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

~~ A method has been developed for the continuous spectrophotometric assay of dihydroxy- acetone synthase present in methanol-grown yeasts. This enzyme catalyses the conden- sation of formaldehyde with a pentose phosphate (most probably xylulose 5-phosphate) to give dihydroxyacetone and glyceraldehyde 3-phosphate. The assay is based on the NADH- and ATP-linked formation of L-glycerol3-phosphate from dihydroxyacetone via the added coupling enzymes glycerol kinase and glycerol-3-phosphate dehydrogenase, and the reaction was followed by the decrease in absorbance at 340 nm. Using this assay, the pH optimum of the dihydroxyacetone synthase was shown to be 7-4 to 7.6. The enzyme, which catalyses a transketolase-like reaction, is a separate enzyme from the classical transketolase because their specific activities varied independently in Candida boidinii and Hansenula polymorpha grown on different substrates and the two enzyme activities could be separated by ion- exchange chromatography.

Pentose Phosphate-dependent Fixation of Formaldehyde by Methanol-grown Hansenula polymorpha and Candida boidinii