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.

引用

页码：801 / &

共 11 条

[1]

BARKER HA, 1967, BIOCHEM J, V105, P1

[2]

BRAY RC, 1968, J BIOL CHEM, V242, P381

[3] MECHANISTIC SIMILARITIES IN REACTIONS CATALYZED BY DIOLDEHYDRASE AND METHYLMALONYL-COA MUTASE [J].