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J. Biochem, 1976, Vol. 80, No. 2 333-339
© 1976 Japanese Biochemical Society

research-article

Biosynthesis of Norvaline, Norleucine, and Homoisoleucine in Serratia marcescens

Masahiko KISUMI, Masaki SUGIURA and Ichiro CHIBATA

Research Laboratory of Applied Biochemistry, Tanabe Seiyaku Co., Ltd. Kashima, Yodogawa-ku, Osaka, Osaka 532

The biosynthetic pathways of norvaline and homoisoleucine were examined using regulatory mutants of leucine biosynthesis in Serratia marcescens. {alpha}-Isopropylmalate synthetase [EC 4.1.3.12 [EC] ], the first enzyme of leucine biosynthesis, catalyzed the condensations of acetyl-CoA with pyruvate, {alpha}-ketobutyrate, {alpha}-ketovalerate, or {alpha}-keto-ß-methylvalerate as well as {alpha}-ketoisovalerate. These condensations were inhibited by leucine in the a-aminobutyrate-resistant mutant, a mutant with derepressed leucine biosynthetic enzymes. However, these condensations were coordinated 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-ß-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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