English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

An aspartate kinase-deficient mutant ofThermus thermophilus , AK001, was constructed. The mutant strain did not grow in a minimal medium, suggesting thatT. thermophilus contains a single aspartate kinase. Growth of the mutant strain was restored by addition of both threonine and methionine, while addition of lysine had no detectable effect on growth. To further elucidate the lysine biosynthetic pathway inT. thermophilus , lysine auxotrophic mutants ofT. thermophilus were obtained by chemical mutagenesis. For all lysine auxotrophic mutants, growth in a minimal medium was not restored by addition of diaminopimelic acid, whereas growth of two mutants was restored by addition of α-aminoadipic acid, a precursor of lysine in biosynthetic pathways of yeast and fungi. ABam HI fragment of 4.34 kb which complemented the lysine auxotrophy of a mutant was cloned. Determination of the nucleotide sequence suggested the presence of homoaconitate hydratase genes, termedhacA andhacB , which could encode large and small subunits of homoaconitate hydratase, in the cloned fragment. Disruption of the chromosomal copy ofhacA yielded mutants showing lysine auxotrophy which was restored by addition of α-aminoadipic acid or α-ketoadipic acid. All of these results indicated that inT. thermophilus , lysine was not synthesized via the diaminopimelic acid pathway, believed to be common to all bacteria, but via a pathway using α-aminoadipic acid as a biosynthetic intermediate.

journal of bacteriology

Aspartate Kinase-Independent Lysine Synthesis in an Extremely Thermophilic Bacterium, <i>Thermus thermophilus</i> : Lysine Is Synthesized via α-Aminoadipic Acid Not via Diaminopimelic Acid

Aspartate Kinase-Independent Lysine Synthesis in an Extremely Thermophilic Bacterium, Thermus thermophilus : Lysine Is Synthesized via α-Aminoadipic Acid Not via Diaminopimelic Acid