Biochemical characterization of wild-type and mutant isoamylases of Chlamydomonas reinhardtii supports a function of the multimeric enzyme organization in amylopectin maturation.

@article{Dauville2001BiochemicalCO,
  title={Biochemical characterization of wild-type and mutant isoamylases of Chlamydomonas reinhardtii supports a function of the multimeric enzyme organization in amylopectin maturation.},
  author={David Dauvill{\'e}e and Christophe Colleoni and Gr{\'e}gory Mouille and Matthew Morell and Christophe D'Hulst and Fabrice Wattebled and Luc Li{\'e}nard and David Delvall{\'e} and Jean Philippe Ral and Alan M Myers and Steven G Ball},
  journal={Plant physiology},
  year={2001},
  volume={125 4},
  pages={
          1723-31
        }
}
Chlamydomonas reinhardtii mutants of the STA8 gene produce reduced amounts of high amylose starch and phytoglycogen. In contrast to the previously described phytoglycogen-producing mutants of C. reinhardtii that contain no residual isoamylase activity, the sta8 mutants still contained 35% of the normal amount of enzyme activity. We have purified this residual isoamylase and compared it with the wild-type C. reinhardtii enzyme. We have found that the high-mass multimeric enzyme has reduced its… CONTINUE READING

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