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Journal Article

Expression of the GTPase activating domain of the neurofibromatosis type 1 (NF1) gene in Escherichia coli and role of the conserved lysine residue

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Wiesmüller,  Lisa
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Wittinghofer,  Alfred
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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http://www.jbc.org/content/267/15/10207.full.pdf
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Citation

Wiesmüller, L., & Wittinghofer, A. (1992). Expression of the GTPase activating domain of the neurofibromatosis type 1 (NF1) gene in Escherichia coli and role of the conserved lysine residue. The Journal of Biological Chemistry, 267(15), 10207-10210. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1587809.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-AB66-3
Abstract
A small catalytic domain from the neurofibromatosis type 1 gene, NF1-333, consisting of 333 amino acids between residues 1197 and 1528, including an additional N-terminal methionine, was expressed in Escherichia coli as a soluble protein. Its catalytic activity under non-saturating conditions is similar to the full-length p120-GAP but different from truncated GAP-334. Under saturating conditions its kcat and KM are lower. Lys-1422, which is totally conserved in all GAP proteins, was mutated and the properties of the mutant protein investigated. Lys-1422 seems to be essential for the stability of the proteins and not for its catalytic activity.