M
Martino L. di Salvo
Researcher at Sapienza University of Rome
Publications - 77
Citations - 2269
Martino L. di Salvo is an academic researcher from Sapienza University of Rome. The author has contributed to research in topics: Pyridoxal & Serine hydroxymethyltransferase. The author has an hindex of 27, co-authored 74 publications receiving 1958 citations. Previous affiliations of Martino L. di Salvo include Virginia Commonwealth University.
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Journal ArticleDOI
Vitamin B(6) salvage enzymes: mechanism, structure and regulation
TL;DR: The proposal that newly formed PLP may be transferred from either enzyme to apo-B(6)-enzymes by direct channeling, an efficient, exclusive, and protected means of delivery of the highly reactive PLP.
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Pyridoxal 5-Phosphate Enzymes as Targets for Therapeutic Agents
Alessio Amadasi,Mariarita Bertoldi,Roberto Contestabile,Stefano Bettati,Barbara Cellini,Martino L. di Salvo,Carla Borri-Voltattorni,Francesco Bossa,Andrea Mozzarelli +8 more
TL;DR: The relevance of recent genomic analysis of PLP-dependent enzymes for the selection of drug targets is discussed, and enzymes that have been recently characterized and proposed as drug targets are reported.
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Molecular mechanisms of the non-coenzyme action of thiamin in brain: biochemical, structural and pathway analysis
Garik Mkrtchyan,Vasily A. Aleshin,Yulia Parkhomenko,Thilo Kaehne,Martino L. di Salvo,Alessia Parroni,Roberto Contestabile,Andrey I. Vovk,Lucien Bettendorff,Victoria I. Bunik +9 more
TL;DR: This interdisciplinary study shows that thiamin is not only a coenzyme for acetyl-CoA production, but also an allosteric regulator of acetyl -CoA metabolism including regulatory acetylation of proteins and acetylcholine biosynthesis.
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L-Threonine aldolase, serine hydroxymethyltransferase and fungal alanine racemase A subgroup of strictly related enzymes specialized for different functions
Roberto Contestabile,Alessandro Paiardini,Stefano Pascarella,Martino L. di Salvo,Simona D'Aguanno,Francesco Bossa +5 more
TL;DR: L-threonine aldolase from Escherichia coli is able to catalyse the same range of reactions catalysed by SHMT, with the exception of the serine hydroxymethyltransferase reaction, which strongly suggests that SHMT and l-th Frenchmanine a Aldolase are closely related enzymes specialized for different functions.
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Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase.
TL;DR: The three‐dimensional fold of the human enzyme is very similar to those of the E. coli and yeast enzymes, and the binding sites for the tightly bound FMN and substrate are highly conserved.