Protein Family Models

This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, Nitric oxide synthase and methionine synthase reductase. [1]. 7657631. The flavin reductase activity of the flavoprotein component of. sulfite reductase from Escherichia coli. A new model for the. protein structure.. Eschenbrenner M, Coves J, Fontecave M;. J Biol Chem 1995;270:20550-20555.. [2]. 7589518. NADPH-sulfite reductase flavoprotein from Escherichia coli:. contribution to the flavin content and subunit interaction.. Eschenbrenner M, Coves J, Fontecave M;. FEBS Lett 1995;374:82-84.. [3]. 8078947. Dissection of NADPH-cytochrome P450 oxidoreductase into distinct. functional domains.. Smith GC, Tew DG, Wolf CR;. Proc Natl Acad Sci U S A 1994;91:8710-8714.. [4]. 9237990. Three-dimensional structure of NADPH-cytochrome P450 reductase:. prototype for FMN- and FAD-containing enzymes.. Wang M, Roberts DL, Paschke R, Shea TM, Masters BS, Kim JJ;. Proc Natl Acad Sci U S A 1997;94:8411-8416. (from Pfam)

Date:

2024-08-14

Cytochrome P450s are haem-thiolate proteins [6] involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyse regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures [6]. [1]. 7549871. A three-dimensional model of aromatase cytochrome P450.. Graham-Lorence S, Amarneh B, White RE, Peterson JA, Simpson ER;. Protein Sci 1995;4:1065-1080.. [2]. 8405421. Molecular evolution of P450 superfamily and P450-containing. monooxygenase systems.. Degtyarenko KN, Archakov AI;. FEBS Lett 1993;332:1-8.. [3]. 7678494. The P450 superfamily: update on new sequences, gene mapping,. accession numbers, early trivial names of enzymes, and. nomenclature.. Nelson DR, Kamataki T, Waxman DJ, Guengerich FP, Estabroo. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity. [1]. 1748631. The sequence of squash NADH:nitrate reductase and its. relationship to the sequences of other flavoprotein. oxidoreductases. A family of flavoprotein pyridine nucleotide. cytochrome reductases.. Hyde GE, Crawford NM, Campbell W;. J Biol Chem 1991;266:23542-23547. (from Pfam)

Date:

2024-08-14

bifunctional cytochrome P450/NADPH--P450 reductase functions as a functions as a fatty acid monooxygenase that catalyzes the hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids, and also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain

Date:

2020-12-14