Structural features of the glycogen branching enzyme encoding genes from aspergilli.

Microbiol Res

Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-ku, Nagoya-shi, Aichi 464-8601, Japan.

Published: January 2003

AI Article Synopsis

  • A maltose binding protein, named p78, was successfully purified from the fungus Aspergillus nidulans using a single chromatography step.
  • The amino acid sequence of p78 showed significant similarities to glycogen branching enzymes found in humans and yeast, confirming its branching enzyme activity.
  • Genomic and cDNA libraries were used to isolate and sequence the gene encoding GBE (p78), revealing strong sequence identity with GBEs from other fungi and even humans, suggesting evolutionary conservation of this enzyme function.

Article Abstract

A maltose binding protein, p78, was purified to homogeneity from Aspergillus nidulans by a single column chromatography step on cross-linked amylose. The partial amino acid sequence was highly homologous to the glycogen branching enzymes (GBEs) of human and yeast, and p78 did show branching enzyme activity. The genomic gene and its cDNA encoding GBE (p78) were isolated from the A. nidulans genomic and cDNA libraries. Furthermore, a cDNA encoding A. oryzae GBE was entirely sequenced. A. nidulans GBE shared overall and significant amino acid sequence identity with GBEs from A. oryzae (83.9%), Saccharomyces cerevisiae (61.1%) and human (63.0%), and with starch branching enzymes from green plants (55-56%).

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http://dx.doi.org/10.1078/0944-5013-00170DOI Listing

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