EC - tert-butanol monooxygenase

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IntEnz Enzyme Nomenclature


Accepted name:
tert-butanol monooxygenase
Other names:
mdpJK (gene names)
tert-butyl alcohol monooxygenase
Systematic name:
tert-butanol,NADPH:oxygen oxidoreductase




The enzyme, characterized from the bacterium Aquincola tertiaricarbonis, is a Rieske nonheme mononuclear iron oxygenase. It can also act, with lower efficiency, on propan-2-ol, converting it to propane-1,2-diol. Depending on the substrate, the enzyme also catalyses EC, tert-amyl alcohol desaturase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  1. Schafer, F., Breuer, U., Benndorf, D., von Bergen, M., Harms, H. and Muller, R.H.
    Growth of Aquincola tertiaricarbonis L108 on tert-butyl alcohol leads to the induction of a phthalate dioxygenase-related protein and its associated oxidoreductase subunit.
    Eng. Life Sci. 7 : 512-519 (2007).
  2. Schuster, J., Schafer, F., Hubler, N., Brandt, A., Rosell, M., Hartig, C., Harms, H., Muller, R. H., Rohwerder, T.
    Bacterial degradation of tert-amyl alcohol proceeds via hemiterpene 2-methyl-3-buten-2-ol by employing the tertiary alcohol desaturase function of the Rieske nonheme mononuclear iron oxygenase MdpJ.
    J. Bacteriol. 194 : 972-981 (2012). [PMID: 22194447]

[EC created 2016]