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 Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Two genes in the genome of Aspergillus niger, aglA and aglB, have been assigned to encode for α-d-galactosidases variant A and B. However, analyses of primary and 3D structures based on structural models of these two enzymes revealed significant differences in their active centers suggesting important differences in their specificity for the hydrolyzed carbohydrates. To test this unexpected finding, a large screening of libraries from 42 strains of filamentous fungi succeeded in identifying an enzyme from A. niger CCIM K2 that exhibited both α-galactosidase and α-N-acetylgalactosaminidase activities, with the latter activity predominating. The enzyme protein was sequenced, and its amino acid sequence could be unequivocally assigned to the enzyme encoded the aglA gene. Enzyme activity measurements and substrate docking clearly demonstrated the preference of the identified enzyme for α-N-acetyl-d-galactosaminide over α-d-galactoside. Thus, we provide evidence that the α-galactosidase type A gene aglA from A. niger in fact encodes a fully functional α-N-acetylgalactosaminidase using a retaining mechanism.

The -galactosidase type A gene aglA from Aspergillus niger encodes a fully functional -N-acetylgalactosaminidase