A modifier protein (M-protein), which increases the affinity of methanol dehydrogenase (MDH) for alcohols but decreases its affinity for formaldehyde, has been partially purified from and . Analysis was complicated by non-protein factors in bacterial extracts that are able to mimic M-protein in one of its functions - that of increasing the activity of MDH with butane- 1,3-diol in the dye-linked assay system. The 67 kDa polypeptide, previously identified as a subunit of the M-protein, is an unrelated cytoplasmic protein. The M-protein is exclusively periplasmic and is a multimeric protein with subunits of 45 kDa. The M-protein is active in the ‘physiological’ assay system with the specific cytochrome electron acceptor for MDH, lowering its affinity for formaldehyde. It has its maximum effect when the ratio of M-protein: MDH is 1:5 but its concentration in the periplasm is much lower than 20% of that of MDH.


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