Methanol oxidase

Methanol Oxidase is an enzyme that catalyzes the oxidation of methanol to formaldehyde. This enzyme plays a crucial role in the methanol metabolism pathway, particularly in certain microorganisms that utilize methanol as a source of carbon and energy.

Function

Methanol oxidase, also known as alcohol oxidase, is a flavoprotein that contains flavin adenine dinucleotide (FAD) as a prosthetic group. It catalyzes the reaction:

methanol + O2 → formaldehyde + H2O2

The enzyme is found in high concentrations in the peroxisomes of yeast cells that are growing on methanol as the sole carbon source. The formaldehyde produced by methanol oxidase is further oxidized to carbon dioxide and water, providing the cell with energy.

Structure

Methanol oxidase is a large, multimeric protein. The enzyme from the yeast Pichia pastoris is an octamer of identical subunits, each of which binds one molecule of FAD. The active site of the enzyme contains a conserved histidine residue that is thought to be involved in catalysis.

Biological Importance

Methanol oxidase is of significant biological importance due to its role in the metabolism of methanol. Certain microorganisms, such as Methylobacterium extorquens and Pichia pastoris, are able to utilize methanol as a sole source of carbon and energy. This ability is of particular interest in biotechnology, where these organisms are used for the production of recombinant proteins and other valuable products.

See Also

• Alcohol dehydrogenase
• Methanol dehydrogenase
• Formaldehyde dehydrogenase
• Pichia pastoris
• Methylobacterium extorquens