Naeem Shafqat qualified with a BPharm degree from the University of Karachi, Pakistan in 1996. After finishing BPharm, he joined Park-e-Davis Pharmaceuticals, Pakistan as a Tablet Production Officer. In 1998, to continue his passion for a medical research he went on for a PhD in Medical Biochemistry at the Karolinska Institute, Stockholm, Sweden. Soon after completing his PhD, he joined the University of Oxford (2004-2011) as a post-doctoral fellow, to study the structure-function properties of human metabolic enzymes associated with the pathogenesis of diabetes mellitus and inflammation. At Oxford Naeem got a unique opportunity to train as an expert in modern state-of-art high-throughput protein expression-purification, crystallization and structure biology techniques. In 2011, being an expert in protein chemistry/structure biology, he joined the University of Birmingham where he studied the structure-function properties of 5alpha-Reductase isozymes and Cytochrome P450 oxidoreductase involved in the pathogenesis of Prostate Cancer and Disorders of Sex Development.
Subsequently, Naeem joined the PAPRSB Institute of Health Sciences (IHS), University Brunei Darussalam in 2015 as a Senior Assistant Professor, where he applies his profound knowledge and expertise is studying the structure-function properties of human metabolic enzymes associated with the pathogenesis of inflammation and different hormone dependent cancer forms.
• 1993-1996: Bachelor of Pharmacy, University of Karachi, Pakistan
• 1999-2004: PhD in Medical Biochemistry, Karolinska Institute, Stockholm, Sweden.
• 2004 -2011: Post-Doctoral studies, Nuffield Department of Clinical Medicine, University of Oxford, UK
• 2011 -2015: Senior Research Fellow, Center for Diabetes and Metabolism, University of Birmingham, UK
• June 2013: Post Graduate Certificate in Higher Education, UK.
• April 2014: Associate Fellow of the Higher Education Acade
Structure-function analysis of human Metabolic enzymes
• Mueller J.W., O’Neill N., Shafqat N. (2015) Small World: A Plant Perspective on Human Sulfate Activation. In: De Kok L., Hawkesford M., Rennenberg H., Saito K., Schnug E. (eds) Molecular Physiology and Ecophysiology of Sulfur. Proceedings of the International Plant Sulfur Workshop. Publisher Springer
• Bhatia C, Oerum S, Bray J, Kavanagh KL, Shafqat N, Yue W, Oppermann U (2015). Towards a systematic analysis of human short-chain dehydrogenases/reductases (SDR): Ligand identifica-tion and structure-activity relationships. Chem Biol Interact. 5; 234:114-25.
• Mueller JW, Shafqat N (2013). Adenosin-5'-phosphosulfate (APS) - a multifaceted modulator of bifunctional PAPS synthases and related enzymes. FEBS J. 280(13):3050-7.
• Shafqat N, Muniz JR, Pilka ES, Paragrigoriou E, von Delft F, Oppermann U, Yue WW (2013). Insight into S-adenosyl-L-methionine biosynthesis from crystal structures of human methionine adenosyltransferase catalytic and regulatory subunits. Biochem J. 452(1):27-36.
• Shafqat N, Kavanagh KL, Sass JO, Christensen E, Fukao T, Lee WH, Oppermann U, Yue WW (2013). A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency. J Inherit Metab Dis. 36(6):983-7.
• Chaikuad A*, Shafqat N*, Al-Mokhtar R, Cameron G, Clarke AR, Brady L, Oppermann U, Frayne J, Yue WW (2011). Structure and kinetic characterization of human sperm-specific glyceraldehydes-3-phosphate dehydrogenase, GAPDS (*equal contribution). Biochem J. 435(2):401-9.
Grant type: , Grant Number: , Project Title: , Investigators (PI/Co-PI): , Funding Details: , Start Date: 31/03/2010, End Date: 31/03/2016
-Please refer to publication list on google scholar.
-Crystallize and determined protein 3D X-ray structures of over 40 human metabolic enzymes; Database Pubmed: Author ID: Naeem Shafqat (https://www.rcsb.org)
University of Oxford
University of Birmingham
The 3D X-ray protein structures determined in the presence of novel substrate and inhibitors will provide a platform for the discovery of future drug, beneficial for the treatment of hormonal dependent metabolic disorders.