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...
Topics
- Amino Acid Sequence
- Base Sequence
- Binding Sites
- Catalysis
- DNA Primers
- Electrophoresis, Polyacrylamide Gel
- Enzyme Activation
- Enzyme Precursors
- Gelatinases
- Glutamates
- Glutamic Acid
- Glycoproteins
- Humans
- Matrix Metalloproteinase 2