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3.4.24.40: serralysin

This is an abbreviated version!
For detailed information about serralysin, go to the full flat file.

Word Map on EC 3.4.24.40

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

Purification

Purification on EC 3.4.24.40 - serralysin

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 immunologically not related enzymes: MW 56000 and MW 60000
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ammonium sulfate precipitation, anion exchange column chromatography, and gel filtration
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ammonium sulfate precipitation, DEAE-cellulose column chromatography, and Sephadex G-75 gel filtration
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ammonium sulfate precipitation, gel filtration, chromatography
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dialysis against 10 mM N-methyldiethanolamine, DE-52 gel filtration, chelating Sepharose 6B gel filtration, dialysis against 0.02M triethanolamine-HCl buffer
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gel filtration
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metal chelate chromatography with copper and hydrophobic interaction chromatography, dialysis
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native enzyme by two different steps of anion exchange chromatography
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precipitation with ammonium sulfate and acetone, gel filtration and chromatography
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purification from culture fluid by Resource Q column chromatography
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purified to homogeneity by precipitation with ammonium sulfate (65%). After dialysis, the crude enzyme is further purified by FPLC using Superdex 200 column
recombinant refolded His-tagged wild-type and mutant AP proteins and domains from inclusion bodies by nickel affinity chromatography
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to near homogeneity
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