3.4.24.B16: protease lasA
This is an abbreviated version!
For detailed information about protease lasA, go to the full flat file.
Word Map on EC 3.4.24.B16
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3.4.24.B16
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aeruginosa
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elastase
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quorum
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pyocyanin
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lysostaphin
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rhamnolipids
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globisporus
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pyoverdine
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sensing-controlled
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pentaglycine
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lyticus
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qs-controlled
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medicine
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degradation
- 3.4.24.B16
- aeruginosa
- elastase
-
quorum
- pyocyanin
- lysostaphin
- rhamnolipids
- globisporus
-
pyoverdine
-
sensing-controlled
- pentaglycine
- lyticus
-
qs-controlled
- medicine
- degradation
Reaction
proteolytic degradation of proteins =
Synonyms
bacteriolytic enzyme, LasA, LasA endopeptidase, LasA protease, M23.002, Pseudomonas elastase, staphylolysin, staphylolytic enzyme
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 3.4.24.B16 - protease lasA
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proteolytic modification
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enzyme precursor contains an elastase cleavage motif at the N-terminus, the enzyme is probably activated by elastase to activate the elastase afterwards
proteolytic modification
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no autoproteolysis, enzyme is synthesized as a pre-proLasA, the signal sequence of pre-proLasA is cleaved off by a signal peptidase, the remaining inactive 42 kDa proLasA is secreted to the extracellular space, where the proform is cleaved to the mature active enzyme via a 28 kDa intermediate, plus a 14 kDa fragment, by elastase and a lysine specific protease, not by alkaline proteinase
proteolytic modification
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no autoproteolysis, the 31 amino acid residues signal sequence of pre-proLasA is cleaved off by a signal peptidase, processing of the remaining 42 kDa proLasA by incubation with the culture filtrate of Pseudomonas aeruginosa or trypsin to the active 20 kDa LasA
proteolytic modification
cleavage of proLasA precursor at position 237 of full-length gene product
proteolytic modification
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no autoproteolysis, the 31 amino acid residues signal sequence of pre-proLasA is cleaved off by a signal peptidase, processing of the remaining 42 kDa proLasA by incubation with the culture filtrate of Pseudomonas aeruginosa or trypsin to the active 20 kDa LasA
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proteolytic modification
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no autoproteolysis, enzyme is synthesized as a pre-proLasA, the signal sequence of pre-proLasA is cleaved off by a signal peptidase, the remaining inactive 42 kDa proLasA is secreted to the extracellular space, where the proform is cleaved to the mature active enzyme via a 28 kDa intermediate, plus a 14 kDa fragment, by elastase and a lysine specific protease, not by alkaline proteinase
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