Article
A pivotal role for tryptophan 447 in enzymatic coupling of human endothelial nitric oxide synthase (eNOS): effects on tetrahydrobiopterin-dependent catalysis and eNOS dimerization.
The Journal of biological chemistry - 11 Oct 2013
Benson Matthew A, Batchelor Helen, Chuaiphichai Surawee, Bailey Jade, Zhu Hanneng, Stuehr Dennis J, Bhattacharya Shoumo, Channon Keith M, Crabtree Mark J
Abstract excerpt
Tetrahydrobiopterin (BH4) is a required cofactor for the synthesis of NO by NOS. Bioavailability of BH4 is a critical factor in regulating the balance between NO and superoxide production by endothelial NOS (eNOS coupling). Crystal structures of the mouse inducible NOS oxygenase domain reveal a homologous BH4-binding site located in the dimer interface and a conserved tryptophan residue that engages in hydrogen...
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