Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Biochemistry & Molecular Biology
1-Aminocyclopropane-1-carboxylate Synthase of Penicillium citrinum: Primary Structure and Expression in Escherichia coli and Saccharomyces cerevisiae
Yukiko KAKUTAToshinori IGARASHIToyotaka MURAKAMIHiroyuki ITOHirokazu MATSUIMamoru HONMA
著者情報
ジャーナル フリー

2001 年 65 巻 7 号 p. 1511-1518

詳細
抄録
A plant hormone, ethylene, is formed through 1-aminocyclopropane-1-carboxylic acid (ACC). A fungus, Penicillium citrium, was found to synthesize ACC and to degrade ACC into 2-oxobutyrate and ammonia. ACC synthase, responsible for ACC synthesis in P. citrinum, was characterized on the molecular level by sequencing of N terminal and proteolytic peptides of the enzyme, and cloning and sequencing of its cDNA. The ACC synthase from P. citrinum had 430 amino acid residues and a shorter C terminal than the plant enzyme. The enzyme purified from Escherichia coli transformed with ACC-synthase-encoding DNA showed similar properties to those of the purified enzyme from P. citrinum. Saccharomyces cerevisiae with ACC synthase accumulated ACC in the medium with increasing time of incubation. The sequence of ACC synthase from P. citrinum was compared with that of the plant enzyme with discussion about important residues for catalysis.
著者関連情報

この記事は最新の被引用情報を取得できません。

© 2001 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
前の記事 次の記事
feedback
Top