Purification and partial sequences of Aralia cordata cinnamyl alcohol dehydrogenase.
Cinnamyl alcohol dehydrogenase (CAD) (EC 1.1.1.195) from a dicot, Aralia cordata, was purified to homogeneity and its properties were characterized. The enzyme shows a preference for cinnamyl alcohols and cinnamyl aldehydes as substrates. The M(r) is estimated at 72,000. The enzyme is composed of two heterogeneous subunits of slightly different sizes, and it differs from the bean enzyme in the size of subunits. Partial amino acid sequencing of the purified enzyme was carried out both from the N-terminus and using selected peptides obtained by cyanogen bromide cleavage.
Hibino
T
T
Mitsui Plant Biotechnology Research Institute, Ibaraki, Japan.
Shibata
D
D
Umezawa
T
T
Higuchi
T
T
D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D010944:Plants / Q000201:enzymology*; D017421:Sequence Analysis; D013379:Substrate Specificity
D000429:Alcohol Oxidoreductases; C018656:cinnamyl alcohol dehydrogenase