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/

Zendy Plus

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

Zendy Tools

Zendy Open

Some marine bacteria synthesize docosahexaenoic acid (DHA; C 22 ) and eicosapentaenoic acid (EPA; C 20 ) by enzyme complexes composed of four subunits (A-D). We recently revealed that β-ketoacyl synthase (KS C )/chain length factor (CLF)-like domains in the "C" subunit of DHA synthase catalyzed the last elongation step (C 20 o C 22 ) even though their amino acid sequences are very similar to those of EPA synthase. To investigate the amino acid residues controlling the product chain length, conserved residues in the KS C /CLF-like domains in DHA synthase were replaced with corresponding EPA synthase residues. Among 12 mutants, two CLF-like domain-mutated genes completely lost DHA productivity and produced trace amounts of EPA when coexpressed with dha-ABD in Escherichia coli , whereas when coexpressed with epa-ABD , they produced the same amounts of EPA as epa-ABCD . These results suggest that the product profiles were subtly controlled by several amino acid residues.

Subtle Control of Carbon Chain Length in Polyunsaturated Fatty Acid Synthases