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- W4244557413 abstract "The 3340-bp fragment containing theEscherichia coli glyA gene coding for serine hydroxymethyltransferase was reduced in size by PCR, and the 1600-bp fragment obtained was cloned into the vector pBR322 in both orientations (5′–3′ and 3′–5′). This DNA manipulation allowed us to perform site-directed mutagenesis by PCR on theglyA gene. To overcome the problem of the presence of wild-type protein in the various mutant enzyme preparations, theE. colistrain GS245 used to express recombinant serine hydroxymethyltransferase was maderecA deficient through generalized transduction mediated by phage P1. The new strain was used for the production of a mutant form of the enzyme, in which the pyridoxal 5′-phosphate-binding lysine was substituted by a glutamine. The preparation of this mutant form was completely devoid of wild-type enzyme contamination and measurements of its catalytic activity in the transamination reactions ofl- andd-alanine confirmed the suggestion that the active site lysine is not the base that removes the α-proton from the substrate (Schirchet al.,1993,J. Biol. Chem.268, 23132–23138)." @default.
- W4244557413 created "2022-05-12" @default.
- W4244557413 date "1985-08-01" @default.
- W4244557413 modified "2023-09-30" @default.
- W4244557413 title "ISPIM news" @default.
- W4244557413 doi "https://doi.org/10.1016/0166-4972(85)90020-3" @default.
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