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PMID: 1908607 Published · ppublish English Journal Article Review

An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals.

Trends in biochemical sciences ·Vol. 16 ·No. 4 ·1991-04-00 ·Pages 154-8

Porter TD

Abstract

The recent determination of the amino acid sequences of the Bacillus megaterium cytochrome P-450 and the flavoprotein component of Salmonella typhimurium NADPH-sulfite reductase revealed that these enzymes contain a flavoprotein moiety remarkably similar to mammalian NADPH-cytochrome P-450 reductase. The presence of this oxidoreductase in these very different enzymes suggests that this flavoprotein arose early in evolution and was utilized as an enzymological building block. The multi-domain structure of the reductase further suggests that it arose through a fusion of genes encoding simple flavin electron-transport proteins.

MeSH Terms
Amino Acid Sequence Animals Bacillus megaterium/enzymology,genetics Base Sequence Flavoproteins/genetics Molecular Sequence Data NADPH-Ferrihemoprotein Reductase/genetics Oxidoreductases Acting on Sulfur Group Donors/genetics Salmonella typhimurium/enzymology,genetics Sulfite Reductase (NADPH)
Chemicals
Flavoproteins NADPH-Ferrihemoprotein Reductase Oxidoreductases Acting on Sulfur Group Donors Sulfite Reductase (NADPH)
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Porter T D
Department of Biological Chemistry, Medical School, University of Michigan, Ann Arbor 48109-0606.
Article Info
Journal
Trends in biochemical sciences
Abbr.
Trends Biochem Sci
ISSN
0968-0004
Published
1991-04-00
Pages
154-8
Language
English
Region
England
NLM ID
7610674
Subset
IM
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