SEQUENCE AND STRUCTURE COMPARISON SUGGEST THAT METHIONINE AMINOPEPTIDASE, PROLIDASE, AMINOPEPTIDASE-P, AND CREATINASE SHARE A COMMON FOLD
SEQUENCE AND STRUCTURE COMPARISON SUGGEST THAT METHIONINE AMINOPEPTIDASE, PROLIDASE, AMINOPEPTIDASE-P, AND CREATINASE SHARE A COMMON FOLD
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DOI：
10.1073/pnas.91.7.2473
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发表时间：
1994-03-29
影响因子：
11.1
通讯作者：
MATTHEWS, BW
中科院分区：
文献类型：
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作者：
BAZAN, JF;WEAVER, LH;MATTHEWS, BW
氨基酸序列比较表明，大肠杆菌蛋氨酸氨基肽酶（EC 3.4.11.18）与恶臭假单胞菌肌酐酶（EC 3.5.3.3）的c端结构域结构相关。对这两种酶的三维折叠的详细比较证实了这种同源性：在一个几乎等于260个残基的链段内，218个C（α）原子的结构在2.5埃内重叠；在这些重叠位置中，只有41个（即19%）在两条蛋白质链中具有相同的氨基酸。尽管在结构上有这种惊人的一致性，蛋氨酸氨基肽酶结合并受到Co2+的刺激，而肌酐酶不是一种依赖金属的酶。利用基于序列和结构的图谱对蛋白质数据库进行搜索，发现了其他酶，包括氨肽酶P （EC 3.4.11.9）、脯氨酸酶（EC 3.4.13.9）和agropine合成酶，它们可能与肌酶和蛋氨酸氨肽酶具有相同的“皮塔面包”折叠。
Amino acid sequence comparison suggests that the structure of Escherichia coli methionine aminopeptidase (EC 3.4.11.18) and the C-terminal domain of Pseudomonas putida creatinase (EC 3.5.3.3) are related. A detailed comparison of the three-dimensional folds of the two enzymes confirms this homology: within an almost-equal-to 260-residue chain segment, 218 C(alpha) atoms of the structures superimpose within 2.5 angstrom; only 41 of these overlapping positions (i.e., 19%) feature identical amino acids in the two protein chains. Notwithstanding this striking correspondence in structure, methionine aminopeptidase binds and is stimulated by Co2+, while creatinase is not a metal-dependent enzyme. Searches of protein data banks using sequence and structure-based profiles reveal other enzymes, including aminopeptidase P (EC 3.4.11.9), prolidase (EC 3.4.13.9), and agropine synthase, that likely share the same ''pita-bread'' fold common to creatinase and methionine aminopeptidase.