Sandbox Reserved 767

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Threonine Dehydratase
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'''Threonine Dehydratase'''
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Introduction
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'''Introduction'''
Threonine dehydratase (TDH) also known as Threonine Ammonia-Lyase and Threonine Deaminase is an enzyme that catalyzes the dehydration of threonine to α-ketobutyrate.
Threonine dehydratase (TDH) also known as Threonine Ammonia-Lyase and Threonine Deaminase is an enzyme that catalyzes the dehydration of threonine to α-ketobutyrate.
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It is the first enzyme in the isoleucine biosynthetic pathway. TDH belongs to the enzyme class EC-4 which cleave C-C, C-O, C-N through hydrolysis or oxidation. TDH [EC 4.3.1.19] specifically cleaves C-N bonds. TDH is found
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It is the first enzyme in the isoleucine biosynthetic pathway. TDH belongs to the enzyme class EC-4 which cleave C-C, C-O, C-N through hydrolysis or oxidation. TDH [EC 4.3.1.19] specifically cleaves C-N bonds. DH was first discovered in E.coli around 1965 but has since been purified from other bacterial sources such as Salmonella typhimurium
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Structure
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'''Structure'''

Revision as of 06:40, 6 December 2013

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This Sandbox is Reserved from Sep 25, 2013, through Mar 31, 2014 for use in the course "BCH455/555 Proteins and Molecular Mechanisms" taught by Michael B. Goshe at the North Carolina State University. This reservation includes Sandbox Reserved 299, Sandbox Reserved 300 and Sandbox Reserved 760 through Sandbox Reserved 779.
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Threonine Dehydratase

Introduction Threonine dehydratase (TDH) also known as Threonine Ammonia-Lyase and Threonine Deaminase is an enzyme that catalyzes the dehydration of threonine to α-ketobutyrate.

It is the first enzyme in the isoleucine biosynthetic pathway. TDH belongs to the enzyme class EC-4 which cleave C-C, C-O, C-N through hydrolysis or oxidation. TDH [EC 4.3.1.19] specifically cleaves C-N bonds. DH was first discovered in E.coli around 1965 but has since been purified from other bacterial sources such as Salmonella typhimurium


Structure


Mechanism of Action


Application

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