Sandbox Reserved 476

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<Structure load='1bks' size='350' frame='true' align='right'
<Structure load='1bks' size='350' frame='true' align='right'
caption='Tryptophan Synthase from Salmonella typhimurium' />
caption='Tryptophan Synthase from Salmonella typhimurium' />
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<span style="font-size:110%">
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'''Introduction'''
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----
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'''Tryptophan synthase ''' is an enzyme present in many organism families, with the notable exception of the kingdom Animalia. The role of this enzyme is to catalyze the final two steps of tryptophan biosynthesis; the first of these being the reversible conversion of indole-3-glycerol phosphate to indole(trp precursor) and glyceraldehyde-3-phosphate(known substrate within Glycolysis pathway), and the latter being the condensation reaction of indole with serine to form the ultimate products of L-tryptophan and water. It is also of significance that Tryptophan synthase was one of the first enzymes possesing two catalytic activities of great interest in the scientific community, as well as the first enzyme discovered to utilize the process of substrate channeling.<ref>Raboni S, Bettati S, Mozzarelli A (April 2009). "Tryptophan synthase: a mine for enzymologists". Cell Mol Life Sci 66 (14): 2391–403. doi:10.1007/s00018-009-0028-0. PMID 19387555</ref>
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== '''Structure''' ==
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== '''Function''' ==
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=='''Applications'''==
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=='''References'''==
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Revision as of 16:21, 2 May 2012

This Sandbox is Reserved from 13/03/2012, through 01/06/2012 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 451 through Sandbox Reserved 500.
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Contents

Tryptophan Synthase

Tryptophan Synthase from Salmonella typhimurium

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Introduction

Tryptophan synthase is an enzyme present in many organism families, with the notable exception of the kingdom Animalia. The role of this enzyme is to catalyze the final two steps of tryptophan biosynthesis; the first of these being the reversible conversion of indole-3-glycerol phosphate to indole(trp precursor) and glyceraldehyde-3-phosphate(known substrate within Glycolysis pathway), and the latter being the condensation reaction of indole with serine to form the ultimate products of L-tryptophan and water. It is also of significance that Tryptophan synthase was one of the first enzymes possesing two catalytic activities of great interest in the scientific community, as well as the first enzyme discovered to utilize the process of substrate channeling.[1]

Structure

Function

Applications

References

1.

2.

3.

4.

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