STAPHYLOCOCCAL PROTEASE - A PROTEOLYTIC-ENZYME SPECIFIC FOR GLUTAMOYL BONDS
STAPHYLOCOCCAL PROTEASE - A PROTEOLYTIC-ENZYME SPECIFIC FOR GLUTAMOYL BONDS
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DOI：
10.1073/pnas.69.12.3506
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发表时间：
1972-01-01
影响因子：
11.1
通讯作者：
DRAPEAU, GR
中科院分区：
文献类型：
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作者：
HOUMARD, J;DRAPEAU, GR
金黄色葡萄球菌 V8 菌株的胞外蛋白酶先前显示可特异性裂解磷酸盐缓冲液 (pH 7.8) 中天冬氨酸或谷氨酸残基羧基末端侧的肽键，但仅水解碳酸氢铵 (pH 7.8) 或醋酸铵 (pH 4.0) 中的谷氨酰键。在所有测试的天冬酰键中，只有天冬氨酸-甘氨酸键以可检测的速率被裂解。葡萄球菌蛋白酶可水解所研究的所有 17 个不同的谷氨酰键，但涉及具有庞大侧链的疏水性氨基酸残基的酶的裂解速率较低。
An extracellular protease ofStaphylococcus 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.