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
-
3.4.24.26
-
thermolysin
-
metalloproteinases
-
collagenase
-
metalloprotease
-
3.4.24.4
-
elastin
-
gelatinase
-
elastases
-
phosphoramidon
-
pseudomonal
-
stromelysin
-
thermolysin-like
-
metalloendopeptidase
-
medicine
-
thermoproteolyticus
-
aureolysin
-
vibriolysin
-
intrastromal
-
industry
-
nutrition
-
biotechnology
-
synthesis
-
pharmacology
-
diagnostics
- 3.4.24.26
- thermolysin
- metalloproteinases
- collagenase
- metalloprotease
-
3.4.24.4
- elastin
- gelatinase
- elastases
- phosphoramidon
-
pseudomonal
- stromelysin
-
thermolysin-like
- metalloendopeptidase
- medicine
- thermoproteolyticus
- aureolysin
- vibriolysin
-
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
Advanced search results
Metals Ions
Metals Ions on EC 3.4.24.26 - pseudolysin
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Ca2+
-
a calcium ion is also required for enzyme activity, and stabilizes its tertiary structure. Contact with the calcium ion is made by the carboxyl groups of Asp136, Glu172, Glu175, and Asp183, the carbonyl group of Leu185, and one water molecule
Zinc
Zn2+
additional information
Zn2+
-
the enzyme has a catalytic zinc ion at the active site cleft with a tetrahedral coordination formed by the two histidines of a HEXXH motif, and a glutamic acid located 18-72 residues C-terminal of the HEXXH motif. The fourth zinc coordinating ligand in the free enzyme is a water molecule
Zn2+
PAE contains zinc, binding site structure, HEXXH is the putative signature of Zn-metalloproteases, overview
Zn2+
-
the enzyme is a metalloprotease that requires a zinc atom, bound to His140, His144, and Glu164, for its activity
Zn2+
zinc metalloproteinase. His140, His144 and Glu164 serve as ligands for zinc ion
additional information
-
Mg2+ and Ca2+ at 0.625 mM have no effect on the activity, Mn2+, Co2+, and Fe3+ at 0.625 mM partly inhibit the enzyme, Zn2+ and Cu2+ inhibit the enzyme completely
additional information
-
metalloprotease, the enzynme contains the typical metalloendopeptidases consensus zinc-binding sequence HEXXH