Purification and characterization of formaldehyde dismutases of Methylobacterium sp. FD1. Issue 7 (2nd July 2020)

• Record Type: Journal Article
• Authors: Imoto, Seiji; Yonemitsu, Hiroshi; Totsui, Noriki; Kishimoto, Noboru
• Is Part Of: Bioscience, biotechnology, and biochemistry. Volume 84:Issue 7(2020)
• Page Start: 1444
• Page End: 1450
• Publication Date: 2020-07-02
• Subjects: Formaldehyde dismutase -- methanol:NDMA oxidoreductase activity -- Methylobacterium sp. FD1; Biotechnology -- Periodicals; Biochemistry -- Periodicals; 660.6
• DOI: 10.1080/09168451.2020.1751582
• Languages: English
• ISSNs: 0916-8451

Abstract

ABSTRACT: In the present study, we purified and characterized three formaldehyde dismutases (Fdms) (EC 1.2.98.1) (Fdm1, Fdm2, and Fdm3) of Methylobacterium sp. FD1. These Fdms (with His-tag) were produced in the recombinant E. coli and purified by immobilized metal affinity chromatography from the E. coli extracts. In each of the three Fdms, the enzyme-bound coenzyme was nicotinamide adenine dinucleotide (NAD(H)) and the enzyme-bound metal was zinc. The quaternary structures of these Fdms were estimated as homotetrameric. The optimal pHs and temperatures of Fdm1, Fdm2, and Fdm3 were approximately 6.5, 6.0, and 6.0, and 35°C, 25°C, and 30°C, respectively. The Km values of Fdm1, Fdm2, and Fdm3 were 621, 865, and 414 mM, respectively. These results were similar to the properties of already-known Fdms. However, each of the Fdms of FD1 had methanol: p -nitroso- N, N -dimethylaniline oxidoreductase activity that is not found in already-known Fdms. GRAPHICAL ABSTRACT: Formaldehyde dismutases with methanol: p -nitroso- N, N -dimethylaniline oxidoreductase activity of Methylobacterium sp. FD1. uf0001