OXIDATION OF SPERMINE BY AN AMINE OXIDASE FROM LENTIL SEEDLINGS

被引：9

作者：

COGONI, A ^{[1
]}

PADIGLIA, A ^{[1
]}

MEDDA, R ^{[1
]}

SEGNI, P ^{[1
]}

FLORIS, G ^{[1
]}

机构：

[1] UNIV CAGLIARI,IST CHIM BIOL,VIA PINETA 77,I-09125 CAGLIARI,ITALY

来源：

PLANT PHYSIOLOGY | 1991年 / 95卷 / 02期

关键词：

D O I：

10.1104/pp.95.2.477

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

Spermine is a substrate of lentil (Lens culinaris) seedling amine oxidase and the oxidation products are reversible inactivators of the enzyme. The spermine is oxidized at the terminal amino groups to a dialdehyde: 2 moles of hydrogen peroxide and 2 moles of ammonia per mole of spermine are formed. The pH optimum of the enzyme with spermine is 7.9 in Tl-HCl buffer; the K(m) value is 4.4. 10(-4) molar, similar to that found with other substrates (putrescine and spermidine).

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收藏

页码：477 / 479

页数：3

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