KEGG   ENZYME: 3.4.24.26
Entry
EC 3.4.24.26                Enzyme                                 
Name
pseudolysin;
Pseudomonas elastase;
Pseudomonas aeruginosa neutral metalloproteinase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
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
DYG: DYGSA30_42460
PLAS: NF212_05650
POJ: PtoMrB4_52660(lasB)
PAE: PA3724(lasB)
PAEV: N297_3847(lasB)
PAEI: N296_3847(lasB)
PAU: PA14_16250(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)
SECH: B18_01600
PAP: PSPA7_1397(lasB)
PPAA: B7D75_06465
PTW: TUM18999_56730(lasB)
PSOA: PSm6_16360(lasB)
SVO: SVI_3873
SVM: KDH10_002292
PCAR: PC2016_3203
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
LSH: CAB17_00405
LCJ: NCTC11976_03280(proA)
LWA: SAMEA4504053_0770(lasB_1) SAMEA4504053_1687(lasB_2)
LSS: NCTC12082_00645(lasB_1) NCTC12082_01997(lasB_2) NCTC12082_02649(lasB_3)
LADL: NCTC12735_00425(lasB_1) NCTC12735_01661(lasB_2)
LANT: TUM19329_05080
LLY: J2N86_02395
LCAD: PXX05_01165
TMC: LMI_0809
TIG: THII_1040
CVI: CV_0057(lasB)
CHAE: CH06BL_47250(lasB)
TCAR: U0034_08140
CFU: CFU_1540
CARE: LT85_3217
UCY: RF679_00130
HOH: Hoch_6312
 » show all
Reference
1
  Authors
Morihara K, 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)
DOI:10.1128/IAI.51.3.736-743.1986
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

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Protein sequence (29)   
   UniProt (20)   
   SWISS-PROT (2)   
   PDBSTR (5)   
   PMD (2)   
DNA sequence (254)   
   GenBank (128)   
   EMBL (126)   
3D Structure (4)   
   PDB (4)   
Protein domain (8)   
   InterPro (7)   
   PROSITE(DOC) (1)   
All databases (295)   

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