Yamanaka Yuko, Kazuoka Takayuki, Yoshida Masahiro, Yamanaka Kazuya, Oikawa Tadao, Soda Kenji
Department of Biotechnology, Faculty of Engineering, Kansai University, Suita, Osaka-fu, Japan.
Biochem Biophys Res Commun. 2002 Nov 15;298(5):632-7. doi: 10.1016/s0006-291x(02)02523-8.
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.
