Reference: Hur E and Wilson DK (2000) Crystallization and aldo-keto reductase activity of Gcy1p from Saccharomyces cerevisiae. Acta Crystallogr D Biol Crystallogr 56(Pt 6):763-5

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Abstract


Crystallization and preliminary X-ray diffraction studies of Gcy1p, an aldo-keto reductase from Saccharomyces cerevisiae, have been performed. Both the wild type and a double-mutant form of Gcy1p were crystallized using the hanging-drop method at 298 K; however, only the double-mutant form has so far yielded crystals suitable for X-ray diffraction analysis. These crystals belonged to the primitive monoclinic space group P2(1), with unit-cell parameters a = 50.94, b = 65.64, c = 86.23 A, beta = 92.64 degrees. Diffraction data were collected to 2.5 A. Assuming two 35 kDa subunits in the asymmetric unit yielded a V(m) of 2.06 A(3) Da(-1). Additionally, a kinetic study performed by measuring the rate of oxidation of NADPH in the presence of several substrates indicates that both wild-type and double-mutant proteins are enzymes possessing NADPH-dependent reductase activity.

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Journal Article | Research Support, Non-U.S. Gov't | Research Support, U.S. Gov't, P.H.S.
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Hur E, Wilson DK
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