BACTERIOPHAGE-T4 PREHEAD PROTEINASE .1. PURIFICATION AND PROPERTIES OF A BACTERIOPHAGE ENZYME WHICH CLEAVES CAPSID PRECURSOR PROTEINS
BACTERIOPHAGE-T4 PREHEAD PROTEINASE .1. PURIFICATION AND PROPERTIES OF A BACTERIOPHAGE ENZYME WHICH CLEAVES CAPSID PRECURSOR PROTEINS
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DOI：
10.1016/s0022-2836(76)80016-2
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发表时间：
1976-01-01
影响因子：
5.6
通讯作者：
ONORATO, L
中科院分区：
文献类型：
--
作者：
SHOWE, MK;ISOBE, E;ONORATO, L
从T4噬菌体感染的细胞中纯化一种酶，该酶将纯化的前头蛋白切割至成熟病毒体中发现的大小。其特异性对应于体内发现的特异性，因为其作用导致在切割的[内部蛋白] IPIII上产生新的丙氨酸氨基末端。这被称为酶T4前头蛋白酶（T4PPase），因为它作用于T4衣壳的前体蛋白。在体外，前体蛋白不需要组装成一个结构，成为酶的底物。T4PPase的活性既不需要活性丝氨酸，也不需要巯基。通过自身消化迅速灭活。
An enzyme from T4 phage-infected cells which cleaves purified prehead proteins to the size found in mature virions was purified. Its specificity corresponds to that found in vivo since its action results in the creation of a new alanine amino-terminal on cleaved [internal protein] IPIII. This is called enzyme T4 prehead proteinase (T4PPase), because it acts on the proteins of the precursor to the T4 capsid. In vitro, the precursor proteins need not be assembled into a structure to be substrates for the enzyme. T4PPase requires neither an active serine nor a sulfhydryl group for activity. It is rapidly inactivated by autodigestion.