Abstract
Cytochrome (CYP) enzymes catalyze the metabolic reactions of endogenous and exogenous compounds. The superfamily of enzymes is found across many organisms, regardless of type, except for plants. Information was gathered about CYP2D enzymes through protein sequences of humans and other organisms. The secondary structure was predicted using the SOPMA. The structural and functional study of human CYP2D was conducted using ProtParam, SOPMA, Predotar 1.03, SignalP, TMHMM 2.0, and ExPASy. Most animals shared five central motifs according to motif analysis results. The tertiary structure of human CYP2D, as well as other animal species, was predicted by Phyre2. Human CYP2D proteins are heavily conserved across organisms, according to the findings. This indicates that they are descended from a single ancestor. They calculate the ratio of alpha-helices to extended strands to beta sheets to random coils. Most of the enzymes are alpha-helix, but small amounts of the random coil were also found. The data were obtained to provide us with a better understanding of mammalian proteins' functions and evolutionary relationships.
Highlights
Cytochrome P450 (CYP) is a unique heme-containing protein that has always been proven as a centrepiece of the organisms’ defense system against toxicants [1, 2]
The human Cytochrome P450 2D (CYP2D) gene family’s amino acid sequence was searched from the Public Database of the National Center for Biotechnology Information (NCBI) https://www.ncbi.nlm.nih.gov, and the protein crystal structure was obtained from the Public Database of Protein Data Bank (PDB) http://www.rcsb.org
This greatly raises the number of Fly/Mammal and Worm/Mammal orthologues compared to the number of Mammal orthologues and has a much more drastic impact on the Fly/Mammal and Worm/Mammal orthologues
Summary
Cytochrome P450 (CYP) is a unique heme-containing protein that has always been proven as a centrepiece of the organisms’ defense system against toxicants [1, 2]. Various compounds, such as medications, steroid hormones, carcinogens, and environmental toxins, are metabolized by these enzymes. The CYPs are thought to be active in xenobiotic detoxification processes and the biosynthesis of a variety of endogenous compounds [4, 5]. CYPs are classified primarily into two distinct forms: membranebound forms found in eukaryotes and soluble forms found. BioMed Research International Fruit fly + Aedes albopictus Yeast + Nematode +.
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