Article
Mutation of the active site glutamic acid of human gelatinase A: effects on latency, catalysis, and the binding of tissue inhibitor of metalloproteinases-1.
Biochemistry - 31 May 1994
Crabbe T, Zucker S, Cockett M I, Willenbrock F, Tickle S, O'Connell J P, Scothern J M, Murphy G, Docherty A J
Abstract excerpt
Human gelatinase A, a member of the matrix metalloproteinase family, is secreted from cells as the M(r) 72,000 latent precursor, progelatinase A. The autolytic removal of an N-terminal propeptide generates the M(r) 66,000 active form. Mutants of recombinant progelatinase A, altered such that the proposed active site glutamic acid residue (E375) was replaced by either an aspartic acid (proE375-->D), an alanine...
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