The enzyme 4-oxalocrotonate tautomerase (4-OT) is part of a catabolic pathway for aromatic hydrocarbons in Pseudomonas putida mt-2, where it catalyzes the conversion of 2-hydroxy-2,4-hexadienedioate(1) to 2-oxo-3-hexenedioate(2). 4-OT is a member of the tautomerase superfamily, a group of homologous proteins that are characterized by a β-α-β structural fold and a catalytic amino-terminal prolin...

Two different isoenzymes of fructose-P2 aldolase can be resolved by chromatography of crude spinach leaf extracts on DEAE-cellulose columns. The acidic isoenzyme comprises about 85% of the total leaf aldolase activity. The two forms differ in primary structure as judged by their distinctive amino acid compositions, tryptic peptide patterns, and immunological properties. Only the acidic isoenzym...

One-pot multistep stereoselective cascade reactions were implemented for the straightforward synthesis of various nitrocyclitols. Two kinases, an aldolase and a phosphatase were involved in this process together with a spontaneous intramolecular Henry reaction to provide a nitrocyclitol moiety. The C-C bond formation catalyzed by the aldolase and the nitroaldol reaction were key steps to build ...

Fructose 1,6-diphosphate aldolase from cells of Bacillus cereus appears to be typical Class II aldolase as judged by its functional and physical properties. Spore and vegetative cell aldolase had similar enzymatic, immunochemical, and heat resistance properties in the absence of calcium, but they differed in their thermal stabilities in the presence of calcium, their Stokes' radii, their mobili...

Dihydroneopterin aldolase (EC 4.1.2.25) is one of the enzymes of folate synthesis that remains to be cloned and characterized from plants. This enzyme catalyzes conversion of 7,8-dihydroneopterin (DHN) to 6-hydroxymethyl-7,8-dihydropterin, and is encoded by the folB gene in Escherichia coli. The E. coli FolB protein also mediates epimerization of DHN to 7,8-dihydromonapterin. Searches of the Ar...

We review recent developments and applications of aldolase-type organocatalytic direct transformations in aqueous media without addition of organic solvent.

N-Bromoacetylethanolamine phosphate, prepared by the bromoacetylation of ethanolamine phosphate, has been tested as an active site-specilic reagent for rabbit and rat muscle fructose diphosphate aldolases. The reagent inactivates both enzymes, and inactivation is prevented by substrates or competitive inhibitors. Loss of activity is pseudo-first order until the later stages of inactivation, and...