Sandbox Reserved 766

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===Amino Acid Composition===
===Amino Acid Composition===
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The Entire amino acid sequence for this enzyme complex can be found below.
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The Entire amino acid sequence for this enzyme complex can be found below.<ref>"RCSB Protein Data Bank - RCSB PDB - 1CT9 Structure Summary." RCSB Protein Data Bank - RCSB PDB - 1CT9 Structure Summary. N.p., n.d. Web. 01 Dec. 2013.
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<ref/>
ASNS consists 1662 residues or 554 amino acids with a molecular weight of 62.7 kDa.
ASNS consists 1662 residues or 554 amino acids with a molecular weight of 62.7 kDa.
[[Image:Screen Shot 2013-12-04 at 7.18.44 PM.png |480px||left|]]
[[Image:Screen Shot 2013-12-04 at 7.18.44 PM.png |480px||left|]]

Revision as of 03:59, 7 December 2013

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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Asparagine Synthetase crystallized from Escherichia Coli using X-Ray Diffraction at a resolution of 2.0 Angstroms.

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Introduction

Asparagine Synthetase (ASNS) is an enzyme that catalyzes the conversion of Aspartic Acid to Asparagine through an ATP dependent amination reaction, using Mg2+ as a co-factor. ASNS can be found in both plants and mammals, however, in plants there are two forms ASNS-A and ASNS-B[1]. Both forms use the same starting molecule of Aspartic Acid and produce Asparagine, the only difference coming from the source of the Nitrogen. ASNS-A uses inorganic Nitrogen in the form of ammonia or diatomic Nitrogen and ASNS-B uses Glutamine as its Nitrogen source; ASNS-B will be the focus of this page because it is very similar and undergoes the same reaction as ASNS in mammals. ASNS is in almost every somatic mammalian cell but is expressed in exponentially higher concentrations in the pancreas.

Structure

Asparagine Synthetase is a homodimer comprised of two domains ligated together. ASPS consists of a (residues 2-191) and and complex (residues 213-536). There are two specific domains that contain the substrate binding sites. The N-terminal domain which contains two layers of anti-parallel beta sheets comprised of six layers each, this is where the Glutamine binds. A C-terminal domain also exists, it is comprised of five parallel beta sheets with alpha helices on either side of it, [2] this is where the Mg2+, ATP and Aspartic Acid bind. The two active sites contained within the terminal domains are linked together by a tunnel of hydrophobic and polar surface amino acid residues. Specifically is important for the binding of the Beta-Asparty-AMP intermediate into the enzyme.

Amino Acid Composition

The Entire amino acid sequence for this enzyme complex can be found below.[3]

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