Literature summary for 1.14.13.39 extracted from

Tran, Q.K.; Leonard, J.; Black, D.J.; Nadeau, O.W.; Boulatnikov, I.G.; Persechini, A.
Effects of combined phosphorylation at Ser-617 and Ser-1179 in endothelial nitric-oxide synthase on EC50(Ca2+) values for calmodulin binding and enzyme activation (2009), J. Biol. Chem., 284, 11892-11899.

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Protein Variants

Protein Variants	Comment	Organism
S1179D	the phosphomimetic substitution at Ser-1179 doubles maximal synthase activity, partially disinhibits cytochrome c reductase activity, and lowers the EC50(Ca2+) values for calmodulin binding and enzyme activation about 35%	Bos taurus
S617D/S1179D	the mutation doubles maximal synthase activity, partially disinhibits cytochrome c reductase activity, and lowers the EC50(Ca2+) values for calmodulin binding and enzyme activation	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	P29473	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 L-arginine + 3 NADPH + 3 H+ + 4 O2	-	Bos taurus	2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O	-	?

Synonyms

Synonyms	Comment	Organism
endothelial nitric-oxide synthase	-	Bos taurus
eNOS	-	Bos taurus

Cofactor

Cofactor	Comment	Organism	Structure
5,6,7,8-tetrahydro-L-biopterin	-	Bos taurus
Calmodulin	in the absence of calmodulin, the wild type enzyme activity is less than 15% of the maximum calmodulin-dependent values	Bos taurus
NADPH	-	Bos taurus

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Release 2023.1 (January 2023)