Staphylococcal Protease: A Proteolytic Enzyme Specific for Glutamoyl Bonds

作者：Jean Houmard, Gabriel R. Drapeau · 发表于：Proceedings of the National Academy of Sciences · 年份：1972 · DOI：10.1073/pnas.69.12.3506 · 被引用次数：705 · 研究领域：Enzyme Structure and Function、Chemical Synthesis and Analysis、Amino Acid Enzymes and Metabolism

An extracellular protease of Staphylococcus aureus, strain V8, previously shown to cleave specifically the peptide bonds on the carboxyl-terminal side of either aspartate or glutamate residues in phosphate buffer (pH 7.8) hydrolyzes only glutamoyl bonds in either ammonium bicarbonate (pH 7.8) or ammonium acetate (pH 4.0). Of all aspartoyl bonds tested, only the Asp-Gly linkage is cleaved at a detectable rate. The staphylococcal protease hydrolyzes all of the seventeen different glutamoyl bonds studied, although those involving hydrophobic aminoacid residues with bulky side chains are cleaved at a lower rate.