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Sci Rep. 2018 Apr 26;8(1):6597. doi: 10.1038/s41598-018-25044-0.

Comparative analyses and structural insights of the novel cytochrome P450 fusion protein family CYP5619 in Oomycetes.

Author information

1
Unit for Drug Discovery Research, Department of Health Sciences, Central University of Technology, Bloemfontein, 9300, Free State, South Africa.
2
College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei Province, China.
3
Department of Microbiology, Immunology and Biochemistry, University of Tennessee Health Science Center, Memphis, TN, 38163, USA.
4
Department of Biochemistry and Microbiology, Faculty of Science and Agriculture, University of Zululand, KwaDlangezwa, 3886, South Africa.
5
Department of Bacteriology, University of Wisconsin-Madison, 3155 MSB, 1550 Linden Drive, Madison, WI, 53706, USA.
6
Department of Physics, University of Alberta, Edmonton, AB T6G 2E1, Canada. jackt@ualberta.ca.
7
Cross Cancer Institute, Department of Oncology, University of Alberta, Edmonton, AB T6G 1Z2, Canada. jackt@ualberta.ca.
8
Department of Biochemistry and Microbiology, Faculty of Science and Agriculture, University of Zululand, KwaDlangezwa, 3886, South Africa. khajamohiddinsyed@gmail.com.

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.

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