Abstract：
: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.
journal_name
Phytochemistryjournal_title
Phytochemistryauthors
Hibino T,Shibata D,Umezawa T,Higuchi Tdoi
10.1016/s0031-9422(00)95137-9subject
Has Abstractpub_date
1993-02-01 00:00:00pages
565-7issue
3eissn
0031-9422issn
1873-3700pii
S0031-9422(00)95137-9journal_volume
32pub_type
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