Premium
NAD‐dependent, PQQ‐containing methanol dehydrogenase: a bacterial dehydrogenase in a multienzyme complex
Author(s) -
Duine J.A.,
Frank J.,
Berkhout M.P.J.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80249-5
Subject(s) - methanol dehydrogenase , nad+ kinase , methanol , alcohol dehydrogenase , dehydrogenase , chemistry , biochemistry , branched chain alpha keto acid dehydrogenase complex , formaldehyde dehydrogenase , glycerol 3 phosphate dehydrogenase , lactate dehydrogenase , enzyme , organic chemistry
Cell‐free extracts of methanol‐grown Nocardia sp. 239 only show significant dye‐linked methanol‐oxidizing activity when NAD + is added to the assay mixture. This activity resides in a multienzyme complex which could be resolved into 3 components, namely the methanol dehydrogenase, NAD‐dependent aldehyde dehydrogenase and NADH dehydrogenase. In its dissociated form, the methanol dehydrogenase no longer shows dye reduction and although rises in the absorbance values around 340 nm are seen on addition of methanol plus NAD + to the enzyme, this is not due to NADH production. However, dye reduction (NAD dependent) could be restored on incubating methanol dehydrogenase with the corresponding NADH dehydrogenase, obtained from the enzyme complex. It is concluded that this novel methanol dehydrogenase transfers the reducing equivalents, derived from methanol, directly to its associated NADH dehydrogenase via a mechanism in which NAD + and PQQ are involved.