Comparison of C-S lyase in Lentinus edodes and Allium sativum.
The characteristics of C-S lyase in Lentinus edodes (shiitake) were compared with those in Allium sativum (garlic). C-S lyase mRNA from shiitake was hybridized with the garlic C-S lyase cDNA fragment, being almost the same length as that from garlic. The isoelectric point of the C-S lyase from shiitake was between pH 4 and 5, while that from garlic was over a wider range between pH 4 and 8. Different from the C-S lyase from garlic, that from shiitake was not a glycoprotein without being stained by PAS, and was not bound to the anti-garlic C-S lyase antibody. Similar to garlic C-S lyase, shiitake C-S lyase comprised a homodimer, and its molecular mass was 84 kDa. However, the N-terminal amino acid sequences of each subunit of shiitake C-S lyase were totally different from those of garlic C-S lyase.
Kumagai
Hitomi
H
Department of Agricultural and Biological Chemistry, College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa-shi 252-8510, Japan. kumagai@brs.nihon-u.ac.jp
Kono
Hidetoshi
H
Sakurai
Hidetoshi
H
Tokimoto
Keisuke
K
D000490:Allium / Q000201:enzymology* / Q000235:genetics; D000595:Amino Acid Sequence; D019281:Dimerization; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008190:Lyases / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D021122:Protein Subunits / Q000737:chemistry; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D020942:Shiitake Mushrooms / Q000201:enzymology* / Q000235:genetics
D021122:Protein Subunits; D012333:RNA, Messenger; D008190:Lyases; C033511:carbon-sulfur lyase