The quaternary structure of Escherichia coli N-acetylneuraminate lyase is essential for functional expression.
作者： Sean R.A. Devenish , Juliet A. Gerrard
DOI: 10.1016/J.BBRC.2009.07.128
关键词: Protein quaternary structure 、 Point mutation 、 Leucine 、 Biochemistry 、 Mutation 、 Enzyme kinetics 、 N-acetylneuraminate lyase 、 Lyase 、 Biology 、 Escherichia coli
摘要: Abstract As part of a general study into the impact quaternary structure on enzyme function, library 31 point mutations were engineered at dimer–dimer interface homotetrameric (β/α)8-barrel protein, N-acetylneuraminate lyase (NAL, EC 4.1.3.3). Disruption generated either soluble tetramers or putative dimers that absolutely insoluble and inactive. Intriguingly, found to have widely varying kcat values, hinting role for in catalysis. Leucine 171 was identified as essential integrity. We conclude NAL is intolerant mutation functional expression.
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