小扁豆幼苗中的胺氧化酶对精脒的氧化。
Oxidation of spermine by an amine oxidase from lentil seedlings.
机构信息
Istituto di Chimica Biologica, Università di Cagliari, via della Pineta, 77 09125 Cagliari, Italy.
出版信息
Plant Physiol. 1991 Feb;95(2):477-9. doi: 10.1104/pp.95.2.477.
Abstract
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 TI-HCI buffer; the K(m) value is 4.4.10(-4) molar, similar to that found with other substrates (putrescine and spermidine).
摘要
腐胺是兵豆（兵豆属）幼苗胺氧化酶的底物，氧化产物是该酶的可逆抑制剂。腐胺在末端氨基上被氧化生成二醛：每摩尔腐胺形成 2 摩尔过氧化氢和 2 摩尔氨。腐胺在 TI-HCI 缓冲液中的酶最适 pH 值为 7.9；K(m)值为 4.4.10(-4)摩尔，与其他底物（腐胺和精胺）相似。
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