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
-
3.4.24.B16
-
aeruginosa
-
elastase
-
quorum
-
pyocyanin
-
lysostaphin
-
rhamnolipids
-
globisporus
-
pyoverdine
-
sensing-controlled
-
pentaglycine
-
lyticus
-
qs-controlled
-
medicine
-
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
Advanced search results
Reaction
Reaction on EC 3.4.24.B16 - protease lasA
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
proteolytic degradation of proteins
enzyme might be a modified serine protease with a His residue in the active site, specifically involved in degradation of elastin
-
proteolytic degradation of proteins
His120 is critical for LasA activity
-
proteolytic degradation of proteins
specific for Gly-Ala peptide bonds within Gly-Gly-Ala sequences in elastin, substrates that contain no Gly-Gly peptide bond, such as beta-casein, appear to be resistant to the enzyme
-
proteolytic degradation of proteins
substrate carbonyl oxygen displaces Zn2+-bound water molecule 2, thereby enabling direct interaction with Zn2+ to polarize the peptide carbonyl bond, rendering it susceptible to nucleophilic attack by the second Zn2+-bound water molecule, water molecule1. Water molecule 1 is oriented by interactions with the Nepsilon atoms of both His120 and His81, while that with Zn2+ is weakened. Either of these residues is capable of abstracting a proton from water molecule 1, enabling its addition, as hydroxide, to the substrate carbonyl carbon to generate an oxyanion that is stabilized by bidentate co-ordination of Zn2+ and by interaction with the unprotonated His residue. Proton transfer from the histidine general base to the departing amide nitrogen facilitates cleavage of the peptide bond to generate a product complex
proteolytic degradation of proteins
His120 is critical for LasA activity
-
-