 1, 2 > [1, 2, 3] cytochrome P450

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[4] Zn2+ [4] azide (, weak, binds to the six-coordinate resting enzyme to form a new six-coordinate Fe2+ species [5]) [5] Cofactors/prosthetic groups FMN

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