Tyr152 plays a central role in the catalysis of 1-aminocyclopropane-1-carboxylate synthase

1-Aminocyclopropane-1-carboxylate (ACC) synthase is a key enzyme in the regulation of ethylene biosynthesis in higher plants. To investigate the catalytic significances of two conserved tyrosine residues, Tyr151 and Tyr152, of a tomato ACC synthase isozyme (LeACS2), five ACC synthase mutants (Y151F,...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 56(2005), 418 vom: 05. Aug., Seite 2203-10
1. Verfasser: Li, Jian-Feng (VerfasserIn)
Weitere Verfasser: Qu, Liang-Hu, Li, Ning
Format: Aufsatz
Sprache:English
Veröffentlicht: 2005
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Amino Acids, Cyclic 1-aminocyclopropane-1-carboxylic acid 3K9EJ633GL Tyrosine 42HK56048U S-Adenosylmethionine 7LP2MPO46S Lyases mehr... EC 4.- 1-aminocyclopropanecarboxylate synthase EC 4.4.1.14
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520 |a 1-Aminocyclopropane-1-carboxylate (ACC) synthase is a key enzyme in the regulation of ethylene biosynthesis in higher plants. To investigate the catalytic significances of two conserved tyrosine residues, Tyr151 and Tyr152, of a tomato ACC synthase isozyme (LeACS2), five ACC synthase mutants (Y151F, Y151G, Y152F, Y152G, and Y151F/Y152F) were constructed and over-expressed in Escherichia coli. Subsequent kinetic analysis indicated that these point mutations in mutants Y152F, Y152G, and Y151F/Y152F, either reduced the catalytic efficiency more than 98% or fully inactivated ACC synthase, while Y151F and Y151G mutants reduced the enzymatic activities by 27% and 83%, respectively. It is therefore concluded that Tyr152, especially its hydroxyl group, plays an essential role in the catalysis of ACC synthase. Thus, a revised catalytic model is hereby proposed for functional ACC synthase 
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700 1 |a Qu, Liang-Hu  |e verfasserin  |4 aut 
700 1 |a Li, Ning  |e verfasserin  |4 aut 
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