Literature DB >> 2897937

Structural requirements of choline derivatives for 'conversion' of pneumococcal amidase. A new single-step procedure for purification of this autolysin.

J M Sanz1, R Lopez, J L Garcia.   

Abstract

Tertiary amines appear to be the minimal structure needed to convert in vitro the inactive form (E-form) of pneumococcal amidase to the catalytic active form (C-form). Diethylethanolamine was one of the compounds that converted the E-form, a finding that has been used successfully to develop an affinity chromatography system in DEAE-cellulose for the rapid and efficient purification of lytic enzymes of pneumococcus and its bacteriophages.

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Year:  1988        PMID： 2897937     DOI： 10.1016/0014-5793(88)80759-2

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  24 in total

1.  Protein-bound choline is released from the pneumococcal autolytic enzyme during adsorption of the enzyme to cell wall particles.

Authors:  Z Markiewicz; A Tomasz
Journal:  J Bacteriol       Date:  1990-05       Impact factor: 3.490

2.  Chimeric phage-bacterial enzymes: a clue to the modular evolution of genes.

Authors:  E Díaz; R López; J L García
Journal:  Proc Natl Acad Sci U S A       Date:  1990-10       Impact factor: 11.205

3.  Characterization of the pneumococcal bacteriophage HB-3 amidase: cloning and expression in Escherichia coli.

Authors:  A Romero; R Lopez; P Garcia
Journal:  J Virol       Date:  1990-01       Impact factor: 5.103

4.  Generation and properties of a Streptococcus pneumoniae mutant which does not require choline or analogs for growth.

Authors:  J Yother; K Leopold; J White; W Fischer
Journal:  J Bacteriol       Date:  1998-04       Impact factor: 3.490

5.  Structure of the beta-galactosidase gene from Thermus sp. strain T2: expression in Escherichia coli and purification in a single step of an active fusion protein.

Authors:  A Vian; A V Carrascosa; J L García; E Cortés
Journal:  Appl Environ Microbiol       Date:  1998-06       Impact factor: 4.792

6.  Characterization of LytA-like N-acetylmuramoyl-L-alanine amidases from two new Streptococcus mitis bacteriophages provides insights into the properties of the major pneumococcal autolysin.

Authors:  Patricia Romero; Rubens López; Ernesto García
Journal:  J Bacteriol       Date:  2004-12       Impact factor: 3.490

7.  Accumulation of partly folded states in the equilibrium unfolding of the pneumococcal choline-binding module C-LytA.

Authors:  Beatriz Maestro; Jesús M Sanz
Journal:  Biochem J       Date:  2005-04-15       Impact factor: 3.857

8.  EJ-1, a temperate bacteriophage of Streptococcus pneumoniae with a Myoviridae morphotype.

Authors:  E Díaz; R López; J L García
Journal:  J Bacteriol       Date:  1992-09       Impact factor: 3.490

9.  Role of the major pneumococcal autolysin in the atypical response of a clinical isolate of Streptococcus pneumoniae.

Authors:  E Díaz; R López; J L García
Journal:  J Bacteriol       Date:  1992-09       Impact factor: 3.490

10.  Characterization of Ejl, the cell-wall amidase coded by the pneumococcal bacteriophage Ej-1.

Authors:  José L Sáiz; Consuelo López-Zumel; Begoña Monterroso; Julio Varea; José Luis R Arrondo; Ibon Iloro; José L García; José Laynez; Margarita Menéndez
Journal:  Protein Sci       Date:  2002-07       Impact factor: 6.725
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