KEGG   ENZYME: 3.4.24.34Help
Entry
EC 3.4.24.34                Enzyme                                 

Name
neutrophil collagenase;
matrix metalloproteinase 8;
PMNL collagenase;
MMP-8
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
BRITE hierarchy
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
HSA: 
4317(MMP8)
PTR: 
740516(MMP8)
PPS: 
100967517(MMP8)
GGO: 
101130698(MMP8)
PON: 
100459562(MMP8)
MCC: 
703536(MMP8)
MCF: 
102141209(MMP8)
MMU: 
17394(Mmp8)
RNO: 
63849(Mmp8)
CGE: 
HGL: 
101716969(Mmp8)
TUP: 
102491284(MMP8)
CFA: 
489429(MMP8)
AML: 
100480934(MMP8)
FCA: 
101080995(MMP8)
BTA: 
100336575(MMP8)
BOM: 
102264685(MMP8)
PHD: 
102315288(MMP8)
CHX: 
102172738(MMP8)
SSC: 
100523811(MMP8)
CFR: 
102517300(MMP8)
ECB: 
100069005(MMP8)
MYB: 
102243196(MMP8)
MDO: 
SHR: 
100914807(MMP8)
OAA: 
FVE: 
 » show all
Taxonomy
Reference
1  [PMID:3038863]
  Authors
Hasty KA, Jeffrey JJ, Hibbs MS, Welgus HG.
  Title
The collagen substrate specificity of human neutrophil collagenase.
  Journal
J. Biol. Chem. 262 (1987) 10048-52.
  Organism
Homo sapiens [GN:hsa]
Reference
2  [PMID:2164002]
  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 (1990) 11421-4.
  Organism
Homo sapiens [GN:hsa]
  Sequence
[hsa:4317]
Reference
3  [PMID:2159879]
  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
Eur. J. Biochem. 189 (1990) 295-300.
  Organism
Homo sapiens [GN:hsa]
  Sequence
[hsa:4317]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9001-12-1

DBGET integrated database retrieval system