cheminform abstract: aldolase antibodies of remarkable scope

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1998 biochemical syntheses, microbiological syntheses biochemical syntheses, microbiological syntheses O 0035 26 - 048 Aldolase Antibodies of Remarkable Scope. Aldolase antibodies 38C2 and 33F12 are shown to catalyze intermolecular ketone–ketone, ketone– aldehyde, aldehyde–ketone, and aldehyde–aldehyde aldol addition reactions and, in some cases, to catalyze their subsequent dehydration to yield aldol condensation products. 23 Donors and 16 acceptors are identified as substrates for these catalysts. Studies of retroaldol reactions demonstrate that the antibodies provide up to 10 8 -fold enhanced efficiency relative to simple amine catalyzed reactions. — (HOFFMANN, T.; ZHONG, G.; LIST, B.; SHABAT, D.; ANDERSON, J.; GRAMATIKOVA, S.; LERNER, R. A.; BARBAS, C. F. III; J. Am. Chem. Soc. 120 (1998) 12, 2768-2779; Dep. Mol. Biol. Chem., Scripps Res. Inst., San Diego, La Jolla, CA 92037, USA; EN) 1

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Page 1: ChemInform Abstract: Aldolase Antibodies of Remarkable Scope

1998 biochemical syntheses, microbiological syntheses

biochemical syntheses, microbiological synthesesO 0035

26 - 048Aldolase Antibodies of Remarkable Scope. — Aldolase antibodies38C2 and 33F12 are shown to catalyze intermolecular ketone–ketone, ketone–aldehyde, aldehyde–ketone, and aldehyde–aldehyde aldol addition reactionsand, in some cases, to catalyze their subsequent dehydration to yield aldolcondensation products. 23 Donors and 16 acceptors are identified as substratesfor these catalysts. Studies of retroaldol reactions demonstrate that theantibodies provide up to 108-fold enhanced efficiency relative to simple aminecatalyzed reactions. — (HOFFMANN, T.; ZHONG, G.; LIST, B.; SHABAT,D.; ANDERSON, J.; GRAMATIKOVA, S.; LERNER, R. A.; BARBAS, C. F.III; J. Am. Chem. Soc. 120 (1998) 12, 2768-2779; Dep. Mol. Biol. Chem.,Scripps Res. Inst., San Diego, La Jolla, CA 92037, USA; EN)

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