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  • Title: [Purification and characteristics of methanol dehydrogenase of Methylobacterium nodulans rhizosphere phytosymbionts].
    Author: Kuznetsova TA, Beschastnyĭ AP, Ponomareva ON, Trotsenko IuA.
    Journal: Prikl Biokhim Mikrobiol; 2012; 48(6):606-11. PubMed ID: 23330386.
    Abstract:
    Methanol dehydrogenase (MDG) of the facultative methylotrophic phytosymbiont Methylobacterium nodulans has been purified for the first time to an electrophoretically homogeneous state and characterized. The native protein with a molecular mass of 70 kDa consists of large (60 kDa) and small (6 kDa) subunits. The purified protein displayed a specter identical to that of pyrochinolinchinon (PCC)-containing MDGs (pI 8.7, pH optimum in the range 9-10). The enzyme was inactive in the absence of ammonium or methylamine and exhibited a wide substrate specificity with regard to C1-C2 alcohols with the highest affinity to methanol (K(M) = 70 mM), but it did not oxidize benzyl and secondary alcohols. The apparent values of K(M) to primary alcohols increased with the length of the carbonic chain. The enzyme was characterized by a high stability level even in the absence of a substrate. An immobilized enzyme was used for amperometric methanol detection.
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