Nitric Oxide Synthase: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Michal Harel (talk | contribs) No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
| Line 1: | Line 1: | ||
<StructureSection load='2g6h' size=' | <StructureSection load='2g6h' size='350' side='right' caption='Neuronal nitric oxide synthase dimer complex with cofactor tetrahydrobiopterin, acetate and Zn+2 (grey), (PDB entry [[2g6h]])' scene=''> | ||
'''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) (for details see [[Nos1]]), 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. See also [[Nos1]]. | '''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) (for details see [[Nos1]]), 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. See also [[Nos1]]. | ||
| Line 124: | Line 124: | ||
**[[3nos]], [[4d1o]] – h-eNOS OD+arginine<br /> | **[[3nos]], [[4d1o]] – h-eNOS OD+arginine<br /> | ||
**[[1m9j]] – h-eNOS OD+chlorzoxazone<br /> | **[[1m9j]] – h-eNOS OD+chlorzoxazone<br /> | ||
**[[1m9k]], [[1m9r]], [[4d1p]] – h-eNOS OD+ inhibitor<br /> | **[[1m9k]], [[1m9r]], [[4d1p]], [[6av7]], [[6av6]] – h-eNOS OD+ inhibitor<br /> | ||
**[[1nsi]] - h-eNOS OD+ Zn | **[[1nsi]] - h-eNOS OD+ Zn | ||