Literature DB >> 3139452

Two ionic forms of exoglucanase in yeast secretory mutants.

G Larriba1, M Ramírez, L M Hernández, I Olivero, R D Basco.   

Abstract

Analysis of exoglucanase activity accumulated by sec mutants from Saccharomyces cerevisiae revealed the presence of two ionic forms of the major exoglucanase (exo II) secreted into the culture medium. From the accumulation pattern of representative sec mutants and the carbohydrate composition it appears that the less acidic form is converted into the more acidic one by addition of one phosphate to one of the oligosaccharide cores as the enzyme progresses through the secretory pathway. Exoglucanase I, the heavier isoenzyme, was not accumulated by the mutants. Accordingly, it should arise from exoglucanase II after the execution point of sec1 mutation.

Entities:  

Mesh:

Substances:

Year:  1988        PMID: 3139452     DOI: 10.1016/0014-5793(88)80170-4

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  A similar protein portion for two exoglucanases secreted by Saccharomyces cerevisiae.

Authors:  M Ramírez; L M Hernández; G Larriba
Journal:  Arch Microbiol       Date:  1989       Impact factor: 2.552

2.  Selective elongation of the oligosaccharide attached to the second potential glycosylation site of yeast exoglucanase: effects on the activity and properties of the enzyme.

Authors:  R D Basco; L M Hernández; M D Muñox; I Olivero; E Andaluz; F Del Rey; G Larriba
Journal:  Biochem J       Date:  1994-12-15       Impact factor: 3.857

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.