type	Journal Article
authors	Kakuta, Y.; Igarashi, T.; Murakami, T.; Ito, H.; Matsui, H.; Honma, M.
title	1-Aminocyclopropane-1-carboxylate synthase of Penicillium citrinum: primary structure and expression in Escherichia coli and Saccharomyces cerevisiae
journal	Biosci Biotechnol Biochem
Activity	4.4.1.14
Family	4.4.1.14.a
sel	selected
ui	11515533
year	(2001)
volume	65
number	7
pages	1511-8
keywords	Amino Acid Sequence
abstract	A plant hormone, ethylene, is formed through 1-aminocyclopropane-1-carboxylic acid (ACC). A fungus, Penicillium citrinum, 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.
last changed	2018/11/27 10:24