Sequence specificity of human skin fibroblast collagenase. Evidence for the role of collagen structure in determining the collagenase cleavage site.
作者： G.B. Fields , H.E. Van Wart , H. Birkedal-Hansen
DOI: 10.1016/S0021-9258(18)45559-7
关键词:
摘要: Abstract The sequence specificity of human skin fibroblast collagenase has been investigated by measuring the rate hydrolysis 16 synthetic octapeptides covering P4 through P4' subsites substrate. choice peptides was patterned after potential cleavage sites (those containing either Gly-Leu-Ala or Gly-Ile-Ala sequences) found in types I, II, and III collagens. initial P1-P1' bond each peptide measured quantitating concentration amino groups produced upon reaction with fluorescamine. reactions have carried out under first-order conditions ([S] much less than KM) kcat/KM values calculated from rates. acids P3 (Pro, Ala, Leu, Asn), P2 (Gln, Hyp, Arg, Asp, Val), P1' (Ile Leu), Thr, His, Pro) all influence However, differences relative rates observed for these cannot themselves explain why hydrolyzes only Gly-Leu Gly-Ile bonds at site native This supports notion that local structure collagen is important determining location mammalian site.
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