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Comparative Analyses And Structural Insights Of The Novel Cytochrome P450 Fusion Protein Family CYP5619 In Oomycetes

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dc.contributor.author Bamal, Hans Denis
dc.contributor.author Chen, Wanping
dc.contributor.author Mashele, Samson Sitheni
dc.contributor.author Nelson, David R.
dc.contributor.author Kappo, Abidemi Paul
dc.contributor.author Mosa, Rebamang Anthony
dc.contributor.author Yu, Jae-Hyuk
dc.contributor.author Tuszynski, Jack A.
dc.contributor.author Syed, Khajamohiddin
dc.date.accessioned 2019-08-16T07:00:24Z
dc.date.available 2019-08-16T07:00:24Z
dc.date.issued 2018-04-26
dc.identifier.other DOI:10.1038/s41598-018-25044-0
dc.identifier.uri http://hdl.handle.net/11462/1997
dc.description Published Article en_US
dc.description.abstract Phylogenetic and structural analysis of P450 proteins fused to peroxidase/dioxygenase has not been reported yet. We present phylogenetic and in silico structural analysis of the novel P450 fusion family CYP5619 from the deadliest fish pathogenic oomycete, Saprolegnia diclina. Data-mining and annotation of CYP5619 members revealed their unique presence in oomycetes. CYP5619 members have the highest number of conserved amino acids among eukaryotic P450s. The highest number of conserved amino acids (78%) occurred in the peroxidase/dioxygenase domain compared to the P450 domain (22%). In silico structural analysis using a high-quality CYP5619A1 model revealed that CYP5619A1 has characteristic P450 structural motifs including EXXR and CXG. However, the heme-binding domain (CXG) in CYP5619 members was found to be highly degenerated. The in silico substrate binding pattern revealed that CYP5619A1 have a high affinity to medium chain fatty acids. Interestingly, the controlling agent of S. diclina malachite green was predicted to have the highest binding affinity, along with linoleic acid. However, unlike fatty acids, none of the active site amino acids formed hydrogen bonds with malachite green. The study’s results will pave the way for assessing CYP5619A1’s role in S. diclina physiology, including the nature of malachite green binding. en_US
dc.language.iso en en_US
dc.publisher Scientific Reports en_US
dc.relation.ispartofseries Scientific Reports, Volume 8, Article number: 6597 (2018);
dc.title Comparative Analyses And Structural Insights Of The Novel Cytochrome P450 Fusion Protein Family CYP5619 In Oomycetes en_US
dc.type Article en_US

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