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Stimulation of human nitric oxide synthase by tetrahydrobiopterin and selective binding of the cofactor
Author(s) -
Klatt Peter,
Heinzel Burghard,
Mayer Bernd,
Ambach Edda,
Werner-Felmayer Gabriele,
Wachter Helmut,
Werner Ernst R.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80886-l
Subject(s) - tetrahydrobiopterin , biopterin , nitric oxide synthase , chemistry , nos1 , gtp cyclohydrolase i , stimulation , neopterin , atp synthase , biochemistry , cofactor , endocrinology , medicine , enzyme , biology
To check the stimulatory potency of the tetrahydro forms of the two major pteridines occurring in human tissues, neopterin and biopterin, NO synthase was purified 6000‐fold from human cerebellum. Tetrahydrobiopterin stimulated the activity up to 4.5‐fold in a concentration dependent manner with a maximum above 1 μM, whereas tetrahydroneopterin was completely inactive in concentrations up to 100 μM. Tetrahydrobiopterin, but not neopterin derivatives, were copurified with the NO synthase activity. Our results demonstrate that human cerebellum contains a tetrahydrobiopterin dependent NO synthase activity.