Literature DB >> 9661793

[Protein engineering of uridine phosphorylase from Escherichia coli K-12. I. Cloning and expression of uridine phosphorylase genes from Klebsiella aerogenes and Salmonella typhimurium in E. coli].

V P Veĭko1, D V Chebotaev, I V Ovcharova, L B Gul'ko.   

Abstract

Genes of uridine phosphorylases (udp) from Klebsiella aerogenes and Salmonella typhimurium were cloned and expressed. Highly effective producer strains of the corresponding proteins were constructed. Enzymic properties of the UPases obtained were studied and compared with those from the Escherichia coli enzyme. Mutant forms of UPase from E. coli (D5E, D5N, D5A) were prepared by site-directed mutagenesis techniques. It was shown that the Asp5 residue plays an insignificant role in the formation of the active form of the protein.

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Year:  1998        PMID: 9661793

Source DB:  PubMed          Journal:  Bioorg Khim        ISSN: 0132-3423


  1 in total

1.  Physicochemical characterization of uridine phosphorylase from Shewanella oneidensis MR-1.

Authors:  N N Mordkovich; T N Safonova; V A Manuvera; V P Veiko; K M Polyakov; K S Alekseev; S N Mikhailov; V O Popov
Journal:  Dokl Biochem Biophys       Date:  2013-08-23       Impact factor: 0.788

  1 in total

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