@prefix pubblicazioni: . @prefix unitaDiPersonaleInterno: . @prefix prodotto: . unitaDiPersonaleInterno:MATRICOLA9808 pubblicazioni:autoreCNRDi prodotto:ID305745 . unitaDiPersonaleInterno:MATRICOLA8954 pubblicazioni:autoreCNRDi prodotto:ID305745 . @prefix prodottidellaricerca: . @prefix istituto: . istituto:CDS010 prodottidellaricerca:prodotto prodotto:ID305745 . @prefix modulo: . modulo:ID8341 prodottidellaricerca:prodotto prodotto:ID305745 . @prefix rdf: . @prefix retescientifica: . prodotto:ID305745 rdf:type retescientifica:ProdottoDellaRicerca , prodotto:TIPO1101 . @prefix rdfs: . prodotto:ID305745 rdfs:label "On the Mechanism of Escherichia coli Pyridoxal Kinase Inhibition by Pyridoxal and Pyridoxal 5'-phosphate (Articolo in rivista)"@en . @prefix xsd: . prodotto:ID305745 pubblicazioni:anno "2015-01-01T00:00:00+01:00"^^xsd:gYear ; pubblicazioni:doi "10.1016/j.bbapap.2015.01.013"^^xsd:string . @prefix skos: . prodotto:ID305745 skos:altLabel "
Martino L. di Salvo, Isabel Nogu\u00E9s, Alessia Parroni, Angela Tramonti, Teresa Milano, Stefano Pascarella, and Roberto Contestabile (2015)
On the Mechanism of Escherichia coli Pyridoxal Kinase Inhibition by Pyridoxal and Pyridoxal 5'-phosphate
in Biochimica et biophysica acta. Proteins and proteomics
"^^rdf:HTML ; pubblicazioni:autori "Martino L. di Salvo, Isabel Nogu\u00E9s, Alessia Parroni, Angela Tramonti, Teresa Milano, Stefano Pascarella, and Roberto Contestabile"^^xsd:string . @prefix ns11: . prodotto:ID305745 pubblicazioni:rivista ns11:ID68078 ; pubblicazioni:affiliazioni "Dipartimento di Scienze Biochimiche \\\"A. Rossi Fanelli\\\", \\\"Sapienza\\\" Universit\u00E0 di Roma, Piazzale Aldo Moro 5, 00185 Roma, Italy\nIstituto di Biologia Ambientale e Forestale, Consiglio Nazionale delle Ricerche, Via Salaria Km 29.300, 00015 Monterotondo Scalo, Roma, Italy\n Istituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Piazzale Aldo Moro 5, 00185 Roma, Italy"^^xsd:string ; pubblicazioni:titolo "On the Mechanism of Escherichia coli Pyridoxal Kinase Inhibition by Pyridoxal and Pyridoxal 5'-phosphate"^^xsd:string ; prodottidellaricerca:abstract "Pyridoxal 5'-phosphate (PLP), the catalytically active form of vitamin B6, plays a crucial role in several cellular processes. In most organisms, PLP is recycled from nutrients and degraded B6-enzymes in a salvage pathway that involves pyridoxal kinase (PLK), pyridoxine phosphate oxidase and phosphatase activities. Regulation of the salvage pathway is poorly understood. Escherichia coli possesses two distinct pyridoxal kinases, PLK1, which is the focus of the present work, and PLK2. From previous studies dating back to thirty years ago, pyridoxal (PL) was shown to inhibit E. coli PLK1 forming a covalent link with the enzyme. This inhibition was proposed to play a regulative role in vitamin B6 metabolism, although its details had never been clarified. Recently, we have shown that also PLP produced during PLK1 catalytic cycle acts as an inhibitor, forming a Schiff base with Lys229, without being released in the solvent. The question arises as to which is the actual inhibition mechanism by PL and PLP. In the present work, we demonstrated that also PL binds to Lys229 as a Schiff base. However, the isolated covalent PLK1-PL complex is not inactive but, in the presence of ATP, is able to catalyse the single turnover production of PLP, which binds tightly to the enzyme and is ultimately responsible for its inactivation. The inactivation mechanism mediated by Lys229 may play a physiological role in controlling cellular levels of PLP. This article is part of a Special Issue entitled: Cofactor-dependent proteins: evolution, chemical diversity and bio-applications." ; prodottidellaricerca:prodottoDi istituto:CDS010 , modulo:ID8341 ; pubblicazioni:autoreCNR unitaDiPersonaleInterno:MATRICOLA9808 , unitaDiPersonaleInterno:MATRICOLA8954 . ns11:ID68078 pubblicazioni:rivistaDi prodotto:ID305745 .