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Using X-ray crystallography of the Asp55Asn mutant of the phosphatidylcholine-preferring phospholipase C from Bacillus cereus to support the mechanistic role of Asp55 as the general base

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第一作者： Antikainen NM.

作者： Antikainen NM. ; Monzingo AF. ; Franklin CL. ; Robertus JD. ; Martin SF.

关键词 Phospholipase c from bacillus cereus Site-directed mutagenesis 2-metal ion catalysis Electron-density maps Substrate-specificity Crystal-structure Proton inventory Binding-site Active-site Resolution Dehydrogenase Mutagenesis

发布时间 2013-11-20

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Archives of Biochemistry and Biophysics

2003年417卷1期

81-86页

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Archives of Biochemistry and Biophysics

2003年417卷1期

81-86页

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Using X-ray crystallography of the Asp55Asn mutant of the phosphatidylcholine-preferring phospholipase C from Bacillus cereus to support the mechanistic role of Asp55 as the general base

Archives of Biochemistry and Biophysics

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Using X-ray crystallography of the Asp55Asn mutant of the phosphatidylcholine-preferring phospholipase C from Bacillus cereus to support the mechanistic role of Asp55 as the general base

Archives of Biochemistry and Biophysics

相似文献

同项目论文

Archives of Biochemistry and Biophysics

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