Thermostable aldehyde dehydrogenase from psychrophile, Cytophaga sp. KUC-1: enzymological characteristics and functional properties.
We found the occurrence of NAD(P)(+)-dependent aldehyde dehydrogenase (EC1.2.1.5) in the cells of a psychrophile from Antarctic seawater, Cytophaga sp. KUC-1, and purified to homogeneity. About 50% of the enzyme activity remained even after heating at 50 degrees C for 65min and the highest activity was observed in the range of 55-60 degrees C. The enzyme was thermostable and thermophilic, although it was derived from a psychrophile. The circular dichroism at 222nm of the enzyme showed a peak at 32 degrees C. This temperature was closely similar to the transition temperature in the Arrhenius plots. The stereospecificity for the hydride transfer at C4-site of nicotinamide moiety of NADH was pro-R. The gene encoding the enzyme consisted of an open reading frame of 1506-bp encoding a protein of 501 amino acid residues. The significant sequence identity (61%) was found between the Cytophaga and the Pseudomonas aeruginosa enzymes, although their thermostabilities are completely different.
Yamanaka
Yuko
Y
Department of Biotechnology, Faculty of Engineering, Kansai University, Suita, Osaka-fu, Japan.
Kazuoka
Takayuki
T
Yoshida
Masahiro
M
Yamanaka
Kazuya
K
Oikawa
Tadao
T
Soda
Kenji
K
D000445:Aldehyde Oxidoreductases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D001483:Base Sequence; D020134:Catalytic Domain; D002942:Circular Dichroism; D003001:Cloning, Molecular; D003589:Cytophaga / Q000201:enzymology* / Q000235:genetics; D004269:DNA, Bacterial / Q000235:genetics; D004795:Enzyme Stability; D005798:Genes, Bacterial; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D009243:NAD / Q000737:chemistry / Q000378:metabolism; D013237:Stereoisomerism; D013379:Substrate Specificity; D013696:Temperature
D004269:DNA, Bacterial; D009243:NAD; D000445:Aldehyde Oxidoreductases; C018699:aldehyde dehydrogenase (NAD(P)+)