Properties of formaldehyde dismutation catalyzing enzyme of Pseudomonas putida F61.

Abstract

Two forms of formaldehyde dismutase distinguishable on disc-gel electrophoresis were isolated from the cell-free extract of Pseudomonas putida F61. The mobilities on SDS-gel electrophoresis and the NH₂-terminal amino acids (arginine) of the two enzyme species were identical. The COOHterminal amino acid sequence was found to be -Ser-Gly-Lys. The enzyme was inhibited by carbonyl, reducing and sulfhydryl reagents. The enzyme catalyzed the cross-dismutation reaction between formaldehyde and an aldehyde, such as propionaldehyde, acrolein, butyraldehyde, isobutyraldehyde and crotonaldehyde. The enzyme also catalyzed a coupled oxidoreduction between an alcohol and an aldehyde (RCH₂OH+ R'CHORCHO+R'CH₂OH) without addition of an electron acceptor. Aliphatic alcohols and aldehydes of C₂ to C₄ were utilized in this reaction.