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大肠杆菌中半胱氨酸合成过程中的一个酶的纯化,过表达

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Research reports

The serine acetyltransferase from Escherichia coli Over-expression, purification and preliminary crystallographic analysis

Dale B. WigleyCorresponding Author Contact Information, Jeremy P. Derrick and William V. Shaw


Department of Biochemistry, University of Leicester, Leicester LE1 7RH, UK
Received 11 October 1990;  revised 25 October 1990.  Available online 21 November 2001.

Volume 277, Issues 1-2, 17 December 1990, Pages 267-271

Abstract

An expression vector has been constructed which increases the expression of serine acetyltransferase (SAT) from E. coli to 17% of the soluble cell protein. A novel purification procedure, using dye-affinity chromatography, allows purification of SAT to homogeneity. The enzyme has been crystallised from polyethylene glycol, in the presence of L-cysteine (an inhibitor of SAT). The crystals which diffract to beyond 3.0 Å resolution are of the tetragonal spacegroup P41212(or P43212) with cell dimensions a = b = 123 Å, c = 79 Å. Since ultracentrifugation and gel-filtration experiments indicate that purified SAT is a tetramer, there appears to be one-half tetramer in the asymmetric unit (Vm = 2.55 Å3/Da).

 fulltext: The serine acetyltransferase from E. coli

另一篇:大肠杆菌和沙门氏菌中酶促合成的半胱氨酸的过程: 

The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium

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