3.4.24.40: serralysin

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For detailed information about serralysin, go to the full flat file.

Reaction

Preferential cleavage of bonds with hydrophobic residues in P1' =

Synonyms

aeruginolysin, Alkaline protease, AMP-P, AP, APR, AprA, AprX, arazyme, calcium-regulated alkaline protease, DR2310 protease, Escherichia freundii proteinase, Extracellular metalloproteinase, LupA, More, protease B, protease C, protease I, Proteinase, Serratia marcescens metallo-, PrtA, PrtA metalloprotease, PrtC, pseudomonal serralysin, Pseudomonas aeruginosa alk. protease, Pseudomonas aeruginosa alkaline protease, Pseudomonas aeruginosa alkaline proteinase, Pseudomonas alkaline protease, psychrophilic alkaline metalloprotease, serralysin, serralysin-like metalloprotease, Serratia marcescens extracellular proteinase, Serratia marcescens metalloprotease, Serratia marcescens metalloproteinase, SlpB, SMP, thermoalkaline protease, thermostable alkaline protease, zinc proteinase

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.40 serralysin

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Results	in table
1	Activating Compound
1130	AA Sequence
4	Application
1	CAS Registry Number
16	Cloned(Commentary)
9	Crystallization (Commentary)
2	Expression
8	General Information
2	General Stability
176	Inhibitors
36	kcat/KM [mM/s]
12	Ki Value [mM]
77	KM Value [mM]
37	Localization
89	Metals/Ions
49	Molecular Weight [Da]
11	Natural Substrates/ Products (Substrates)
74	Organism
13	PDB ID
34	pH Optimum
9	pH Range
12	pH Stability
3	pI Value
1	Posttranslational Modification
13	Protein Variants
29	Purification (Commentary)
1	Reaction
1	Reaction Type
72	Reference
1	Renatured (Commentary)
12	Source Tissue
10	Specific Activity [micromol/min/mg]
4	Storage Stability
261	Substrates and Products (Substrate)
19	Subunits
64	Synonyms
15	Temperature Optimum [°C]
3	Temperature Range [°C]
25	Temperature Stability [°C]
48	Turnover Number [1/s]

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RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

recombinant His-tagged wild-type and mutant AP proteins and domains under denaturing conditions are refolded from inclusion bodies using either urea for RTX, or guanidine HCl for full-length and truncation mutants

Pseudomonas aeruginosa

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717874