KEGG   ENZYME: 3.4.24.26Help
Entry
EC 3.4.24.26                Enzyme                                 

Name
pseudolysin;
Pseudomonas elastase;
Pseudomonas aeruginosa neutral metalloproteinase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
BRITE hierarchy
Reaction(IUBMB)
Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1'. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects
Comment
In peptidase family M4 (thermolysin family). From the pathogenic bacteria Pseudomonas aeruginosa and Legionella pneumophila, and causes tissue damage.
History
EC 3.4.24.26 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.26
Orthology
K01399  pseudolysin
Genes
RHD: R2APBS1_0936
PAE: PA3724(lasB)
PAEV: N297_3847(lasB)
PAEI: N296_3847(lasB)
PAU: PA14_16250(lasB)
PAP: PSPA7_1397(lasB)
PAG: PLES_12581(lasB)
PAF: PAM18_1222(lasB)
PNC: NCGM2_4855(lasB)
PAEB: NCGM1900_2552(lasB)
PDK: PADK2_05720
PSG: G655_06175
PRP: M062_19690
PAEP: PA1S_06475
PAER: PA1R_gp1580
PAEM: U769_06260
PAEL: T223_06195
PAES: SCV20265_1285
PAEU: BN889_04117(lasB_1)
PAEG: AI22_27120
PAEC: M802_3844(lasB)
PAEO: M801_3712(lasB)
SVO: SVI_3873
LPN: lpg0467 lpg1655(lasB) lpg2977
LPH: LPV_0568(proA) LPV_1911(lasB)
LPO: LPO_0533(proA) LPO_1690(lasB) LPO_3312(lasB)
LPU: LPE509_00028 LPE509_01540 LPE509_02756
LPM: LP6_0458(proA1) LP6_1633(lasB1) LP6_3016(lasB)
LPF: lpl0508(proA) lpl1620 lpl2906
LPP: lpp0532(proA) lpp1626 lpp3049
LPC: LPC_1085(lasB) LPC_2877(proA) LPC_3292(lasB)
LPA: lpa_00713(lasB) lpa_02392(lasB) lpa_04362(lasB) lpa_04363(lasB)
LPE: lp12_0470 lp12_1593 lp12_2969
LLO: LLO_2670 LLO_2721(proA)
LFA: LFA_2656
LHA: LHA_0574 LHA_1395
TMC: LMI_0809
TIG: THII_1040
CVI: CV_0057(lasB)
CFU: CFU_1540
CARE: LT85_3217
HOH: Hoch_6312
 » show all
Taxonomy
Reference
1
  Authors
Morihara, K. and Tsuzuki, H.
  Title
Pseudomonas aeruginosa elastase: affinity chromatography and some properties as a metallo-neutral proteinase.
  Journal
Agric Biol Chem 39:1123-1128 (1975)
Reference
2  [PMID:6767718]
  Authors
Nishino N, Powers JC.
  Title
Pseudomonas aeruginosa elastase. Development of a new substrate, inhibitors, and an affinity ligand.
  Journal
J Biol Chem 255:3482-6 (1980)
Reference
3  [PMID:3512431]
  Authors
Dreyfus LA, Iglewski BH.
  Title
Purification and characterization of an extracellular protease of Legionella pneumophila.
  Journal
Infect Immun 51:736-43 (1986)
Reference
4  [PMID:2842313]
  Authors
Bever RA, Iglewski BH.
  Title
Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene.
  Journal
J Bacteriol 170:4309-14 (1988)
DOI:10.1128/JB.170.9.4309-4314.1988
  Sequence
[pae:PA3724]
Reference
5  [PMID:2110146]
  Authors
Black WJ, Quinn FD, Tompkins LS.
  Title
Legionella pneumophila zinc metalloprotease is structurally and functionally homologous to Pseudomonas aeruginosa elastase.
  Journal
J Bacteriol 172:2608-13 (1990)
DOI:10.1128/JB.172.5.2608-2613.1990
  Sequence
[lpn:lpg0467]
Other DBs
ExplorEnz - The Enzyme Database: 3.4.24.26
IUBMB Enzyme Nomenclature: 3.4.24.26
ExPASy - ENZYME nomenclature database: 3.4.24.26
BRENDA, the Enzyme Database: 3.4.24.26
CAS: 171715-23-4

  All links  
Gene (65)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (64)   
Protein sequence (67)   
   UniProt (58)   
   SWISS-PROT (2)   
   RefSeq(pep) (2)   
   PDBSTR (3)   
   PMD (2)   
DNA sequence (143)   
   RefSeq(nuc) (2)   
   GenBank (71)   
   EMBL (70)   
3D Structure (3)   
   PDB (3)   
Protein domain (1)   
   PROSITE(DOC) (1)   
All databases (279)   

Download RDF
DBGET integrated database retrieval system