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体内应激诱导的1-氨基环丙烷羧酸合酶的失活与体外底物依赖性失活不同。

Inactivation of stress induced 1-aminocyclopropane carboxylate synthase in vivo differs from substrate-dependent inactivation in vitro.

作者信息

Spanu P, Felix G, Boller T

机构信息

Botanisches Institut der Universität Basel, Hebelstrasse 1, CH-4056 Basel, Switzerland.

出版信息

Plant Physiol. 1990 Aug;93(4):1482-5. doi: 10.1104/pp.93.4.1482.

Abstract

The activity of 1-aminocyclopropane carboxylate (ACC) synthase increased rapidly in tomato (Lycopersicon esculentum Mill.) leaf discs after vacuum infiltration, reached a maximum after about 30 minutes, and subsequently decayed with an apparent half-life of about 20 minutes. Aminoethoxyvinylglycine, a known inhibitor of ACC synthase, did not alter the apparent turnover of ACC synthase in vivo although it efficiently blocked inactivation of the enzyme by its substrate S-adenosylmethionine in vitro. Similar results were obtained, using a novel assay with permeabilized cells, for ACC synthase in tomato cell cultures treated with a fungal elicitor. The results indicate that inactivation of ACC synthase in vivo differs from substrate-dependent inactivation in vitro.

摘要

番茄(Lycopersicon esculentum Mill.)叶片圆片在真空渗入后,1-氨基环丙烷羧酸(ACC)合酶的活性迅速增加,约30分钟后达到最大值,随后以约20分钟的表观半衰期衰减。氨基乙氧基乙烯基甘氨酸是一种已知的ACC合酶抑制剂,虽然它在体外能有效阻断该酶被其底物S-腺苷甲硫氨酸的失活,但在体内并未改变ACC合酶的表观周转。使用一种针对透化细胞的新检测方法,对用真菌激发子处理的番茄细胞培养物中的ACC合酶进行检测,也得到了类似结果。这些结果表明,ACC合酶在体内的失活与体外的底物依赖性失活不同。

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