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 COOH-terminal 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 + RCHO⇌RCHO + R'CH2OH) without addition of an electron acceptor. Aliphatic alcohols and aldehydes of C2 to C4 were utilized in this reaction. © 1984, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.