|Gene:||lasB||Accession Number: G-11140 (MetaCyc)|
Species: Pseudomonas aeruginosa
The enzyme has been first isolated and characterized in 1965 [Morihara65]. The purified enzyme, whose molecular weight was calculated to be 39.5 kDa, was shown to act on a variety of protein substrates, including casein, hemoglobin, egg albumin and fibrin. Later it was shown that the enzyme degrades additional proteins, including elastin [Heck86], collagen [Heck86a], human IgG [Holder84], serum I proteinase inhibitor [Morihara84], and components of the complement system [Schultz74].
The lasB gene that encodes the enzyme has been cloned and characterized [Schad87, Bever88, Fukushima89] and found to direct the synthesis of 54- and 50-kilodalton (kDa) proteins. The deduced amino acid sequence showed that the gene contains a signal sequence followed by a large propeptide, which are both cleaved to generate the mature 33-kDa elastase protein [Bever88, Kessler92a]. Bacteria carrying the gene on multicopy plasmids exhibited high levels of both elastase activity and elastase antigens [Fukushima89].
Gene Citations: [Rust96]
Molecular Weight of Polypeptide: 53.687 kD (from nucleotide sequence), 33.0 kD (experimental) [Bever88 ]
pI: 5.9 [Morihara65]
Relationship Links: Entrez-Nucleotide:PART-OF:M19472 , InterPro:IN-FAMILY:IPR001570 , InterPro:IN-FAMILY:IPR011096 , InterPro:IN-FAMILY:IPR013856 , InterPro:IN-FAMILY:IPR023612 , InterPro:IN-FAMILY:IPR025711 , PDB:Structure:1EZM , PDB:Structure:1U4G , PDB:Structure:3DBK , Pfam:IN-FAMILY:PF01447 , Pfam:IN-FAMILY:PF02868 , Pfam:IN-FAMILY:PF03413 , Pfam:IN-FAMILY:PF07504 , Prints:IN-FAMILY:PR00730 , Prosite:IN-FAMILY:PS00142
EC Number: 188.8.131.52
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
The reaction is physiologically favored in the direction shown.
pH(opt): 8 [Morihara65]
Fukushima89: Fukushima J, Yamamoto S, Morihara K, Atsumi Y, Takeuchi H, Kawamoto S, Okuda K (1989). "Structural gene and complete amino acid sequence of Pseudomonas aeruginosa IFO 3455 elastase." J Bacteriol 171(3);1698-704. PMID: 2493453
Heck86: Heck LW, Morihara K, Abrahamson DR (1986). "Degradation of soluble laminin and depletion of tissue-associated basement membrane laminin by Pseudomonas aeruginosa elastase and alkaline protease." Infect Immun 54(1);149-53. PMID: 3093382
Holder84: Holder IA, Wheeler R (1984). "Experimental studies of the pathogenesis of infections owing to Pseudomonas aeruginosa: elastase, an IgG protease." Can J Microbiol 30(9);1118-24. PMID: 6439405
Kessler92a: Kessler E, Safrin M, Peretz M, Burstein Y (1992). "Identification of cleavage sites involved in proteolytic processing of Pseudomonas aeruginosa preproelastase." FEBS Lett 299(3);291-3. PMID: 1544509
Morihara65: Morihara, K, Tsuzuki, H, Oka, T, Inoue, H, Ebata, M (1965). "Pseudomonas aeruginosa elastase. isolation, crystallization, and preliminary characterization." J Biol Chem 240;3295-304. PMID: 14321366
Morihara84: Morihara K, Tsuzuki H, Harada M, Iwata T (1984). "Purification of human plasma alpha 1-proteinase inhibitor and its inactivation by Pseudomonas aeruginosa elastase." J Biochem 95(3);795-804. PMID: 6427201
Schultz74: Schultz DR, Miller KD (1974). "Elastase of Pseudomonas aeruginosa: inactivation of complement components and complement-derived chemotactic and phagocytic factors." Infect Immun 10(1);128-35. PMID: 4210424
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493