3.4.24.26: pseudolysin
This is an abbreviated version!
For detailed information about pseudolysin, go to the full flat file.
Word Map on EC 3.4.24.26
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3.4.24.26
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thermolysin
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metalloproteinases
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collagenase
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metalloprotease
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3.4.24.4
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elastin
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gelatinase
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elastases
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phosphoramidon
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pseudomonal
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stromelysin
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thermolysin-like
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metalloendopeptidase
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medicine
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thermoproteolyticus
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aureolysin
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vibriolysin
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intrastromal
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industry
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nutrition
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biotechnology
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synthesis
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pharmacology
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diagnostics
- 3.4.24.26
- thermolysin
- metalloproteinases
- collagenase
- metalloprotease
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3.4.24.4
- elastin
- gelatinase
- elastases
- phosphoramidon
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pseudomonal
- stromelysin
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thermolysin-like
- metalloendopeptidase
- medicine
- thermoproteolyticus
- aureolysin
- vibriolysin
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intrastromal
- industry
- nutrition
- biotechnology
- synthesis
- pharmacology
- diagnostics
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
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Engineering
Engineering on EC 3.4.24.26 - pseudolysin
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D189A
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site-directed mutagenesis, the mutant shows decreased thermal stabilities and increased activities compared to the wild-type enzyme
D201A
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site-directed mutagenesis, the mutant shows slightly increased thermal stability and slightly decreased activity compared to the wild-type enzyme
E249A
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site-directed mutagenesis, the mutant shows both decreased thermal stability and decreased activity compared to the wild-type enzyme
N212Q
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site-directed mutagenesis, the mutant enzyme shows similar activity and slightly decreased thermostability compared to the wild-type enzyme
N212Q/N280Q
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site-directed mutagenesis, 90.6% decreased activity compared to the wild-type enzyme
N280Q
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site-directed mutagenesis, the mutant enzyme shows similar activity and slightly decreased thermostability compared to the wild-type enzyme
N43Q
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site-directed mutagenesis, the mutant enzyme shows similar activity and slightly decreased thermostability compared to the wild-type enzyme
N43Q/N212Q
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site-directed mutagenesis, 68.7% decreased activity compared to the wild-type enzyme
N43Q/N212Q/N280Q
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site-directed mutagenesis, 90.6% decreased activity compared to the wild-type enzyme
N43Q/N280Q
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site-directed mutagenesis, 73.6% decreased activity compared to the wild-type enzyme
R179A
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site-directed mutagenesis, the mutant shows decreased thermal stabilities and increased activities compared to the wild-type enzyme
R205A
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site-directed mutagenesis, the mutant shows slightly increased thermal stability and slightly decreased activity compared to the wild-type enzyme
additional information
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mutation of any potential N-glycosylation site was detrimental to its expression in Pichia pastoris with 23.9% decrease in expression of the N43Q mutant, 63.6% of the N212Q mutant, and 63.7% of the N280Q mutant compared with the wild type