Escherichia coli K12 mutants defective in the glycine cleavage enzyme system

✍ Scribed by Plamann, Michael D. ;Rapp, William D. ;Stauffer, George V.

• Publisher: Springer
• Year: 1983
• Tongue: English
• Weight: 613 KB
• Volume: 192
• Category: Article
• ISSN: 0026-8925
• DOI: 10.1007/bf00327641

✦ Synopsis

Two routes of one-carbon biosynthesis have been described in Escherichia coli K12. One is from serine via the serine hydroxymethyltransferase (SHMT) reaction, and the other is from glycine via the glycine cleavage (GCV) enzyme system. To isolate mutants deficient in the GCV pathway, we used a selection procedure that is based on the assumption that loss of this enzyme system in strains blocked in serine biosynthesis results in their inability to use glycine as a serine source. Mutants were accordingly isolated that grow with a serine supplement, but not with a glycine supplement. Enzyme assays demonstrated that three independently isolated mutants have no detectable GCV enzyme activity. The absence of a functional GCV pathway results in the excretion of glycine, but has no affect on the cell's primary source of one-carbon units, the SHMT reaction. The new mutations, designated gcv, were mapped between the serA and lysA genes on the E. coli chromosome.