Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Alteration of bacillus-subtilis glutamine-synthetase results in overproduction of enzyme

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Dean, D. R.
  • Hoch, James
  • Aronson, A. I.

publication date

  • 1977

journal

  • Journal of Bacteriology  Journal

abstract

  • A mutational leading to glutamine auxotrophy was located near a 5-fluorouracil resistance marker in the citB-thyA region of the Bacillus subtilis chromosome. This mutation resulted in a glutamine synthetase with altered kinetic and feedback properties. The specific activity of manganese-stimulated glutamine synthetase activity in crude extracts was 18-fold higher, and the magnesium-stimulated activity was about 30% that of the wild type. Quantitation of the enzyme by precipitation with antibody prepared against pure enzyme confirmed the presence of high enzyme levels in the mutant. This mutation is very closely linked (recombination index of 0.03) to another glutamine auxotroph containing enzyme with altered electrophoretic and heat sensitivity properties. Mutations in the structural gene for glutamine synthetase may result not only in altered catalytic and regulatory properties but also in altered production of the enzyme.

subject areas

  • Alanine
  • Bacillus subtilis
  • Cell-Free System
  • Chromosome Mapping
  • Feedback
  • Genes
  • Glutamate-Ammonia Ligase
  • Glutamine
  • Glycine
  • Hot Temperature
  • Magnesium
  • Manganese
  • Mutation
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0021-9193

PubMed ID

  • 19424
scroll to property group menus

Additional Document Info

start page

  • 981

end page

  • 987

volume

  • 131

issue

  • 3

©2019 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support