A new model for the membrane topology of glucose-6-phosphatase: the enzyme involved in von Gierke disease.
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.
Hemrika
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W
E.C. Slater Institute, Amsterdam, The Netherlands.
Wever
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R
D000595:Amino Acid Sequence; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D005952:Glucose-6-Phosphatase / Q000737:chemistry*; D005953:Glycogen Storage Disease Type I / Q000201:enzymology*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data
D008565:Membrane Proteins; D005952:Glucose-6-Phosphatase