Identification of the amino acid residues conferring substrate specificity upon Selenomonas ruminantium lysine decarboxylase.
Lysine decarboxylase (LDC, EC 4.1.1.18) from Selenomonas ruminantium has decarboxylating activities towards both L-lysine and L-ornithine with similar K(m) and Vmax. Here, we identified four amino acid residues that confer substrate specificity upon S. ruminantium LDC and that are located in its catalytic domain. We have succeeded in converting S. ruminantium LDC to an enzyme with a preference in decarboxylating activity for L-ornithine when the four-residue of LDC were replaced by the corresponding residues of mouse ornithine decarboxylase (EC 4.1.1.17).
Takatsuka
Y
Y
Department of Molecular and Cell Biology, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan.
Tomita
T
T
Kamio
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D002262:Carboxy-Lyases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D051379:Mice; D008969:Molecular Sequence Data; D016296:Mutagenesis; D009955:Ornithine Decarboxylase / Q000737:chemistry / Q000235:genetics; D020357:Selenomonas / Q000201:enzymology* / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D002262:Carboxy-Lyases; D009955:Ornithine Decarboxylase; C021520:lysine decarboxylase