User:Kay Owosela
From Proteopedia
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= Stoichiometry = | = Stoichiometry = | ||
| - | The stoichiometry of Glutamine Synthetase is as follows: | ||
| - | Glutamate + NHз + ATP --> Glutamine + ADP + Pi + H+ | ||
| - | In this reaction, Glutamate is used as a major reactant and ATP is used for energy to form Glutamine. It should be noted that along with the enzyme, Me+ which can be either manganese or magnesium is used as a catalyst. | ||
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| - | This is however, a 2-step reaction. In the first step of this reaction, an intermediate Υ-glutamyl phosphate is formed. The formation of the intermediate is done by phosphoryl transfer an ATP group Y-carboxylate group of glutamate. In the second step of this reaction, NHз attacks the activated intermediate to release the phosphate group yielding Glutamine. | ||
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| - | = Quarternary Structure of Salmonella typhimurium Glutamine Synthetase= | ||
The enzyme Glutamine Synthetase is made up of twelve subunits. The structure consists of two identical hexameric rings held together by hydrophobic and hydrogen bonding forces. The N-terminal helix of each subunit is exposed to hydrophilic solvent, where as the C-terminal is concealed in hydrophobic regions inside the helical structure of the rings. The central channel is linked together by six four-stranded anti-parallel L-sheets which along with the twelve monomers enhance the stability of the ring structure. | The enzyme Glutamine Synthetase is made up of twelve subunits. The structure consists of two identical hexameric rings held together by hydrophobic and hydrogen bonding forces. The N-terminal helix of each subunit is exposed to hydrophilic solvent, where as the C-terminal is concealed in hydrophobic regions inside the helical structure of the rings. The central channel is linked together by six four-stranded anti-parallel L-sheets which along with the twelve monomers enhance the stability of the ring structure. | ||
Revision as of 19:00, 18 December 2008
Biol 430
Biology Major
Partners: Delo Sarr, Mustafa Husain
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Contents |
Jmol practice
Backbone with ligand
Labeled Ligands in Chain A
Active Site with Amino Acid Residues
Connection between Chain F residue 63 and Chain G residue 319
Stoichiometry
The enzyme Glutamine Synthetase is made up of twelve subunits. The structure consists of two identical hexameric rings held together by hydrophobic and hydrogen bonding forces. The N-terminal helix of each subunit is exposed to hydrophilic solvent, where as the C-terminal is concealed in hydrophobic regions inside the helical structure of the rings. The central channel is linked together by six four-stranded anti-parallel L-sheets which along with the twelve monomers enhance the stability of the ring structure.
Active Site
In this enzyme, there are 12 similar subunits bonded to each other. Each subunit has an active site. The active site of glutamine synthetase lies primarily around 3 manganese atoms. It is surrounded by 3 important ligands: MPD, ADP, TL as labeled in the applet. ADP is short for Adenosite Diphosphate. The ligand MPD is (4s)-2-methyl-2,4-pentanediol. And the metal ion, Thallium is also labeled in the applet.
Glutamine Synthetase Symmetry
Reference
1. Eisenberg, David and Gill, Harindarpal and Pfluegl, Gaston and Rotstein, Sergio. “Structure-function relationships of glutamine synthetases.” Elsevier, archives of biochemistry and biophysics 1477(Dec 1999):122-123.
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