Roberto Contestabile

Full professor of Molecular Biology

roberto.contestabile@uniroma1.it

Academic Appointments

Coordinator of the Master’s degree in Biochemistry, Sapienza University of Rome, Itlay.

Scientific interests

Regulation of vitamin B6 metabolism in bacteria and humans. Neurological disorders related to vitamin B6 metabolism. Enzyme inhibition as a mean of chemotherapy intervention.

Contribution to Science

My research activity has mainly concerned pyridoxal phosphate-dependent enzymes and vitamin B6 metabolism in bacteria and humans. Concerning PLP-dependent enzymes, I have dealt with their catalytic mechanism, catalytic promiscuity and evolution of catalytic activities, the design and experimentation of specific inhibitors. Concerning vitamin B6 metabolism, I have contributed to the understanding of transcriptional regulation of vitamin B6 biosynthesis in bacteria and of the molecular basis of neurological disorders related to vitamin B6 metabolism. At present, I my research activity focused on the study of the pyridoxal 5’-phosphate (PLP) binding protein (PLPBP), an important regulatory component of PLP biosynthesis and salvage pathways in bacteria and humans whose function is unknown. I am also involved in the design and testing of inhibitors of vitamin B6 metabolism as means of chemotherapy intervention.

5 Selected publications

  • Graziani C, Barile A, Parroni A, di Salvo ML, De Cecio I, Colombo T, Babor J, de Crécy-Lagard V, Contestabile R, Tramonti A. The ubiquitous pyridoxal 5′-phosphate-binding protein is also an RNA-binding protein. Protein Sci. 2024 Dec;33(12):e5242. doi: 10.1002/pro.5242. PMID: 39604152
  • Graziani C, Barile A, Antonelli L, Fiorillo A, Ilari A, Vetica F, di Salvo ML, Paiardini A, Tramonti A, Contestabile R. The Z isomer of pyridoxilidenerhodanine 5′-phosphate is an efficient inhibitor of human pyridoxine 5′-phosphate oxidase, a crucial enzyme in vitamin B6 salvage pathway and a potential chemotherapeutic target. FEBS J. 2024 Nov;291(22):4984-5001. doi: 10.1111/febs.17274. Epub 2024 Sep 17. PMID: 39288205
  • Malatesta M, Fornasier E, Di Salvo ML, Tramonti A, Zangelmi E, Peracchi A, Secchi A, Polverini E, Giachin G, Battistutta R, Contestabile R, Percudani R. One substrate many enzymes virtual screening uncovers missing genes of carnitine biosynthesis in human and mouse. Nat Commun. 2024 Apr 13;15(1):3199. doi: 10.1038/s41467-024-47466-3. PMID: 38615009
  • Tramonti A, Donkor AK, Parroni A, Musayev FN, Barile A, Ghatge MS, Graziani C, Alkhairi M, AlAwadh M, di Salvo ML, Safo MK, Contestabile R. Functional and structural properties of pyridoxal reductase (PdxI) from Escherichia coli: a pivotal enzyme in the vitamin B6 salvage pathway. FEBS J. 2023 Dec;290(23):5628-5651. doi: 10.1111/febs.16962. Epub 2023 Oct 2. PMID: 37734924
  • Tramonti A, Ghatge MS, Babor JT, Musayev FN, di Salvo ML, Barile A, Colotti G, Giorgi A, Paredes SD, Donkor AK, Al Mughram MH, de Crécy-Lagard V, Safo MK, Contestabile R. Characterization of the Escherichia coli pyridoxal 5′-phosphate homeostasis protein (YggS): Role of lysine residues in PLP binding and protein stability. Protein Sci. 2022 Nov;31(11):e4471. doi: 10.1002/pro.4471. PMID: 36218140

On-going Grants

Project Title Funding source Amount (Euros) Period Role of the PI
The enigmatic Escherichia coli PLP-binding protein (YggS) is an RNA-binding protein - Investigating the structural and functional implications of this novel observation. Istituto Pasteur-Fondazione Cenci Bolognetti 40.000 1/3/2025–28/02/2027 PI (30 % of time)

Complete list of published work in MyBibliography:
https://pubmed.ncbi.nlm.nih.gov/?term=contestabile+r

KEYWORDS
Vitamin B6 metabolism; RNA binding proteins; pyridoxal 5’-phosphate; PLP-binding protein

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