Title : Inhibitors and specificity of Pseudomonas aeruginosa LasA.

Pub. Date : 1997 Apr 11

PMID : 9092525






5 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 N-terminal amino acid sequencing of two fragments derived from soluble elastin indicated that both resulted from cleavages of Gly-Ala peptide bonds located within similar sequences, Pro-Gly-Val-Gly-Gly-Ala-Xaa (where Xaa is Phe or Gly). Glycine elastin Homo sapiens
2 N-terminal amino acid sequencing of two fragments derived from soluble elastin indicated that both resulted from cleavages of Gly-Ala peptide bonds located within similar sequences, Pro-Gly-Val-Gly-Gly-Ala-Xaa (where Xaa is Phe or Gly). Glycine elastin Homo sapiens
3 The present results suggest that LasA is a zinc metalloendopeptidase selective for Gly-Ala peptide bonds within Gly-Gly-Ala sequences in elastin. Glycine elastin Homo sapiens
4 The present results suggest that LasA is a zinc metalloendopeptidase selective for Gly-Ala peptide bonds within Gly-Gly-Ala sequences in elastin. Glycine elastin Homo sapiens
5 The present results suggest that LasA is a zinc metalloendopeptidase selective for Gly-Ala peptide bonds within Gly-Gly-Ala sequences in elastin. Glycine elastin Homo sapiens