Entry |
|
Name |
neutrophil collagenase;
matrix metalloproteinase 8;
PMNL collagenase;
MMP-8
|
Class |
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
|
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
|
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
|
History |
EC 3.4.24.34 created 1992
|
Orthology |
K01402 | matrix metalloproteinase-8 (neutrophil collagenase) |
|
Genes |
» show all
|
Reference |
|
Authors |
Hasty KA, Jeffrey JJ, Hibbs MS, Welgus HG. |
Title |
The collagen substrate specificity of human neutrophil collagenase. |
Journal |
J Biol Chem 262:10048-52 (1987) |
Reference |
|
Authors |
Hasty KA, Pourmotabbed TF, Goldberg GI, Thompson JP, Spinella DG, Stevens RM, Mainardi CL |
Title |
Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases. |
Journal |
J Biol Chem 265:11421-4 (1990) |
Sequence |
|
Reference |
|
Authors |
Knauper V, Kramer S, Reinke H, Tschesche H. |
Title |
Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms. |
Journal |
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Sequence |
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Other DBs |
ExPASy - ENZYME nomenclature database: | 3.4.24.34 |
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