Bacterial alpha-glucan phosphorylases

FEMS Microbiol Lett. 1999 Feb 15;171(2):73-9. doi: 10.1111/j.1574-6968.1999.tb13414.x.

Abstract

Although glycogen and other alpha-1,4-D-glucan storage polysaccharides are present in many bacteria, only few glucan phosphorylases from bacteria have been identified and characterised on the protein or gene level. All bacterial phosphorylases follow the same catalytic mechanisms as their plant and vertebrate counterparts, but differ considerably in terms of their substrate specificity and regulation. The catalytic domains are highly conserved while the regulatory sites are only poorly conserved. The degree of conservation between bacterial and mammalian phosphorylases is comparable to that of other non-mammalian and mammalian alpha-glucan phosphorylases. Only for maltodextrin phosphorylase from E. coli the physiological role of the enzyme in the utilisation of maltodextrins is known in detail; that of all other phosphorylases remains still unclear. Roles in regulation of endogenous glycogen metabolism in periods of starvation, and sporulation, stress response or quick adaptation to changing environments are imaginable.

Publication types

  • Review

MeSH terms

  • Bacterial Proteins / metabolism*
  • Escherichia coli / enzymology*
  • Glucosyltransferases / metabolism*
  • Phosphorylases / metabolism*

Substances

  • Bacterial Proteins
  • Glucosyltransferases
  • Phosphorylases
  • maltodextrin phosphorylase