| Literature DB >> 10586514 |
Y Takatsuka1, T Tomita, Y Kamio.
Abstract
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).Entities:
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Year: 1999 PMID: 10586514 DOI: 10.1271/bbb.63.1843
Source DB: PubMed Journal: Biosci Biotechnol Biochem ISSN: 0916-8451 Impact factor: 2.043