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3.4.24.34: neutrophil collagenase

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

Word Map on EC 3.4.24.34

Reaction

Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, interstitial collagenase, this enzyme cleaves type III collagen additional information slowly than type I =

Synonyms

collagenase-2, collagenases-8, EC 3.4.24.7, HNC, human neutrophil collagenase, matrix metalloproteinase, Matrix metalloproteinase 8, Matrix metalloproteinase-8, metalloproteinase-8, MetMMP-8, MMP-7, MMP-8, MMP8, neutrophil collagenase, neutrophil collagenase MMP-8, neutrophil interstitial collagenase, PheMMP-8, PMNL collagenase, PMNL-CL, polymorphonuclear leukocyte collagenase, whMMP-8

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.34 neutrophil collagenase

Purification

Purification on EC 3.4.24.34 - neutrophil collagenase

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
as latent enzyme
-
catalytic domain
from culture supernatant of phorbol myristate acetate stimulated neutrophils, immunoaffinity chromatography
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recombinant His-tagged thioredoxin-S-fusion enzyme from Escherichia coli strain BL21 by nicke affinity chromatography, ultrafiltration, tag cleavage by thrombin, followed by gel filtration, recombinant His-/claMP-tagged enzyme is purified by nicel affinity chromatography, tag cleavage by factor Xa, and gel filtration. Reaction with Factor Xa leads to incomplete cleavage but the uncut fusion protein is easily removed by gel filtration
whMMP-8 proenzyme
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