000061942 001__ 61942
000061942 005__ 20230313141235.0
000061942 0247_ $$2doi$$a10.1038/s41598-017-07716-5
000061942 0248_ $$2sideral$$a100708
000061942 037__ $$aART-2017-100708
000061942 041__ $$aeng
000061942 100__ $$0(orcid)0000-0001-7202-4587$$aSebastián, María$$uUniversidad de Zaragoza
000061942 245__ $$aThe FAD synthetase from the human pathogen Streptococcus pneumoniae: a bifunctional enzyme exhibiting activity-dependent redox requirements
000061942 260__ $$c2017
000061942 5060_ $$aAccess copy available to the general public$$fUnrestricted
000061942 5203_ $$aProkaryotic bifunctional FAD synthetases (FADSs) catalyze the biosynthesis of FMN and FAD, whereas in eukaryotes two enzymes are required for the same purpose. FMN and FAD are key cofactors to maintain the flavoproteome homeostasis in all type of organisms. Here we shed light to the properties of the hitherto unstudied bacterial FADS from the human pathogen Streptococcus pneumoniae (SpnFADS). As other members of the family, SpnFADS catalyzes the three typical activities of prokaryotic FADSs: Riboflavin kinase (RFK), ATP:FMN:adenylyltransferase (FMNAT), and FAD pyrophosphorylase (FADpp). However, several SpnFADS biophysical properties differ from those of other family members. In particular; i) the RFK activity is not inhibited by the riboflavin (RF) substrate, ii) the FMNAT and FADSpp activities require flavin substrates in the reduced state, iii) binding of adenine nucleotide ligands is required for the binding of flavinic substrates/products and iv) the monomer is the preferred state. Collectively, our results add interesting mechanistic differences among the few prokaryotic bifunctional FADSs already characterized, which might reflect the adaptation of the enzyme to relatively different environments. In a health point of view, differences among FADS family members provide us with a framework to design selective compounds targeting these enzymes for the treatment of diverse infectious diseases.
000061942 536__ $$9info:eu-repo/grantAgreement/ES/DGA/B89$$9info:eu-repo/grantAgreement/ES/MICINN/CTQ2013-44367-C2-2-P$$9info:eu-repo/grantAgreement/ES/MINECO/BFU2016-75633-P$$9info:eu-repo/grantAgreement/ES/MINECO/BIO2013-42978-P$$9info:eu-repo/grantAgreement/ES/MINECO/BIO2016-75183-P
000061942 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000061942 590__ $$a4.122$$b2017
000061942 591__ $$aMULTIDISCIPLINARY SCIENCES$$b12 / 64 = 0.188$$c2017$$dQ1$$eT1
000061942 592__ $$a1.533$$b2017
000061942 593__ $$aMultidisciplinary$$c2017$$dQ1
000061942 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000061942 700__ $$aLira-Navarrete, Erandi
000061942 700__ $$aSerrano, Ana$$uUniversidad de Zaragoza
000061942 700__ $$0(orcid)0000-0003-3459-8605$$aMarcuello, Carlos
000061942 700__ $$0(orcid)0000-0001-5702-4538$$aVelázquez-Campoy, Adrián$$uUniversidad de Zaragoza
000061942 700__ $$0(orcid)0000-0001-7460-5916$$aLostao, Anabel$$uUniversidad de Zaragoza
000061942 700__ $$0(orcid)0000-0002-3122-9401$$aHurtado-Guerrero, Ramón$$uUniversidad de Zaragoza
000061942 700__ $$0(orcid)0000-0001-8743-0182$$aMedina, Milagros$$uUniversidad de Zaragoza
000061942 700__ $$0(orcid)0000-0001-9047-0046$$aMartínez-Júlvez, Marta$$uUniversidad de Zaragoza
000061942 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000061942 773__ $$g7, 7609 (2017), [15 pp]$$pSci. rep.$$tScientific Reports$$x2045-2322
000061942 8564_ $$s3120947$$uhttps://zaguan.unizar.es/record/61942/files/texto_completo.pdf$$yVersión publicada
000061942 8564_ $$s110604$$uhttps://zaguan.unizar.es/record/61942/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000061942 909CO $$ooai:zaguan.unizar.es:61942$$particulos$$pdriver
000061942 951__ $$a2023-03-13-13:54:21
000061942 980__ $$aARTICLE