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PMID: 5650079 Published · ppublish English Journal Article

Regulation of nitrogen fixation in Azotobacter vinelandii OP and in an apparently partially constitutive mutant.

Journal of bacteriology ·Vol. 95 ·No. 5 ·1968-05-00 ·Pages 1721-6

Sorger GJ

Abstract

Methylamine and 2-methylalanine appeared to act as co-repressors of nitrogenase in Azotobacter vinelandii OP. They inhibited the growth of this organism on molecular nitrogen but not on nitrate, ammonia, or Casamino Acids; they prevented the formation of nitrogenase by cells transferred from repression to induction conditions; and they did not inhibit the activity of nitrogenase in vitro. A mutant of strain OP, selected on the basis of its relative resistance to methylalanine, appeared partially constitutive because nitrogenase in this strain was less sensitive to repressors than was the enzyme in the wild-type strain.

MeSH Terms
Alanine/pharmacology Amines/pharmacology Ammonia/pharmacology Azotobacter/drug effects,metabolism Enzyme Repression Glucosephosphate Dehydrogenase/metabolism Mutation Nitrogen Fixation Oxidoreductases/metabolism
Chemicals
Amines Ammonia Oxidoreductases Glucosephosphate Dehydrogenase Alanine
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Sorger G J
References (14)
14 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1968-05-00
Pages
1721-6
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC252202
Subset
IM
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