Nitric Oxide Synthase: Difference between revisions

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{{STRUCTURE_2g6h|PDB=2g6h|SCENE=Nitric_oxide_synthase/Nos_oxygenase_med_cofaktore/1}}
{{STRUCTURE_2g6h|PDB=2g6h|SCENE=Nitric_oxide_synthase/Nos_oxygenase_med_cofaktore/1}}


The <scene name='Sandbox_5/Nos_oxygenase_med_cofaktore/3'>oxygenase domain</scene> contains the active site of the enzyme. The active site binds the substrate L-<scene name='Sandbox_5/Nos_oxygenase_arg/2'>Arginine</scene> ([http://en.wikipedia.org/wiki/Arginine Arginine]) and is converted into citruline and NO (explained in details below). The domain has three cofactors bound:  
The <scene name='Sandbox_5/Nos_oxygenase_med_cofaktore/3'>oxygenase domain</scene> contains the active site of the enzyme. The active site binds the substrate L-<scene name='Sandbox_5/Nos_oxygenase_arg/2'>Arginine</scene> ([http://en.wikipedia.org/wiki/Arginine Arginine]) which is converted into citruline and NO (explained in details below). The domain has three cofactors bound:  


<scene name='Sandbox_5/Nos_oxygenase_bh4/2'>BH4</scene> ([http://en.wikipedia.org/wiki/BH4 (6R).5,6,7,8-Tetrahydrobiopterin])
<scene name='Sandbox_5/Nos_oxygenase_bh4/2'>BH4</scene> ([http://en.wikipedia.org/wiki/BH4 (6R).5,6,7,8-Tetrahydrobiopterin])
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and a <scene name='Nitric_oxide_synthase/Nos_oxygenase_zinc/1'>Zinc ion</scene>.
and a <scene name='Nitric_oxide_synthase/Nos_oxygenase_zinc/1'>Zinc ion</scene>.


General Structure
==== General Structure ====
The oxygenase domain can also be divided into three subdomains. Firstly, the substrate-binding subdomain, which is crescent in shape, binds the substrate in an interior pocket of the crescent. The Heme group is located between the tips of the crescent shape, thus closing the pocket in which the substrate is located. Secondly the the BH4 binding subdomain serves as a cap for the for the cavity created by the substrate binding domain's crescent shape. Thirdly there is a subdomain with two helical bundles making up a hydrophobic core, however this subdomain is not thought to take part of the catalytic activity of the enzyme.
The oxygenase domain can be divided into three subdomains. Firstly, the substrate-binding subdomain, which is crescent in shape, binds the substrate in an interior pocket of the crescent. The Heme group is located between the tips of the crescent shape, thus closing the pocket in which the substrate is located. Secondly the the H4B binding subdomain serves as a cap for the for the cavity created by the substrate binding domain's crescent shape. Thirdly there is a subdomain with two helical bundles making up a hydrophobic core, however this subdomain is not thought to take part of the catalytic activity of the enzyme.


=== Substrate binding ===
=== Substrate binding ===

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Michael Skovbo Windahl, Sara Toftegaard Petersen, Mathilde Thomsen, Mette Trauelsen, Eran Hodis, Jaime Prilusky, Karl Oberholser, Alexander Berchansky, Michal Harel, Ann Taylor