Revisiting and revising the purinosome

Mol Biosyst. 2014 Mar 4;10(3):369-74. doi: 10.1039/c3mb70397e. Epub 2014 Jan 10.

Abstract

Some metabolic pathway enzymes are known to organize into multi-enzyme complexes for reasons of catalytic efficiency, metabolite channeling, and other advantages of compartmentalization. It has long been an appealing prospect that de novo purine biosynthesis enzymes form such a complex, termed the "purinosome." Early work characterizing these enzymes garnered scarce but encouraging evidence for its existence. Recent investigations led to the discovery in human cell lines of purinosome bodies-cytoplasmic puncta containing transfected purine biosynthesis enzymes, which were argued to correspond to purinosomes. New discoveries challenge both the functional and physiological relevance of these bodies in favor of protein aggregation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Cytoplasmic Granules / metabolism
  • Humans
  • Multienzyme Complexes / metabolism*
  • Protein Binding
  • Protein Transport
  • Proteins / metabolism
  • Purines / biosynthesis*

Substances

  • Multienzyme Complexes
  • Proteins
  • Purines
  • purine