Understanding the P1‘ Specificity of the Matrix Metalloproteinases: Effect of S1‘ Pocket Mutations in Matrilysin and Stromelysin-1

Matrilysin (MAT) prefers leucine over residues that have aromatic side chains at the P1‘ position of peptide and protein substrates, while stromelysin (HFS) has a broader specificity. The X-ray structures of these enzymes show that their respective S1‘ subsites differ primarily due to the amino acid...

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Veröffentlicht in:	Biochemistry (Easton) 1996-08, Vol.35 (31), p.10103-10109
Hauptverfasser:	Welch, Anthony R, Holman, Christopher M, Huber, Martin, Brenner, Mitchell C, Browner, Michelle F, Van Wart, Harold E
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Base Sequence Binding Sites Cloning, Molecular Escherichia coli Humans Kinetics Matrix Metalloproteinase 3 Matrix Metalloproteinase 7 Metalloendopeptidases - chemistry Metalloendopeptidases - isolation & purification Metalloendopeptidases - metabolism Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Oligodeoxyribonucleotides Point Mutation Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Sequence Homology, Amino Acid Substrate Specificity
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