Literature DB >> 241407

Regulatory responses of arginine deiminase in whole cells of Clostridium sporogenes.

V Venugopal, P Harikumar, S N Doke, U S Kumta.   

Abstract

Arginine deiminase (EC 3.5.3.6) has been shown to have regulatory properties. The activity was observed to be sigmoidal with respect to substrate concentrations. Addition of histidine to the system caused the abolition of sigmoidal responses. The regulatory properties of the enzyme as well as the desensitising action of histidine could also be demonstrated with whole cell suspensions. The pH of the system also seemed to influence modulations in the enzyme.

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Year:  1975        PMID: 241407     DOI: 10.1016/0005-2744(75)90080-7

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  Regulation of the arginine dihydrolase pathway in Clostridium sporogenes.

Authors:  V Venugopal; G B Nadkarni
Journal:  J Bacteriol       Date:  1977-08       Impact factor: 3.490

Review 2.  Biosynthesis and metabolism of arginine in bacteria.

Authors:  R Cunin; N Glansdorff; A Piérard; V Stalon
Journal:  Microbiol Rev       Date:  1986-09

3.  Regulation of arginine-ornithine exchange and the arginine deiminase pathway in Streptococcus lactis.

Authors:  B Poolman; A J Driessen; W N Konings
Journal:  J Bacteriol       Date:  1987-12       Impact factor: 3.490

  3 in total

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