Enzymatic Production of Glyoxal from Ethylene Glycol Using Alcohol Oxidase from Methanol Yeast.

A new oxidative reaction of ethylene glycol was found with two alcohol oxidases from methanol yeast, Candida sp. and Pichia pastoris. Both alcohol oxidases oxidized ethylene glycol to glyoxal via glycolaldehyde.

An open reading frame in the Rhodospirillum rubrum plasmid, pKY1, similar to algA, encoding the bifunctional enzyme phosphomannose isomerase-guanosine diphospho-D-mannose pyrophosphorylase (PMI-GMP).

The nucleotide sequence of a BglII fragment (3188 bp) from the plasmid pKY1 of Rhodospirillum rubrum was determined. A significant similarity was found between the amino acid sequences deduced from the nucleotide sequence of BglII fragment with that of algA, encoding the bifunctional enzyme with both the activities of phosphomannose isomerase and guanosine diphospho-D-mannose pyrophosphorylase of Pseudomonas aeruginosa.

Vitamin B6 biosynthesis and glycolate reductase in Flavobacterium sp. 238-7.

An enzyme which reduces glycolate to glycolaldehyde as the first step of the biosynthesis of vitamin B6 was studied using the particulate fraction of Flavobacterium sp. 238-7, a vitamin B6 producer. The enzyme catalyzes the reduction of glycolate in the presence of NADPH, but not the oxidation of glycolaldehyde, and is designated as glycolate reductase.