| Entry |
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| Name |
neutrophil collagenase;
matrix metalloproteinase 8;
PMNL collagenase;
MMP-8
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| Class |
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
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| Reaction(IUBMB) |
Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, interstitial collagenase, this enzyme cleaves type III collagen more slowly than type I
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| Comment |
Similar to interstitial collagenase in specificity, but the product of a different gene and highly glycosylated. Stored in the specific granules of neutrophil leukocytes. In peptidase family M10 (interstitial collagenase family). Formerly included in EC 3.4.24.7
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| History |
EC 3.4.24.34 created 1992
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| Orthology |
| K01402 | matrix metalloproteinase-8 (neutrophil collagenase) |
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| Genes |
» show all
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| Reference |
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| Authors |
Hasty KA, Jeffrey JJ, Hibbs MS, Welgus HG. |
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| Title |
The collagen substrate specificity of human neutrophil collagenase. |
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| Journal |
J Biol Chem 262:10048-52 (1987) |
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| Reference |
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| Authors |
Hasty KA, Pourmotabbed TF, Goldberg GI, Thompson JP, Spinella DG, Stevens RM, Mainardi CL |
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| Title |
Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases. |
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| Journal |
J Biol Chem 265:11421-4 (1990) |
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| Sequence |
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| Reference |
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| Authors |
Knauper V, Kramer S, Reinke H, Tschesche H. |
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| Title |
Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms. |
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| Journal |
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| Sequence |
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| Other DBs |
| ExPASy - ENZYME nomenclature database: | 3.4.24.34 |
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