Open AccessThe Saccharomyces cerevisiae YPR184w gene encodes the glycogen debranching enzyme
Author(s) -
Teste Marie Ange,
Enjalbert Brice,
Parrou Jean Luc,
François Jean M.
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb09410.x
Subject(s) - glycogen debranching enzyme , glycogen , biochemistry , glycogen synthase , biology , saccharomyces cerevisiae , glycogen branching enzyme , gene , microbiology and biotechnology
The YPR184w gene encodes a 1536‐amino acid protein that is 34–39% identical to the mammal, Drosophila melanogaster and Caenorhabditis elegans glycogen debranching enzyme. The N‐terminal part of the protein possesses the four conserved sequences of the α‐amylase superfamily, while the C‐terminal part displays 50% similarity with the C‐terminal of other eukaryotic glycogen debranching enzymes. Reliable measurement of α‐1,4‐glucanotransferase and α‐1,6‐glucosidase activity of the yeast debranching enzyme was determined in strains overexpressing YPR184w . The α‐1,4‐glucanotransferase activity of a partially purified preparation of debranching enzyme preferentially transferred maltosyl units than maltotriosyl. Deletion of YPR184w prevents glycogen degradation, whereas overexpression had no effect on the rate of glycogen breakdown. In response to stress and growth conditions, the transcriptional control of YPR184w gene, renamed GDB1 (for G lycogen D e B ranching gene), is strictly identical to that of other genes involved in glycogen metabolism.