Cloning and random mutagenesis of the Erwinia herbicola tyrR gene for high-level expression of tyrosine phenol-lyase

Article Abstract:

Researchers have created a mutant form of the enzyme tyrosine phenol-lyase from Erwinia herbicola that does not require L-tyrosine. This bacterium is used to produce L-DOPA for the treatment of Parkinson's disease, but the wild enzyme requires tyrosine. The tyrosine must then be separated from L-DOPA.

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Use of bacterial gamma-glutamyltranspeptidase for enzymatic synthesis of gamma-D-glutamyl compounds

Article Abstract:

An enzymatic method for synthesizing various gamma-D-glutamyl compounds efficiently and stereospecifically involving bacterial gamma-glutamyltranspeptidase with D-glutamine as a gamma-glutamyl donor was developed. By-products such as gamma-glutamylglutamine and gamma-glutamyl-gamma-glutamyltaurine were not synthesized and the yield of gamma-glutamyltaurine dramatically increased from 25 to 71%.

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A single amino acid substitution converts gama-glutamyltranspeptidase to a class IV cephalosporin acylase (glutaryl-7-aminocephalosporanic acid acylase)

Article Abstract:

Escherichia coli, one of the residues that are conserved completely in glutamyltranspeptidase (GGT) but not in IV cephalosporin acylase and the GGT enzyme with the D433N mutation was sought and studied. It is concluded that the single amino acid substitution of GGT, Asp-433 to Asn, converted GGT to cephalosporin (GL-7-ACA) acylase.

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