Nitric Oxide Synthase: Difference between revisions

Michal Harel (talk | contribs)
No edit summary
Michal Harel (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:2g6h.png|left|200px|thumb|Crystal Structure of nitric oxide synthase, [[2g6h]]]]
[[Image:2g6h.png|left|200px|thumb|Crystal Structure of nitric oxide synthase, [[2g6h]]]]
{{STRUCTURE_2g6h|  PDB=2g6h  | SIZE=400| SCENE=Nitric_oxide_synthase/Nos/1 |right|CAPTION=Neuronal nitric oxide synthase complex with cofactor tetrahydrobiopterin, acetate and Zn, [[2g6h]] }}
{{STRUCTURE_2g6h|  PDB=2g6h  | SIZE=400| SCENE=Nitric_oxide_synthase/Nos/1 |right|CAPTION=Neuronal nitric oxide synthase dimer complex with cofactor tetrahydrobiopterin, acetate and Zn, [[2g6h]] }}
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 


'''Nitric Oxide Synthase''' (NOS) is an enzyme catalysing the formation of L-citrulline and [http://en.wikipedia.org/wiki/Nitric_Oxide/ nitric oxide] (NO) from L-arginine. NOS is a homodimeric protein with 125- to 160-kDa per monomer.  In mammals, NOS appears as 3 isozymes: neuronal NOS (nNOS), cytokine-inducible NOS (iNOS) and endothelial NOS (eNOS).  The N-terminal domain of NOS is an oxygenase domain (OD).  NOS cofactors are: NADPH, FAD, FMN, heme and O2.
'''Nitric Oxide Synthase''' (NOS) is an enzyme catalysing the formation of L-citrulline and [http://en.wikipedia.org/wiki/Nitric_Oxide/ nitric oxide] (NO) from L-arginine. NOS is a homodimeric protein with 125- to 160-kDa per monomer.  In mammals, NOS appears as 3 isozymes: neuronal NOS (nNOS), cytokine-inducible NOS (iNOS) and endothelial NOS (eNOS).  The N-terminal domain of NOS is an oxygenase domain (OD).  NOS cofactors are: NADPH, FAD, FMN, heme and O2.

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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