Threonine ammonia-lyase

（重定向自Threonine dehydratase）

Key residues that interact with PLP within the active site. Generated from 1VE5.[1]

The mechanism of threonine ammonia-lyase.[8][9] PLP and lysine are shown in blue.

A diagram of the feedback regulatory pathways of threonine ammonia-lyase.[2]

Threonine ammonia-lyase, also commonly referred to as threonine deaminase or threonine dehydratase, is an enzyme responsible for catalyzing the conversion of L-threonine into alpha-ketobutyrate and ammonia. Alpha-ketobutyrate can be converted into L-isoleucine, so threonine ammonia-lyase functions as a key enzyme in BCAA synthesis. It employs a pyridoxal-5’-phosphate cofactor, similar to many enzymes involved in amino acid metabolism. It is found in bacteria, yeast, and plants, though most research to date has focused on forms of the enzyme in bacteria. This enzyme was one of the first in which negative feedback inhibition by the end product of a metabolic pathway was directly observed and studied. The enzyme serves as an excellent example of the regulatory strategies used in amino acid homeostasis.

单词	Threonine dehydratase
释义	Threonine dehydratase 英语百科 Threonine ammonia-lyase （重定向自Threonine dehydratase） Threonine ammonia-lyase, also commonly referred to as threonine deaminase or threonine dehydratase, is an enzyme responsible for catalyzing the conversion of L-threonine into alpha-ketobutyrate and ammonia. Alpha-ketobutyrate can be converted into L-isoleucine, so threonine ammonia-lyase functions as a key enzyme in BCAA synthesis. It employs a pyridoxal-5’-phosphate cofactor, similar to many enzymes involved in amino acid metabolism. It is found in bacteria, yeast, and plants, though most research to date has focused on forms of the enzyme in bacteria. This enzyme was one of the first in which negative feedback inhibition by the end product of a metabolic pathway was directly observed and studied. The enzyme serves as an excellent example of the regulatory strategies used in amino acid homeostasis.
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