Steady-State Kinetics of Substrate Binding and Iron Release in Tomato ACC Oxidase

Julia S.Thrower; Richard Blalock III; Judith P.Klinman

首页> 外文期刊>Biochemistry >Steady-State Kinetics of Substrate Binding and Iron Release in Tomato ACC Oxidase

【24h】

Steady-State Kinetics of Substrate Binding and Iron Release in Tomato ACC Oxidase

机译：番茄ACC氧化酶中底物结合和铁释放的稳态动力学

获取原文

获取原文并翻译 | 示例

掌桥外文数据库（机构版） >>

开具论文收录证明 >>

文献代查 >>

页面导航

摘要
著录项
相似文献
相关主题

摘要

l-Aminocyclopropane-l-carboxylate oxidase (ACC oxidase) catalyzes the last step in the biosynthetic pathway of the plant hormone, ethylene. This unusual reaction results in the oxidative ring cleavage of l-aminocyclopropane carboxylate (ACC) into ethylene, cyanide, and C0_2 and requires ferrous ion, ascorbate, and molecular oxygen for catalysis. A new purification procedure and assay method have been developed for tomato ACC oxidase that result in greatly increased enzymatic activity. This method allowed us to determine the rate of iron release from the enzyme and the effect of the activator, C0_2, on this rate. Initial velocity studies support an ordered kinetic mechanism where ACC binds first followed by 0_2; ascorbate can bind after 0_2 or possibly before ACC. This kinetic mechanism differs from one recently proposed for the ACC oxidase from avocado.

机译：1-氨基环丙烷-1-羧酸氧化酶（ACC氧化酶）催化植物激素乙烯的生物合成途径中的最后一步。这种不寻常的反应导致I-氨基环丙烷羧酸酯（ACC）的氧化环裂解为乙烯，氰化物和CO_2，并且需要亚铁离子，抗坏血酸和分子氧进行催化。已经开发了用于番茄ACC氧化酶的新的纯化程序和测定方法，其导致大大提高的酶活性。该方法使我们能够确定酶中铁的释放速率以及活化剂C0_2对该速率的影响。初始速度研究支持一种有序的动力学机制，其中ACC首先结合，然后是0_2。抗坏血酸可以在0_2之后或在ACC之前结合。这种动力学机理不同于最近提出的鳄梨ACC氧化酶的动力学机理。

著录项

来源
《Biochemistry》 |2001年第32期|共8页
作者
Julia S.Thrower; Richard Blalock III; Judith P.Klinman;
展开▼
作者单位

展开▼
收录信息
原文格式 PDF
正文语种 eng
中图分类
关键词

相似文献

外文文献
中文文献
专利

1. Steady-State Kinetics of Substrate Binding and Iron Release in Tomato ACC Oxidase [J] . Julia S.Thrower, Richard Blalock III, Judith P.Klinman Biochemistry . 2001,第32期

机译：番茄ACC氧化酶中底物结合和铁释放的稳态动力学
2. Substrate-binding recognition and specificity of trehalose phosphorylase from Schizophyllum commune examined in steady-state kinetic studies with deoxy and deoxyfluoro substrate analogues and inhibitors. [J] . Eis C, Nidetzky B The Biochemical Journal . 2002,第Pta2期

机译：在稳态动力学研究中，用脱氧和脱氧氟底物类似物和抑制剂检查了裂褶菌属海藻糖磷酸酶的底物结合识别和特异性。
3. Substrate-binding recognition and specificity of trehalose phosphorylase from Schizophyllum commune examined in steady-state kinetic studies with deoxy and deoxyfluoro substrate analogues and inhibitors [J] . Eis C, Nidetzky B The Biochemical Journal . 2002,第2期

机译：稳态动力学研究中使用脱氧和脱氧氟底物类似物和抑制剂检查了裂褶菌属海藻糖磷酸化酶的底物结合识别和特异性
4. ACC-Oxidase Is the Rate Limiting Step in Ethylene Biosynthesis during Postharvest Storage of Tomato [C] . B. Van de Poel, I. Bulens, M.L.A.T.M. Hertog, International Conference Postharvest Unlimited . 2012

机译：ACC-氧化酶是番茄后储存期间乙烯生物合成的速率限制步骤
5. Molecular cloning of two 1-aminocyclopropane-1-carboxylate (ACC) synthases and an ACC oxidase from Pelargonium x hortorum cv. Snow Mass leaves. [D] . Wang, Tzann-Wei. 1994

机译：从天竺葵x hortorum cv的两个1-氨基环丙烷-1-羧酸（ACC）合成酶和ACC氧化酶的分子克隆。雪团叶。
6. Substrate-binding recognition and specificity of trehalose phosphorylase from Schizophyllum commune examined in steady-state kinetic studies with deoxy and deoxyfluoro substrate analogues and inhibitors. [O] . Christian Eis, Bernd Nidetzky 2002

机译：在稳态动力学研究中用脱氧和脱氧氟底物类似物和抑制剂检查了裂褶菌属海藻糖磷酸化酶的底物结合识别和特异性。
7. Substrate-binding recognition and specificity of trehalose phosphorylase from Schizophyllum commune examined in steady-state kinetic studies with deoxy and deoxyfluoro substrate analogues and inhibitors. [O] . Eis Christian, Nidetzky Bernd 2002

机译：在稳态动力学研究中，用脱氧和脱氧氟底物类似物和抑制剂检查了裂褶菌属海藻糖磷酸化酶的底物结合识别和特异性。

Steady-State Kinetics of Substrate Binding and Iron Release in Tomato ACC Oxidase

摘要

著录项

相似文献

相关主题

期刊订阅