Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme.

The final step in the biosynthesis of the plant signaling molecule ethylene is catalyzed by 1-aminocyclopropane-1-carboxylic acid oxidase (ACCO). ACCO requires bicarbonate as an activator and catalyzes the oxidation of ACC to give ethylene, CO2, and HCN. We report crystal structures of ACCO in apo-f...

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Main Authors: Zhang, Z, Ren, J, Clifton, I, Schofield, C
Format: Journal article
Language:English
Published: 2004
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author Zhang, Z
Ren, J
Clifton, I
Schofield, C
author_facet Zhang, Z
Ren, J
Clifton, I
Schofield, C
author_sort Zhang, Z
collection OXFORD
description The final step in the biosynthesis of the plant signaling molecule ethylene is catalyzed by 1-aminocyclopropane-1-carboxylic acid oxidase (ACCO). ACCO requires bicarbonate as an activator and catalyzes the oxidation of ACC to give ethylene, CO2, and HCN. We report crystal structures of ACCO in apo-form (2.1 A resolution) and complexed with Fe(II) (2.55 A) or Co(II) (2.4 A). The active site contains a single Fe(II) ligated by three residues (His177, Asp179, and His234), and it is relatively open compared to those of the 2-oxoglutarate oxygenases. The side chains of Arg175 and Arg244, proposed to be involved in binding bicarbonate, project away from the active site, but conformational changes may allow either or both to enter the active site. The structures will form a basis for future mechanistic and inhibition studies.
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spelling oxford-uuid:d03be2af-9307-47a6-990c-085a7f50267e2022-03-27T07:48:32ZCrystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d03be2af-9307-47a6-990c-085a7f50267eEnglishSymplectic Elements at Oxford2004Zhang, ZRen, JClifton, ISchofield, CThe final step in the biosynthesis of the plant signaling molecule ethylene is catalyzed by 1-aminocyclopropane-1-carboxylic acid oxidase (ACCO). ACCO requires bicarbonate as an activator and catalyzes the oxidation of ACC to give ethylene, CO2, and HCN. We report crystal structures of ACCO in apo-form (2.1 A resolution) and complexed with Fe(II) (2.55 A) or Co(II) (2.4 A). The active site contains a single Fe(II) ligated by three residues (His177, Asp179, and His234), and it is relatively open compared to those of the 2-oxoglutarate oxygenases. The side chains of Arg175 and Arg244, proposed to be involved in binding bicarbonate, project away from the active site, but conformational changes may allow either or both to enter the active site. The structures will form a basis for future mechanistic and inhibition studies.
spellingShingle Zhang, Z
Ren, J
Clifton, I
Schofield, C
Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme.
title Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme.
title_full Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme.
title_fullStr Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme.
title_full_unstemmed Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme.
title_short Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme.
title_sort crystal structure and mechanistic implications of 1 aminocyclopropane 1 carboxylic acid oxidase the ethylene forming enzyme
work_keys_str_mv AT zhangz crystalstructureandmechanisticimplicationsof1aminocyclopropane1carboxylicacidoxidasetheethyleneformingenzyme
AT renj crystalstructureandmechanisticimplicationsof1aminocyclopropane1carboxylicacidoxidasetheethyleneformingenzyme
AT cliftoni crystalstructureandmechanisticimplicationsof1aminocyclopropane1carboxylicacidoxidasetheethyleneformingenzyme
AT schofieldc crystalstructureandmechanisticimplicationsof1aminocyclopropane1carboxylicacidoxidasetheethyleneformingenzyme