Purification, characterization, and cloning of a bifunctional molybdoenzyme with hydratase and alcohol dehydrogenase activity.
A bifunctional hydratase/alcohol dehydrogenase was isolated from the cyclohexanol degrading bacterium Alicycliphilus denitrificans DSMZ 14773. The enzyme catalyzes the addition of water to α,β-unsaturated carbonyl compounds and the subsequent alcohol oxidation. The purified enzyme showed three subunits in SDS gel, and the gene sequence revealed that this enzyme belongs to the molybdopterin binding oxidoreductase family containing molybdopterins, FAD, and iron-sulfur clusters.
Biocatalysis and Organic Chemistry, Department of Biotechnology, Delft University of Technology, Delft, The Netherlands. j.jin@tudelft.nl
Jianfeng
J
Jin
Adrie J J
AJ
Straathof
Martijn W H
MW
Pinkse
Ulf
U
Hanefeld
D000426:Alcohol Dehydrogenase / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*; D003001:Cloning, Molecular; D003067:Coenzymes / Q000378:metabolism; D042621:Comamonadaceae / Q000201:enzymology* / Q000235:genetics; D004269:DNA, Bacterial / Q000737:chemistry / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D006836:Hydro-Lyases / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*; D054354:Iron Carbonyl Compounds / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D008667:Metalloproteins / Q000378:metabolism; D008969:Molecular Sequence Data; D000090006:Molybdenum Cofactors; D021122:Protein Subunits; D011621:Pteridines / Q000378:metabolism; D017422:Sequence Analysis, DNA
D000426:Alcohol Dehydrogenase; D003067:Coenzymes; D004269:DNA, Bacterial; D005182:Flavin-Adenine Dinucleotide; D006836:Hydro-Lyases; D054354:Iron Carbonyl Compounds; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D000090006:Molybdenum Cofactors; D021122:Protein Subunits; D011621:Pteridines; C022261:molybdopterin