Literature summary for 1.14.14.1 extracted from

Valikhani, D.; Bolivar, J.; Dennig, A.; Nidetzky, B.
A tailor-made, self-sufficient and recyclable monooxygenase catalyst based on coimmobilized cytochrome P450 BM3 and glucose dehydrogenase (2018), Biotechnol. Bioeng., 115, 2416-2425 .

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Application

Application	Comment	Organism
synthesis	BM3 is coimmobilized with glucose dehydrogenase (type IV, from B. megaterium), as fusion proteins with the polycationic binding module Zbasic2, on anionic sulfopropyl?activated carrier. Immobilization via Zbasic2 enables each enzyme to be loaded in controllable amount. Using lauric acid as a representative P450 substrate, complete hydroxylation at low catalyst loading (below 0.1 mol%) and efficient electron coupling (74%), inside of the catalyst particle, to the regeneration of NADPH from glucose (27 cycles) is achieved. The immobilized P450 BM3 shows a total turnover number of about 18000 per second	Priestia megaterium

Organism

Organism	UniProt	Comment	Textmining
Priestia megaterium	P14779	bifunctional cytochrome P450/NADPH-P450 reductase, cf. EC 1.6.2.4	-
Priestia megaterium DSM 32	P14779	bifunctional cytochrome P450/NADPH-P450 reductase, cf. EC 1.6.2.4	-

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Release 2023.1 (January 2023)