Literature DB >> 1175596

Trans-N-deoxyribosylase: purification by affinity chromatography and characterization.

J Holguin, R Cardinaud.   

Abstract

trans-N-Deoxyribosylase (EC 2.4.2.6) is usually considered as a single protein catalyzing indifferently the transfer of the deoxyribosyl moiety to and from a purine or a pyrimidine base. Affinity chromatography of an extract from Lactobacillus helveticus with two types of ligands allowed the separation and purification of two distinct trans-N-deoxyribosylases. One catalyzes specifically the deoxyribosyl transfer to and from purine bases exclusively: trans-N-deoxyribosylase-I, the other catalyzes the transfer to and from pyrimidine and purine bases: trans-N-deoxyribosylase-II. A Tris inhibition study showed a markedly different susceptibility of the two enzymes. Preliminary results indicate that the purine-specific enzyme is a polymeric enzyme of molecular weight 86 000 (+/- 4000).

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Year:  1975        PMID: 1175596     DOI: 10.1111/j.1432-1033.1975.tb04163.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  3 in total

1.  Lactobacillus reuteri 2'-deoxyribosyltransferase, a novel biocatalyst for tailoring of nucleosides.

Authors:  Jesús Fernández-Lucas; Carmen Acebal; José V Sinisterra; Miguel Arroyo; Isabel de la Mata
Journal:  Appl Environ Microbiol       Date:  2010-01-04       Impact factor: 4.792

2.  Substrate specificity of the purine-2'-deoxyribonucleosidase of Crithidia luciliae.

Authors:  D J Steenkamp; T J Hälbich
Journal:  Biochem J       Date:  1992-10-01       Impact factor: 3.857

3.  New trends in nucleoside biotechnology.

Authors:  I A Mikhailopulo; A I Miroshnikov
Journal:  Acta Naturae       Date:  2010-07       Impact factor: 1.845

  3 in total

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