Galactaro δ-lactone isomerase: lactone isomerization by a member of the amidohydrolase superfamily.

Galactaro δ-lactone isomerase: lactone isomerization by a member of the amidohydrolase superfamily.
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DOI:
10.1021/bi5000492
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发表时间:
2014-02-04
期刊:
影响因子:
2.9
通讯作者:
Gerlt JA
Gerlt JA
中科院分区:
生物学3区
文献类型:
--
作者:
Bouvier JT;Groninger-Poe FP;Vetting M;Almo SC;Gerlt JA

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根癌土壤杆菌菌株C58可以通过其中第一步是将d-半乳糖醛酸氧化为d-半乳糖-1,5-内酯的途径利用d-半乳糖醛酸作为唯一碳源。我们已经鉴定了一种新的酶,d-半乳糖醛酸内酯异构酶(GLI),它催化d-半乳糖醛酸-1,5-内酯异构化为d-半乳糖醛酸-1,4-内酯。GLI是功能多样的酰胺水解酶超家族的成员,是LigI的同源物,其在木质素降解中催化2-吡喃酮-4,6-二羧酸的水解。GLI催化内酯异构化而不是水解的能力可以通过不存在2-吡喃酮-4,6-二羧酸内酯酶所使用的一般碱性催化来解释。
Agrobacterium tumefaciens strain C58 can utilize d-galacturonate as a sole source of carbon via a pathway in which the first step is oxidation of d-galacturonate to d-galactaro-1,5-lactone. We have identified a novel enzyme, d-galactarolactone isomerase (GLI), that catalyzes the isomerizaton of d-galactaro-1,5-lactone to d-galactaro-1,4-lactone. GLI, a member of the functionally diverse amidohydrolase superfamily, is a homologue of LigI that catalyzes the hydrolysis of 2-pyrone-4,6-dicarboxylate in lignin degradation. The ability of GLI to catalyze lactone isomerization instead of hydrolysis can be explained by the absence of the general basic catalysis used by 2-pyrone-4,6-dicarboxylate lactonase.
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