The resurgence of aldolase isozymes in cancerous tissues is a well-known but poorly understood phenomenon. This resurgence poses the problem of whether or not adult and fetal aldolase isozymes are produced by the same cells. For clarification of this question, the immunoperoxidase technique was used to locate aldolases A, B, and C in one type of fast-growing hepatoma, the LF hepatoma and, by co...

The synthesis of novel fluorogenic retro-aldol substrates for aldolase antibody 38C2 is described. These substrates are efficiently and specifically processed by antibody aldolases but not by natural cellular enzymes. Together, the fluorogenic substrates and antibody aldolases provide reporter gene systems that are compatible with living cells. The broad scope of the antibody aldolase allows fo...

The 2-deoxy-d-ribose-5-phosphate aldolase (DERA) offers access to highly desirable building blocks for organic synthesis by catalyzing a stereoselective C-C bond formation between acetaldehyde and certain electrophilic aldehydes. DERA´s potential is particularly highlighted by the ability to catalyze sequential, highly enantioselective aldol reactions. However, its synthetic use is limited by t...

Enamines and imines have long been recognized as key intermediates in enzyme catalysis, particularly within a class of enzymes organic chemists would very much like to emulate, the aldolases. Here we summarize the contributions of this laboratory to converting enzymatic enamines, and in some cases imines, into a versatile catalytic asymmetric strategy powered by small organic molecules.

Threonine aldolases catalyze the pyridoxal phosphate (PLP) dependent cleavage of threonine into glycine and acetaldehyde and play a major role in the degradation of this amino acid. In nature, L- as well as D-specific enzymes have been identified, but the exact physiological function of D-threonine aldolases (DTAs) is still largely unknown. Both types of enantio-complementary enzymes have a con...

1. A method is described for partial purification of the total aldolase of rabbit brain by ammonium sulphate precipitation followed by fractionation of the aldolase into five electrophoretically distinct forms. 2. The method allows a laboratory-scale preparation of the five aldolases. 3. With the exception of band 3 the fructose 1,6-diphosphate/fructose 1-phosphate activity ratios of the isolat...

In previous work from this laboratory, we have demonstrated the formation of a Schiff base intermediale between fructose 1,6-diphosphate aldolase and one of its substrates, dihydroxyacetone phosphate (l-3). Upon reduction of the intermediate with sodium borohydride, it is converted to a stable secondary amine derivative which has been isolated from the protein hydrolysates and identified as NG-...