Adenylosuccinate Synthetase

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	==Reaction Mechanism==		==Reaction Mechanism==
		+	AdSS undergoes the following amination reaction:
-		+	GTP + IMP + L-Asp -> GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
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	==References==		==References==

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Revision as of 04:01, 28 March 2010

Template:STRUCTURE 3hid

Adenylosuccinate Synthetase

Contents 1 Introduction 2 Structure 3 Reaction Mechanism 4 References

Introduction

Adenylosuccinate Synthetase (AdSS) is an enzyme that is mainly involved in purine bio-synthesis. It does this by catalyzing the GTP dependent changeover of IMP and aspartic acid to AMP. ^[1]

Structure

The AdSS enzyme is a dimer consisting of two identical monomeric subunits. The main structural component of each monomer is a centrally located beta sheet that is comprised of 10 strands. Nine of the 10 strands are parallel while the 10th strand is anti-parallel with respect to the other 9 strands. There are also several other secondary structures including 2 small 3/10 helices, two anti-parallel sheets consisting of 2 and 3 strands respectively. Additionally there are 11 alpha helices.^[2]

Helices are highlighted in green and beta sheets are shown in orange .

Reaction Mechanism

AdSS undergoes the following amination reaction:

GTP + IMP + L-Asp -> GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP

References

1. ↑ Mukhopadhyay RP, Chandra AL. Keratinase of a streptomycete. Indian J Exp Biol. 1990 Jun;28(6):575-7. PMID:1698173
2. ↑ Poland BW, Silva MM, Serra MA, Cho Y, Kim KH, Harris EM, Honzatko RB. Crystal structure of adenylosuccinate synthetase from Escherichia coli. Evidence for convergent evolution of GTP-binding domains. J Biol Chem. 1993 Dec 5;268(34):25334-42. PMID:8244965

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