大肠杆菌中的脯氨酸生物合成。谷氨酸半醛脱氢酶催化反应的化学计量和终产物鉴定。
Proline biosynthesis in Escherichia coli. Stoichiometry and end-product identification of the reaction catalysed by glutamate semialdehyde dehydrogenase.
作者信息
Hayzer D J, Leisinger T
出版信息
Biochem J. 1981 Aug 1;197(2):269-74. doi: 10.1042/bj1970269.
Abstract
The stoichiometry of the oxidative phosphorylation of glutamic acid 5-semialdehyde by gamma-glutamyl phosphate reductase (glutamate semialdehyde dehydrogenase) has been established. Equimolar amounts of NADP+ and L-glutamic acid 5-semialdehyde are consumed and equimolar amounts of 5-oxiopyrroilidine-2-carboxylic acid and NADPH are formed. The end-product of the reaction is demonstrated to be 5-oxopyrrolidine-2-carboxylic acid, probably arising from the true end-product gamma-glutamyl phosphate.
摘要
γ-谷氨酰磷酸还原酶（谷氨酸半醛脱氢酶）催化谷氨酸5-半醛氧化磷酸化的化学计量关系已得到确定。等摩尔量的NADP⁺和L-谷氨酸5-半醛被消耗，同时生成等摩尔量的5-氧代吡咯烷-2-羧酸和NADPH。该反应的终产物被证明是5-氧代吡咯烷-2-羧酸，可能由真正的终产物γ-谷氨酰磷酸生成。
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