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Cytochrome P450: Metabolism, Structure-Function, Evolution and Applications
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Cytochrome P450: Metabolism, Structure-Function, Evolution and Applications

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: 30 March 2025 | Viewed by 433

Special Issue Editors

Prof. Dr. Khajamohiddin Syed

E-Mail Website
Guest Editor
Department of Biochemistry and Microbiology, Faculty of Science and Agriculture, University of Zululand, KwaDlangezwa 3886, South Africa
Interests: annotation, structure-function analysis, evolution, and applications of P450s
Prof. Dr. David Lamb

E-Mail Website
Guest Editor
Institute of Life Science, Medical School, Swansea University, Swansea SA2 8PP, UK
Interests: cytochrome P450; monooxidation; redox proteins; biodiversity; evolution

Special Issue Information

Dear Colleagues,

Cytochrome P450 monooxygenases (CYPs/P450s) belong to a superfamily of heme-thiolate proteins that play a vital role in primary and secondary metabolism. P450s are ubiquitous in all domains of life, catalyzing a wide range of reactions with substrate promiscuity and stereo- and regio-specificity. Because of this, P450s have been utilized in a wide range of pharmacological, biotechnological, and environmental applications, including drug discovery and development, the production of fine chemicals, fragrances, pharmaceutical compounds, biofuels, biosensing, and bioremediation. Without being limited to a specific research category, we welcome original articles, short communications, case reports, and reviews (wet laboratory or in silico-based studies) on any topic regarding P450s.

Prof. Dr. Khajamohiddin Syed
Prof. Dr. David Lamb
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • cytochrome P450 monooxygenase
  • metabolism
  • structure-function
  • evolution
  • applications

Published Papers (1 paper)

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Research

35 pages, 8530 KiB  
Article
Structure–Function Analysis of the Essential Mycobacterium tuberculosis P450 Drug Target, CYP121A1
by Tiara Padayachee, David C. Lamb, David R. Nelson and Khajamohiddin Syed
Int. J. Mol. Sci. 2024, 25(9), 4886; https://doi.org/10.3390/ijms25094886 - 30 Apr 2024
Viewed by 272
Abstract
Cytochrome P450 CYP121A1 is a well-known drug target against Mycobacterium tuberculosis, the human pathogen that causes the deadly disease tuberculosis (TB). CYP121A1 is a unique P450 enzyme because it uses classical and non-classical P450 catalytic processes and has distinct structural features among [...] Read more.
Cytochrome P450 CYP121A1 is a well-known drug target against Mycobacterium tuberculosis, the human pathogen that causes the deadly disease tuberculosis (TB). CYP121A1 is a unique P450 enzyme because it uses classical and non-classical P450 catalytic processes and has distinct structural features among P450s. However, a detailed investigation of CYP121A1 protein structures in terms of active site cavity dynamics and key amino acids interacting with bound ligands has yet to be undertaken. To address this research knowledge gap, 53 CYP121A1 crystal structures were investigated in this study. Critical amino acids required for CYP121A1’s overall activity were identified and highlighted this enzyme’s rigid architecture and substrate selectivity. The CYP121A1-fluconazole crystal structure revealed a novel azole drug–P450 binding mode in which azole heme coordination was facilitated by a water molecule. Fragment-based inhibitor approaches revealed that CYP121A1 can be inhibited by molecules that block the substrate channel or by directly interacting with the P450 heme. This study serves as a reference for the precise understanding of CYP121A1 interactions with different ligands and the structure–function analysis of P450 enzymes in general. Our findings provide critical information for the synthesis of more specific CYP121A1 inhibitors and their development as novel anti-TB drugs. Full article
(This article belongs to the Special Issue Cytochrome P450: Metabolism, Structure-Function, Evolution and Applications)
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