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A new model for the membrane topology of glucose‐6‐phosphatase: the enzyme involved in von Gierke disease
Author(s) -
Hemrika Wieger,
Wever Ron
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00530-9
Subject(s) - phosphatase , vanadate , topology (electrical circuits) , active site , glucose 6 phosphatase , transmembrane protein , biochemistry , enzyme , chemistry , membrane topology , membrane , biology , membrane protein , mathematics , receptor , combinatorics
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.