By William C. Parks, Robert P. Mecham
The chapters during this booklet completely conceal the constitution, rules, and serve as of matrix metalloproteinases, and supply details at the most recent recommendations to inhibit enzyme task. This paintings might be an crucial reference software for investigators with an curiosity in extracellular matrix biology, matrix turnover, enzymology and biochemistry of proteinases, developmental biology, pathology, and healing interventions. Key beneficial properties* presents state of the art info on a box with extensive implications to many parts of biology* contains specific assurance of the constitution and rules of all significant matrix metalloproteinases* Chapters concentrate on a well timed and increasing box* subject matters have direct relevance to knowing human ailment pathology of melanoma, arthritis, and vascular affliction* Discusses most recent ideas utilized in the advance of latest therapeutics to inhibit metalloproteinase task
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Additional resources for Matrix Metalloproteinases (Biology of Extracellular Matrix)
In the case of the rat homologue, the catalytic efficiency against type II collagen is approximately equal to that exhibited against types I and III. In the case of human MMP-13, the catalytic efficiency of the enzyme against type II collagen is some 10-fold higher than the efficiency of the enzyme on types I and II. , 1997). The biological significance of this unanticipated extra cleavage in cartilage collagen is unknown. In addition, it has been found that human MMP13 degrades denatured collagen extremely efficiently, as had previously been shown for rat collagenase.
J. (1986). The biological regulation of collagenase activity. P. ), pp. ] 24 JOHN J. JEFFREY When the data describing the energetics of MMP-1 activity are taken together with the considerations presented by the structural analyses of MMP-1, it is tempting to paint a picture of a combination of scissile bonds in a hydrophobic environment, requiring energy to transport the water of hydrolysis to the correct site. Together with major induced-fit changes in the enzyme molecule to fully enable an active site that appears to have difficulty accessing its substrate the result is a low rate ofproteolysis.
Collagen and collagenase--Pregnancy and parturition. Semin. Perinatol. 15, 118-126. , et al. (1983). Studies on the activation energy and deuterium effect of human skin collagenase on homologous collagen substrates. J. Biol. Chem. 258, 11123-11127. Jenne, D. (1991). Homology of placental protein 11 and pea seed albumin 2 with vitronectin. Biochem. Biophys. Res. Commun. 176, 1000-1006. K. (1987). Nucleotide sequence and organization of the human S-protein gene: Repeating peptide motifs in the pexin family and a model for their evolution.
Matrix Metalloproteinases (Biology of Extracellular Matrix) by William C. Parks, Robert P. Mecham