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梭菌脯氨酸还原酶还原D-脯氨酸过程中羧基氧的命运。

The fate of the carboxyl oxygens during D-proline reduction by clostridial proline reductase.

作者信息

Arkowitz R A, Dhe-Paganon S, Abeles R H

机构信息

MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.

出版信息

Arch Biochem Biophys. 1994 Jun;311(2):457-9. doi: 10.1006/abbi.1994.1262.

Abstract

D-Proline is converted to 5-amino valeric acid by D-proline reductase. This conversion involves the reductive cleavage of the alpha-carbon-nitrogen bond. We have examined the fate of the carboxyl oxygen atoms during conversion of D-proline to delta-NH2-valeric acid. 18O atoms from the carboxyl group of D-proline are not lost during conversion to product. In contrast, in the conversion of glycine to acetyl phosphate by glycine reductase a carboxyl oxygen atom is lost to solvent. An intermediate acyl-enzyme is found during the reduction of glycine. We conclude that the reduction of proline proceeds without the formation of an acyl enzyme intermediate.

摘要

D-脯氨酸通过D-脯氨酸还原酶转化为5-氨基戊酸。这种转化涉及α-碳-氮键的还原裂解。我们研究了D-脯氨酸转化为δ-NH2-戊酸过程中羧基氧原子的去向。D-脯氨酸羧基中的18O原子在转化为产物的过程中不会丢失。相比之下,在甘氨酸还原酶将甘氨酸转化为乙酰磷酸的过程中,一个羧基氧原子会释放到溶剂中。在甘氨酸还原过程中发现了一种中间酰基酶。我们得出结论,脯氨酸的还原过程中不会形成酰基酶中间体。

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