The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases
The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases
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DOI：
10.1002/pro.5560040502
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发表时间：
1995-05
期刊：
影响因子：
8
通讯作者：
W. Stöcker;F. Grams;P. Reinemer;W. Bode;U. Baumann;F. Gomis‐Rüth;D. Mckay
中科院分区：
文献类型：
--
作者：
W. Stöcker;F. Grams;P. Reinemer;W. Bode;U. Baumann;F. Gomis‐Rüth;D. Mckay
锌内肽酶人中性粒细胞胶原酶、响尾蛇毒的adamalysin II、铜绿假单胞菌的碱性蛋白酶和小龙虾的astacin的三维结构在拓扑学上相似，都是以典型的顺序排列的五股β折叠和三股α螺旋。这四种蛋白质表现出特征性的一致基序HEXXXHXXGXXH，其三个组氨酸残基参与催化必需的锌离子的结合。此外，它们都在活性位点金属下方共享一个保守的甲硫氨酸残基，作为可重叠的“Met-turn”的一部分。这种结构关系是由拓扑等价的基础上进行的序列比对，显示微弱的，但不同的序列相似性的支持。碱性蛋白酶与人中性粒细胞胶原酶和astacin的距离相等（26%序列同一性），与adamalysin II的距离稍远（17%同一性）。对astacin/adamalysin II，astacin/人嗜中性粒细胞胶原酶，和adamalysin II/人嗜中性粒细胞胶原酶分别表现出16%，14%和13%的序列同一性。因此，相应的四个不同的锌肽酶家族，虾红素，基质金属蛋白酶（基质蛋白，胶原酶），adamalysins/reproplysins（蛇毒蛋白酶/生殖道蛋白），和serralysins（来自沙雷氏菌，欧文氏菌，和假单胞菌属）似乎起源于一个共同祖先的分化进化，并形成一个蛋白水解酶超家族，已经提出了“Metzincins”。metzincins与嗜热菌蛋白酶样酶之间也存在微弱但重要的结构关系，它们共享截短的锌结合基序HEXXH，此外，在其N末端结构域中具有相似的拓扑结构。
The three‐dimensional structures of the zinc endopeptidases human neutrophil collagenase, adamalysin II from rattle snake venom, alkaline proteinase from Pseudomonas aeruginosa, and astacin from crayfish are topologically similar, with respect to a five‐stranded β‐sheet and three α‐helices arranged in typical sequential order. The four proteins exhibit the characteristic consensus motif HEXXHXXGXXH, whose three histidine residues are involved in binding of the catalytically essential zinc ion. Moreover, they all share a conserved methionine residue beneath the active site metal as part of a superimposable “Met‐turn.” This structural relationship is supported by a sequence alignment performed on the basis of topological equivalence showing faint but distinct sequential similarity. The alkaline proteinase is about equally distant (26% sequence identity) to both human neutrophil collagenase and astacin and a little further away from adamalysin II (17% identity). The pairs astacin/adamalysin II, astacin/human neutrophil collagenase, and adamalysin II/human neutrophil collagenase exhibit sequence identities of 16%, 14%, and 13%, respectively. Therefore, the corresponding four distinct families of zinc peptidases, the astacins, the matrix metalloproteinases (matrixins, collagenases), the adamalysins/reprolysins (snake venom proteinases/reproductive tract proteins), and the serralysins (large bacterial proteases from Serratia, Erwinia, and Pseudomonas) appear to have originated by divergent evolution from a common ancestor and form a superfamily of proteolytic enzymes for which the designation “metzincins” has been proposed. There is also a faint but significant structural relationship of the metzincins to the thermolysin‐like enzymes, which share the truncated zinc‐binding motif HEXXH and, moreover, similar topologies in their N‐terminal domains.