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2000•Angewandte Chemie International EditionOpen access

Cofactor-Bound Cross-Linked Enzyme Crystals (CLEC) of Alcohol Dehydrogenase

Nancy St. Clair, Yi-Fong Wang, Alexey L. Margolin

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Abstract

Horse liver alcohol dehydrogenase was crystallized in the presence of its cofactor. The cross-linked enzyme crystals (CLECs) produced showed good catalytic activity without the addition of extra cofactor (see scheme). The enantioselectivity and stereochemical preference of the CLEC were the same as with the soluble enzyme, and both cofactor and enzyme were considerably more stable in CLEC form. Cofactor regeneration studies on the reduction of cinnemaldehyde indicate the potential for a high level of catalyst productivity.

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Horse liver alcohol dehydrogenase was crystallized in the presence of its cofactor. The cross-linked enzyme crystals (CLECs) produced showed good catalytic activity without the addition of extra cofactor (see scheme). The enantioselectivity and stereochemical preference of the CLEC were the same as with the soluble enzyme, and both cofactor and enzyme were considerably more stable in CLEC form. Cofactor regeneration studies on the reduction of cinnemaldehyde indicate the potential for a high level of catalyst productivity.

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Available abstract

Horse liver alcohol dehydrogenase was crystallized in the presence of its cofactor. The cross-linked enzyme crystals (CLECs) produced showed good catalytic activity without the addition of extra cofactor (see scheme). The enantioselectivity and stereochemical preference of the CLEC were the same as with the soluble enzyme, and both cofactor and enzyme were considerably more stable in CLEC form. Cofactor regeneration studies on the reduction of cinnemaldehyde indicate the potential for a high level of catalyst productivity.

Key concepts: Alcohol dehydrogenase, Cofactor, Enzyme, Chemistry, Alcohol oxidoreductase, Alcohol, Biochemistry, Dehydrogenase

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