Crystal structures of Pseudomonas aeruginosa guanidinobutyrase and guanidinopropionase, members of the ureohydrolase superfamily
Crystal structures of Pseudomonas aeruginosa guanidinobutyrase and guanidinopropionase, members of the ureohydrolase superfamily
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DOI：
10.1016/j.jsb.2011.05.002
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发表时间：
2011-09-01
影响因子：
3
通讯作者：
Suh, Se Won
中科院分区：
文献类型：
--
作者：
Lee, Sang Jae;Kim, Do Jin;Suh, Se Won
铜绿假单胞菌胍基丁酸酶（GbuA）和胍基丙酸酶（GpuA）分别催化4-胍基丁酸和3-胍基丙酸的水解。它们属于脲水解酶超家族，其包括尿素酶、胍丁胺酶、前氨基乙酸脒基水解酶和甲酰亚胺谷氨酰胺酶。在这项研究中，我们已经确定了从铜绿假单胞菌GbuA和GpuA的晶体结构，以提供其底物特异性的结构洞察。虽然GbuA和GpuA共享典型的尿素水解酶超家族的共同结构折叠，但它们在两个活性位点环中表现出显着的变化。位于活性位点环1的GbuA的Met 161和GpuA的Tyr 157的突变显著影响了它们的酶性质，这意味着它们在催化中的重要作用。(C)2011 Elsevier Inc. All rights reserved.
Pseudomonas aeruginosa guanidinobutyrase (GbuA) and guanidinopropionase (GpuA) catalyze the hydrolysis of 4-guanidinobutyrate and 3-guanidinopropionate, respectively. They belong to the ureohydrolase superfamily, which includes arginase, agmatinase, proclavaminate amidinohydrolase, and formiminoglutamase. In this study, we have determined the crystal structures of GbuA and GpuA from P. aeruginosa to provide a structural insight into their substrate specificity. Although GbuA and GpuA share a common structural fold of the typical ureohydrolase superfamily, they exhibit significant variations in two active site loops. Mutagenesis of Met161 of GbuA and Tyr157 of GpuA, both of which are located in the active site loop 1 and predicted to be involved in substrate recognition, significantly affected their enzymatic properties, implying their important roles in catalysis. (C) 2011 Elsevier Inc. All rights reserved.