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Catalytic properties of recombinant 3-hydroxy-3-methylglutaryl coenzyme A synthase-1 from Blattella germanica.

作者信息

Cabañó J, Buesa C, Hegardt F G, Marrero P F

机构信息

Unidad de Bioquímica, Facultad de Farmacia, Barcelona, Spain.

出版信息

Insect Biochem Mol Biol. 1997 Jun;27(6):499-505. doi: 10.1016/s0965-1748(97)00024-6.

Abstract

Blattella germanica is the first organism in which two cytosolic HMG-CoA synthase genes have been described: HMGS-1 (Martínez-González et al., 1993b) and HMGS-2 (Buesa et al., 1994). The HMGS-1 gene showed special features, which led us to characterize the kinetic properties of the enzyme it encodes. Here we report the expression of recombinant HMGS-1, the protocol of enzyme purification, and the measurement of kinetic parameters. The K(m) for acetyl-CoA is 15.2 microM and the Ki for the other substrate, acetoacetyl-CoA, is 1.26 microM, both similar to that of yeast, ox, and chicken liver enzymes; the Vmax of HMGS-1 measured in this paper is 66 mU, which is the lowest Vmax of the HMG-CoA synthases reported to date.

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