Stromelysin 2 (EC 3.4.24.22, matrix metalloproteinase 10, transin 2, proteoglycanase 2) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
| Stromelysin 2 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.22 | ||||||||
| CAS no. | 140610-48-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- Similar to stromelysin 1, but action on collagen types III, IV and V is weak
This enzyme belongs to the peptidase family M10 (interstitial collagenase family).
References edit
- ^ Breathnach R, Matrisian LM, Gesnel MC, Staub A, Leroy P (February 1987). "Sequences coding for part of oncogene-induced transin are highly conserved in a related rat gene". Nucleic Acids Research. 15 (3): 1139–51. doi:10.1093/nar/15.3.1139. PMC 340513. PMID 3547333.
- ^ Muller D, Quantin B, Gesnel MC, Millon-Collard R, Abecassis J, Breathnach R (July 1988). "The collagenase gene family in humans consists of at least four members". The Biochemical Journal. 253 (1): 187–92. doi:10.1042/bj2530187. PMC 1149273. PMID 2844164.
- ^ Nicholson R, Murphy G, Breathnach R (June 1989). "Human and rat malignant-tumor-associated mRNAs encode stromelysin-like metalloproteinases". Biochemistry. 28 (12): 5195–203. doi:10.1021/bi00438a042. PMID 2548603.
External links edit
- Stromelysin+2 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
