Literature DB >> 3549359

dam methylase from E. coli. Circular dichroism investigations of the secondary structure and influence of S-adenosylmethionine.

A Kriebardis, W Guschlbauer.   

Abstract

The enzyme dam methylase which recognizes and methylates the adenine in the palindromic sequence GATC in DNA was isolated and the secondary structure was determined by CD spectroscopy and various predicting methods from the amino acid sequence. The interaction of dam methylase with S-adenosylmethionine was studied by CD spectroscopy indicating a decrease of the percentage of alpha-helix as the amount of S-adenosylmethionine bound to the enzyme was increased.

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Year:  1987        PMID: 3549359     DOI: 10.1016/0014-5793(87)81509-0

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


  1 in total

1.  The double role of methyl donor and allosteric effector of S-adenosyl-methionine for Dam methylase of E. coli.

Authors:  A Bergerat; W Guschlbauer
Journal:  Nucleic Acids Res       Date:  1990-08-11       Impact factor: 16.971

  1 in total

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