Stöcker W, Bode W
Zoologisches Institut der Universität Heidelberg, Germany.
Curr Opin Struct Biol. 1995 Jun;5(3):383-90. doi: 10.1016/0959-440x(95)80101-4.
A large number of zinc endopeptidases contain an HEXXHXXGXXH consensus motif in their catalytic site (single letter code; X is any amino acid residue). These enzymes can be grouped into four distinct families, the astacins, the adamalysins, the serralysins and the matrix metalloproteinases (matrixins). Despite a low degree of sequence similarity, their catalytic modules are topologically similar. A topology derived sequence alignment suggests that the four families form a superfamily, called the metzincins because of a perfectly superimposable methionine residue close to the zinc-binding active site. Topological similarity to the thermolysin-like enzymes indicates that these enzymes may have had a common ancestor.
大量的锌内肽酶在其催化位点含有HEXXHXXGXXH共有基序（单字母代码；X为任意氨基酸残基）。这些酶可分为四个不同的家族，即虾红素蛋白酶家族、解整合素和金属蛋白酶家族、锯齿状蛋白酶家族以及基质金属蛋白酶家族（基质溶素）。尽管序列相似性程度较低，但它们的催化模块在拓扑结构上相似。基于拓扑结构的序列比对表明，这四个家族形成了一个超家族，由于靠近锌结合活性位点有一个完全可叠加的甲硫氨酸残基，故称为金属锌蛋白酶超家族。与嗜热菌蛋白酶样酶的拓扑相似性表明，这些酶可能有一个共同的祖先。
