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Structure and mechanism of HpcH: A metal ion dependent class II aldolase from the homoprotocatechuate degradation pathway of Escherichia coli

机译:HpcH的结构和机制:大肠杆菌的同源原儿茶酸降解途径中的一种金属离子依赖性II类醛缩酶

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Microorganisms are adept at degrading chemically resistant aromatic compounds. One of the longest and most well characterized aromatic catabolic pathways is the 4-hydroxyphenylacetic acid degradation pathway of Escherichia coli. The final step involves the conversion of 4-hydroxy-2-oxoheptane-1,7-dioate into pyruvate and succinic semialdehyde. This reaction is catalyzed by 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (HpcH), a member of the divalent metal ion dependent class 11 aldolase enzymes that have great biosynthetic potential. We have solved the crystal structure of HpcH in the apo form, and with magnesium and the substrate analogue oxamate bound, to 1.6 angstrom and 2.0 angstrom, respectively. Comparison with similar structures of the homologous 2-dehydro-3-deoxygalactarate aldolase, coupled with site-directed mutagenesis data, implicate histidine 45 and arginine 70 as key catalytic residues. (C) 2007 Published by Elsevier Ltd.
机译:微生物擅长降解耐化学性的芳族化合物。最长的和最充分表征的芳香族分解代谢途径之一是大肠杆菌的4-羟苯基乙酸降解途径。最后一步涉及将4-羟基-2-氧庚烷-1,7-二酸酯转化为丙酮酸酯和琥珀酸半醛。该反应由4-羟基-2-氧代庚烷-1,7-二酸醛缩酶(HpcH)催化,HpcH是二价金属离子依赖性11类醛缩酶的成员,具有很大的生物合成潜力。我们已经解决了载脂蛋白形式的HpcH的晶体结构,并结合了镁和底物类似物草酸酯,分别为1.6埃和2.0埃。与同源2-脱氢-3-脱氧半乳糖醛酸醛缩酶的相似结构的比较,加上定点诱变数据,暗示组氨酸45和精氨酸70为关键催化残基。 (C)2007年由Elsevier Ltd.出版

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