Catalytic activity:Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus| at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.|cofactor:Binds 2 zinc ions per subunit.|cofactor:Binds 4 calcium ions per subunit.|The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion| thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.|There are two distinct domains in this protein; the catalytic N-terminal| and the C-terminal which is involved in substrate specificity and in binding TIMP (tissue inhibitor of metalloproteinases).|enzyme regulation:Can be activated without removal of the activation peptide.|Cleaves collagens of types I| II| and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection| interacts and cleaves the secreted viral Tat protein| leading to a decrease in neuronal Tat's mediated neurotoxicity.|online information:Collagenase entry|PTM:Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase.|Belongs to the peptidase M10A family.|Contains 4 hemopexin-like domains.|subunit:Interacts with HIV-1 Tat.|
Cerere de ofertă
La cerere
Număr Catalog 772-BT-AP03630-50ulCategorieAfaceri și industrie > Știință și laboratorFurnizorJiaxing Korain Biotech Ltd (BT Labs)GentaurDimensiune50ulTipsingle
