MECHANISM OF BETA-LYSINE-MUTASE REACTION

被引:19
作者
RETEY, J
KUNZ, F
STADTMAN, TC
ARIGONI, D
机构
[1] Organisch-chemisches Laboratorium der Eidg. Technischen Hochschule, Zürich
[2] The Laboratory of Biochemistry, Section on Enzymes, National Heart Institute, National Institutes of Health, Bethesda, Maryland
来源
EXPERIENTIA | 1969年 / 25卷 / 08期
关键词
D O I
10.1007/BF01897884
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Using tritium labelled substrates it is shown that in the rearrangement of (S) -β-lysine to 3,5-diaminohexanoic acid catalysed by β-lysine mutase a stereospecific hydrogen migration from C-5 to C-6 of the substrate occurs. When the reaction is carried out in the presence of [5′-3H]-coenzyme B12, the heavy isotope is transferred both to C-6 of 3, 5-diaminohexanoate and to C-5 of β-lysine. In the latter the labelled atom occupies the same diastereotopic position as the H atom that is transferred to C-6 of the product. © 1969 Birkhäuser Verlag.
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页码:801 / &
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