1961•The Journal of General and Applied MicrobiologyOpen access

STUDIES ON MUTANTS OF BACILLUS SUBTILIS REQUIRING D-GLUTAMIC ACID

Haruo Momose, Yōnosuke Ikeda

Open full text 0 citations

Abstract

To look for the site of genetic block in the mutants of Bacillus subtilis K requring D-glutamic acid, several enzymes that were considered important for the biosynthesis of D- and L-glutamic acid were investigated. In mutant 3d, alanine racemase activity was about one tenth of that in the wild-type strain. It appears therefore that the block site in this mutant is between L-alanine and D-alanine. The mutant requires D-alanine, D-aspartic acid, or D-glutamic acid for growth.L-Alanine dehydrogenase activity was exceptionally low in mutant 2a. Because the mutant is able to synthesize L-aspartic acid and L-glutamic acid from fumarate too, the requirement of L-alanine, D-alanine, D-aspartic acid, or D-glutamic acid may be due to the slow reaction between pyruvate and L-alanine.Mutant 4a possesses a low activity of D-alanine-D-glutamic acid transaminase and responds to L-aspartic acid, L-glutamic acid, D-aspartic acid, or D-glutamic acid. The dependency on D-aspartic acid or D-glutamic acid is reasonable if these D-amino acids are produced from D-alanine by transamination, while the dependency on L-aspartic acid or L-glutamic acid remains unexplained. The correlation between a genetic damage and an enzyme formation was discussed in this connection.

Open-access reader

About this research paper

What this paper is about

To look for the site of genetic block in the mutants of Bacillus subtilis K requring D-glutamic acid, several enzymes that were considered important for the biosynthesis of D- and L-glutamic acid were investigated. In mutant 3d, alanine racemase activity was about one tenth of that in the wild-type strain. It appears therefore that the block site in this mutant is between L-alanine and D-alanine. The mutant requires D-alanine, D-aspartic acid, or D-glutamic acid for growth.L-Alanine dehydrogenase activity was exceptionally low in mutant 2a. Because the mutant is able to synthesize L-aspartic acid and L-glutamic acid from fumarate too, the requirement of L-alanine, D-alanine, D-aspartic acid, or D-glutamic acid may be due to the slow reaction between pyruvate and L-alanine.Mutant 4a possesses a low activity of D-alanine-D-glutamic acid transaminase and responds to L-aspartic acid, L-glutamic acid, D-aspartic acid, or D-glutamic acid. The dependency on D-aspartic acid or D-glutamic acid is reasonable if these D-amino acids are produced from D-alanine by transamination, while the dependency on L-aspartic acid or L-glutamic acid remains unexplained. The correlation between a genetic damage and an enzyme formation was discussed in this connection.

Why it matters

A significance statement is not available in the OpenAlex record.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

To look for the site of genetic block in the mutants of Bacillus subtilis K requring D-glutamic acid, several enzymes that were considered important for the biosynthesis of D- and L-glutamic acid were investigated. In mutant 3d, alanine racemase activity was about one tenth of that in the wild-type strain. It appears therefore that the block site in this mutant is between L-alanine and D-alanine. The mutant requires D-alanine, D-aspartic acid, or D-glutamic acid for growth.L-Alanine dehydrogenase activity was exceptionally low in mutant 2a. Because the mutant is able to synthesize L-aspartic acid and L-glutamic acid from fumarate too, the requirement of L-alanine, D-alanine, D-aspartic acid, or D-glutamic acid may be due to the slow reaction between pyruvate and L-alanine.Mutant 4a possesses a low activity of D-alanine-D-glutamic acid transaminase and responds to L-aspartic acid, L-glutamic acid, D-aspartic acid, or D-glutamic acid. The dependency on D-aspartic acid or D-glutamic acid is reasonable if these D-amino acids are produced from D-alanine by transamination, while the dependency on L-aspartic acid or L-glutamic acid remains unexplained. The correlation between a genetic damage and an enzyme formation was discussed in this connection.

Key concepts: Aspartic acid, Alanine, Glutamic acid, Biochemistry, Transamination, Bacillus subtilis, Transaminase, Amino acid

Related papers

Back to paper searchBrowse research topicsOriginal source
STUDIES ON MUTANTS OF BACILLUS SUBTILIS REQUIRING D-GLUTAMIC ACID — Research Paper | ScholarLens