Obermeier N, Poralla K
Arch Microbiol. 1976 Aug;109(1-2):59-63. doi: 10.1007/BF00425113.
Mutants of Bacillus subtilis constitutive for L-leucine dehydrogenase synthesis were selected. Using these mutants we could determine two functional roles for the L-leucine dehydrogenase. This enzyme liberates ammonium ions from branched chain amino acids when supplied as the sole nitrogen source. Another function is to synthesize from L-isoleucine, L-leucine, and L-valine the branched chain alpha-keto acids which are precursors of branched chain fatty acid biosythesis. These results together with the inducibility of the enzyme suggest that the L-leucine dehydrogenase has primarily a catabolic rather than an anabolic function in the metabolism of Bacillus subtilis.
筛选出了枯草芽孢杆菌中组成型合成L-亮氨酸脱氢酶的突变体。利用这些突变体,我们可以确定L-亮氨酸脱氢酶的两个功能作用。当作为唯一氮源提供时,这种酶可从支链氨基酸中释放铵离子。另一个功能是由L-异亮氨酸、L-亮氨酸和L-缬氨酸合成支链α-酮酸,这些是支链脂肪酸生物合成的前体。这些结果以及该酶的可诱导性表明,L-亮氨酸脱氢酶在枯草芽孢杆菌的代谢中主要具有分解代谢而非合成代谢功能。