Purification and properties of the phosphate eliminating enzyme involved in the biosynthesis of BH4 in man.
Biochem Biophys Res Commun
; 127(1): 213-9, 1985 Feb 28.
Article
en En
| MEDLINE
| ID: mdl-2983706
ABSTRACT
An enzyme catalyzing the elimination of triphosphate from 7,8-dihydroneopterin triphosphate in the presence of Mg2+ has been purified approx. 3000 fold from human liver. It has a molecular weight of approx. 63'000, a pI value of 4.4 - 4.6 and is stable at 80 degrees C for 5 min. This enzyme catalyzes the formation of tetrahydrobiopterin in the presence of sepiapterin reductase, Mg2+ and NADPH. It is thus possible, that it also catalyzes the internal oxidoreduction leading to formation of the intermediate 6-pyruvoyl-tetrahydropterin, suggesting that no further enzyme is obligatory for biosynthesis of tetrahydrobiopterin.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Pteridinas
/
Pirofosfatasas
/
Biopterinas
/
Hígado
Límite:
Humans
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
1985
Tipo del documento:
Article