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MetaCyc Enzyme: elastase

Gene: lasB Accession Number: G-11140 (MetaCyc)

Synonyms: PA3724

Species: Pseudomonas aeruginosa

Summary:
The elastase protein of Pseudomonas aeruginosa is one of more than a dozen virulence factors produced by the pathogen upon infection of a host.

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].

The enzyme, which contains three Zn2+ ligands and a single Ca2+ ion, has been purified and crystallized, and the crystal structure has been solved to 1.5-Å resolution [Thayer91].

Gene Citations: [Rust96]

Molecular Weight of Polypeptide: 53.687 kD (from nucleotide sequence), 33.0 kD (experimental) [Bever88 ]

pI: 5.9 [Morihara65]

Unification Links: Protein Model Portal:P14756 , SMR:P14756 , String:208964.PA3724 , UniProt:P14756

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

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Credits:
Created 12-Mar-2009 by Caspi R , SRI International


Enzymatic reaction of: pseudolysin (elastase)

EC Number: 3.4.24.26

a protein + H2O <=> 2 a peptide

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.

Cofactors or Prosthetic Groups: Zn2+ [Thayer91], Ca2+ [Thayer91]

pH(opt): 8 [Morihara65]


References

Bever88: Bever RA, Iglewski BH (1988). "Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene." J Bacteriol 170(9);4309-14. PMID: 2842313

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

Heck86a: Heck LW, Morihara K, McRae WB, Miller EJ (1986). "Specific cleavage of human type III and IV collagens by Pseudomonas aeruginosa elastase." Infect Immun 51(1);115-8. PMID: 3079727

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

Rust96: Rust L, Pesci EC, Iglewski BH (1996). "Analysis of the Pseudomonas aeruginosa elastase (lasB) regulatory region." J Bacteriol 178(4);1134-40. PMID: 8576049

Schad87: Schad PA, Bever RA, Nicas TI, Leduc F, Hanne LF, Iglewski BH (1987). "Cloning and characterization of elastase genes from Pseudomonas aeruginosa." J Bacteriol 169(6);2691-6. PMID: 3034864

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

Thayer91: Thayer MM, Flaherty KM, McKay DB (1991). "Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution." J Biol Chem 266(5);2864-71. PMID: 1899664


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Mon Aug 3, 2015, biocyc11.