Article
Cloning and sequencing of the gene encoding a novel lysine-specific cysteine proteinase (Lys-gingipain) in Porphyromonas gingivalis: structural relationship with the arginine-specific cysteine proteinase (Arg-gingipain).
Journal of biochemistry - 1 Aug 1996
Okamoto K, Kadowaki T, Nakayama K, Yamamoto K
Abstract excerpt
Lys-gingipain (KGP), so termed due to its peptide cleavage specificity for lysine residues, is a cysteine proteinase produced by the Gram-negative anaerobic bacterium Porphyromonas gingivalis. Mixed oligonucleotide primers designed from the NH2-terminal sequence of the purified enzyme were used t...
Topics
- Adhesins, Bacterial
- Amino Acid Sequence
- Base Sequence
- Cloning, Molecular
- Cysteine Endopeptidases
- DNA Primers
- DNA, Bacterial
- Genes, Bacterial
- Gingipain Cysteine Endopeptidases
- Hemagglutinins
- Molecular Sequence Data
- Molecular Structure
- Mutation
- Polymerase Chain Reaction
