Biosynthesis of norvaline, norleucine, and homoisoleucine in Serratia marcescens
Journal of Biochemistry
M KisumiI Chibata
The biosynthetic pathways of norvaline homoisoleucine were examined using regulatory mutants of leucine biosynthesis in Serratia marcescens. alpha-Isopropylmalate synthetase [EC 188.8.131.52], the first enzyme of leucine biosynthesis, catalyzed the condensations of acetyl-CoA with pyruvate, alpha-ketobutyrate, alpha-ketovalerate, or alpha-keto-beta-methylvalerate as well as alpha-ketoisovalerate. These condensations were inhibited by leucine in the alpha-aminobutyrate-resistant mutant, a mutant with derepressed leucine biosynthetic enzymes. However, these condensations were coordinately desensitized in the isoleucine leaky revertant, a leucine accumulator. The formation of norvaline or homoisoleucine was greater in the leucine accumulator, but its leucine auxotroph did not form these unnatural amino acids. Thus, norvaline and homoisoleucine are considered to be formed from alpha-ketobutyrate and alpha-keto-beta-methylvalerate by the leucine biosynthetic enzymes. This view was confirmed by the findings that a norvaline accumulator could be obtained by derivation of the leucine accumulator into an isoleucine-valine auxotroph. Norleucine was also found to be formed from alpha-ketovalerate, an alpha-ketoacid corresponding to norvaline.
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