Heterologous Expression and Partial Characterization of a New Alanine Dehydrogenase from Amycolatopsis sulphurea

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dc.authoridAKTAS, Fatih/0000-0002-2031-298X
dc.contributor.authorAktas, Fatih
dc.date.accessioned2021-12-01T18:47:29Z
dc.date.available2021-12-01T18:47:29Z
dc.date.issued2021
dc.department[Belirlenecek]en_US
dc.description.abstractA novel alanine dehydrogenase (AlaDH; EC.1.4.1.1) was isolated from Amycolatopsis sulphurea and the AlaDH gene was cloned into a pET28a(+) plasmid and expressed in E. coli BL21 (DE3). The molecular mass of this enzyme was calculated as 41.09 kDa and the amino acid residues of the pure protein indicated the presence of N terminus polyhistidine tags. Its enzyme kinetic values were K-m 2.03 mM, k(cat) 13.24 (s(-1)), and k(cat)/K-m 6.53 (s(-1) mM(-1)). AlaDH catalyzes the reversible conversion of l-alanine and pyruvate, which has an important role in the TCA energy cycle. Maximum AlaDH activity occurred at about pH 10.5 and 25 degrees C for the oxidative deamination of l-alanine. AlaDH retained about 10% of its relative activity at 55 degrees C and it remained about 90% active at 50 degrees C. These findings show that the AsAlaDH from A. sulphurea has the ability to produce valuable molecules for various industrial purposes and could represent a new potential biocatalyst for biotechnological applications after further characterization and improvement of its catalytic properties.en_US
dc.identifier.doi10.1007/s10930-021-09982-9
dc.identifier.endpage347en_US
dc.identifier.issn1572-3887
dc.identifier.issn1573-4943
dc.identifier.issue3en_US
dc.identifier.pmid33818657en_US
dc.identifier.scopus2-s2.0-85103590061en_US
dc.identifier.scopusqualityN/Aen_US
dc.identifier.startpage342en_US
dc.identifier.urihttps://doi.org/10.1007/s10930-021-09982-9
dc.identifier.urihttps://hdl.handle.net/20.500.12684/10285
dc.identifier.volume40en_US
dc.identifier.wosWOS:000636954400001en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakPubMeden_US
dc.indekslendigikaynakScopusen_US
dc.institutionauthorAktas, Fatih
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofProtein Journalen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectAlanine dehydrogenaseen_US
dc.subjectAmycolatopsis sulphureaen_US
dc.subjectl-alanineen_US
dc.subjectOxidative deaminationen_US
dc.titleHeterologous Expression and Partial Characterization of a New Alanine Dehydrogenase from Amycolatopsis sulphureaen_US
dc.typeArticleen_US

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