Reference on EC 1.6.2.4 - NADPH-hemoprotein reductase and Organism(s) Priestia megaterium and UniProt Accession P14779

Please use the Reference Search for a specific query.

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

Murataliev, M.B.; Feyereisen, R.

Functional interactions in cytochrome P450BM3. Fatty acid substrate binding alters electron-transfer properties of the flavoprotein domain

Biochemistry

15029-15037

1996

Priestia megaterium

Girvan, H.M.; Toogood, H.; Littleford, R.E.; Seward, H.E.; Smith, W.E.; Ekanem, I.; Leys, D.; Cheesman, M.; Munro, A.W.

Novel heme coordination variants of flavocytochrome P450 BM3

Biochem. J.

417

65-76

2009

Priestia megaterium (P14779), Priestia megaterium

Milhim, M.; Gerber, A.; Neunzig, J.; Hannemann, F.; Bernhardt, R.

A novel NADPH-dependent flavoprotein reductase from Bacillus megaterium acts as an efficient cytochrome P450 reductase

J. Biotechnol.

231

83-94

2016

Priestia megaterium, Priestia megaterium DSM319