3.4.24.26: pseudolysin

This is an abbreviated version!
For detailed information about pseudolysin, go to the full flat file.

Reaction

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 =

Synonyms

A2 elastase, aeruginolysin, ealastase LasB, EC 3.4.24.4, elastase, elastase B, elastolytic metalloproteinase, EPa, LasB, LasB protease, LepA, More, Neutral metalloproteinase, PAE, PASP, PE, PsE, Pseudomonas aeruginosa elastase, Pseudomonas aeruginosa neutral metalloproteinase, Pseudomonas aeruginosa small protease, Pseudomonas elastase, Pseudomonas protease

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.26 pseudolysin

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Results	in table
6	Activating Compound
26	AA Sequence
24	Application
1	CAS Registry Number
14	Cloned(Commentary)
4	Crystallization (Commentary)
2	Expression
25	General Information
2	General Stability
24	IC50 Value
155	Inhibitors
18	Ki Value [mM]
26	KM Value [mM]
39	Localization
25	Metals/Ions
39	Molecular Weight [Da]
18	Natural Substrates/ Products (Substrates)
31	Organic Solvent Stability
87	Organism
3	PDB ID
18	pH Optimum
2	pH Range
7	pH Stability
3	pI Value
6	Posttranslational Modification
26	Protein Variants
30	Purification (Commentary)
1	Reaction
1	Reaction Type
83	Reference
2	Renatured (Commentary)
4	Source Tissue
9	Specific Activity [micromol/min/mg]
1	Storage Stability
215	Substrates and Products (Substrate)
28	Subunits
95	Synonyms
14	Temperature Optimum [°C]
3	Temperature Range [°C]
15	Temperature Stability [°C]
28	Turnover Number [1/s]

Posttranslational Modification

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Posttranslational Modification on EC 3.4.24.26 - pseudolysin

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

glycoprotein

Pseudomonas aeruginosa

-

the recombinant elastase contains three potential N-glycosylation sites N43, N212, and N280 (Asn-Xaa-Ser/Thr consensus sequences), potential role of N-glycosylation in the activity and stability. Non- and glycosylated isoforms of rPAE display similar kinetic parameters for hydrolyzing casein in aqueous medium, and when catalyzing bipeptide synthesis in 50% v/v DMSO, they exhibit identical substrate specificity and activity, and produce similar yields. The N-linked oligosaccharides of Pichia pastoris-secreted glycoproteins are a high-mannose type (Man8GlcNAc2 or Man9GlcNAc2) with molecular weights close to 2 kDa

733746

proteolytic modification

5 entries

proteolytic modification

Pseudomonas aeruginosa

-

the pro-sequence, consisting of 174 amino acids, is cleaved by autoproteolytic processing in the periplasm to produce the active, mature elastase of 301 amino acids

717673

proteolytic modification

Pseudomonas aeruginosa

-

the enzyme is synthesized in the cytoplasm as a pre-proenzyme consisting of a 2.4-kDa signal peptid, an 18.1-kDa pro-peptide and the 33.1-kDa mature protein. The signal peptide is cleaved from the pre-proenzyme during translocation across the inner membrane, leaving a 51.2-kDa proenzyme (consisting of the pro-peptide and the mature protein). In the periplasm, the proenzymeis folded, guided by the pro-peptide, and a disulfide bond between Cys270 and Cys297 is formed. The pro-peptide is then removed by autoproteolysis, but remains non-covalently attached to mature pseudolysin. A second disulfide bond between Cys30 and Cys58 of the enzyme is then formed. The pro-peptide and mature enzyme are secreted from the cell together, where they dissociate, and the liberated pro-peptide is degraded by the active enzyme

733746

proteolytic modification

Pseudomonas aeruginosa

Q02RJ6

LasB is produced as a precursor protein that requires autocatalytic processing to ensure proper folding as it is exported across the outer membrane. Ca2+ is needed either for efficient transcription of lasB or during the process of folding and export, as calcium plays a role in the structural integrity of LasB

753798

proteolytic modification

Pseudomonas aeruginosa A2

-

the pro-sequence, consisting of 174 amino acids, is cleaved by autoproteolytic processing in the periplasm to produce the active, mature elastase of 301 amino acids

-

proteolytic modification

Pseudomonas aeruginosa UCBPP-PA14

-

LasB is produced as a precursor protein that requires autocatalytic processing to ensure proper folding as it is exported across the outer membrane. Ca2+ is needed either for efficient transcription of lasB or during the process of folding and export, as calcium plays a role in the structural integrity of LasB

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