A new model for the membrane topology of glucose-6-phosphatase: the enzyme involved in von Gierke disease.

Abstract

Very recently we have proposed [Hemrika et al. (1997) Proc. Natl. Acad. Sci. USA 94, 2145-2149] that the active site of the vanadate-containing chloroperoxidase from the fungus Curvularia inaequalis, of which the tertiary structure is known, is structurally very similar to that of the membrane-bound mammalian glucose-6-phosphatases for which no structural data are available. The proposed active site of glucose-6-phosphatase, however, is incompatible with the six transmembrane-helix topology model that is currently used. Here we present a new topology model for glucose-6-phosphatase which is in agreement with all available data.

• Authors: W Hemrika, R Wever
• Journal: FEBS letters (FEBS Lett) Vol. 409 Issue 3 Pg. 317-9 (Jun 16 1997) ISSN: 0014-5793 [Print] England
• PMID: 9224681 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)

Chemical References

• Membrane Proteins
• Glucose-6-Phosphatase

Topics

• Amino Acid Sequence
• Animals
• Cell Membrane (enzymology)
• Glucose-6-Phosphatase (chemistry)
• Glycogen Storage Disease Type I (enzymology)
• Humans
• Membrane Proteins (chemistry)
• Models, Molecular
• Molecular Sequence Data