Purification and characterization of cytoplasmic NAD-dependent polypropylene glycol dehydrogenase from Stenotrophomonas maltophilia.
The oxidizing enzyme NAD(+)-dependent polypropylene glycol dehydrogenase (PPG-DH) was purified to homogeneity from the cytoplasmic fraction of Stenotrophomonas maltophilia grown on polypropylene glycol (diol type) 2000. The purified enzyme consisted of a homotetrameric protein (37 kDa subunit) with a molecular mass of around 154 kDa. The N-terminal amino acid sequence (25 residues) showed similarity to the sequences of NAD(+)-dependent secondary alcohol dehydrogenases and NADH-dependent reductases. The enzyme preferentially oxidized medium-chain secondary alcohols, di- and tri-propylene glycols and polypropylene glycols including those with secondary alcohol groups in their molecular structure. Consequently, the enzyme was classified into a group of NAD(+)-dependent secondary alcohol dehydrogenases.
Tachibana
Shinjiro
S
Department of Bioscience and Biotechnology, Faculty of Agriculture, University of the Ryukyus, Okinawa, Japan.
Naka
Naohito
N
Kawai
Fusako
F
Yasuda
Masaaki
M
D000426:Alcohol Dehydrogenase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D000595:Amino Acid Sequence; D003593:Cytoplasm / Q000201:enzymology; D008969:Molecular Sequence Data; D009243:NAD / Q000378:metabolism*; D011108:Polymers / Q000378:metabolism*; D011409:Propylene Glycols / Q000378:metabolism*; D020615:Stenotrophomonas maltophilia / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development / Q000302:isolation & purification; D013379:Substrate Specificity
D011108:Polymers; D011409:Propylene Glycols; D009243:NAD; C012504:polypropylene glycol; D000426:Alcohol Dehydrogenase