Properties of formaldehyde dismutation catalyzing enzyme of Pseudomonas putida F61.

スポンサーリンク

概要

• 論文の詳細を見る

• 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.

• 公益社団法人 日本農芸化学会の論文

著者

• SHIMAO Masayuki

  Department of Environmental Chemistry and Technology, Tottori University

関連論文

• Properties of formaldehyde dismutation catalyzing enzyme of Pseudomonas putida F61.

スポンサーリンク