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- W4255992051 endingPage "480" @default.
- W4255992051 startingPage "472" @default.
- W4255992051 abstract "This chapter discusses the activity, specificity and structural chemistry of collagenasae 1. Matrix metalloproteinase 1 (MMP-1) cleaves collagen types I, II, III, VII, and X. It is calculated that only 22 molecules of collagen are degraded per molecule of collagenase per hour and this turnover rate is one of the slowest observed for an enzyme-catalyzed reaction. Highly cross-linked collagen is slowly attacked by MMP-1; however, the rate increases if other proteinases, such as stromelysin, are present. Gelatin and the core protein of proteoglycan can be cleaved. The activity against gelatin is low compared with that of collagenase 3/MMP-13, which has a broad proteolytic activity. Collagen cleavage is unusual as three peptide bonds must be cleaved and the active-site cleft is too small and rigid to accommodate all three a chains of the collagen molecule at one time, being only 5 Å wide whilst the diameter of triple-helical collagen is about 15 Å. It is estimated that the closest peptide bond of collagen is about 7 Å away from the catalytic zinc atom so changes in conformation of either enzyme, substrate or both is required for catalysis." @default.
- W4255992051 created "2022-05-12" @default.
- W4255992051 creator A5010381724 @default.
- W4255992051 date "2004-01-01" @default.
- W4255992051 modified "2023-09-26" @default.
- W4255992051 title "Collagenase 1" @default.
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- W4255992051 doi "https://doi.org/10.1016/b978-0-12-079611-3.50133-6" @default.
- W4255992051 hasPublicationYear "2004" @default.
- W4255992051 type Work @default.