Rat liver uroporphyrinogen III synthase has similar properties to the enzyme from Euglena gracilis, including absence of a requirement for a reversibly bound cofactor for activity.
Biochem J
; 253(1): 275-9, 1988 Jul 01.
Article
em En
| MEDLINE
| ID: mdl-3138984
ABSTRACT
Uroporphyrinogen III synthase purified from rat liver is a monomer of Mr 36,000 by gel filtration and 28,000 by SDS/polyacrylamide-gel electrophoresis. The enzyme exists in two interconvertible forms separable on h.p.l.c. Both forms of the enzyme could be renatured with full activity after SDS/polyacrylamide-gel electrophoresis, demonstrating the absence of a reversibly bound cofactor. The enzyme activity could be inhibited by pyridoxal 5'-phosphate in the absence and in the presence of NaBH4, consistent with (an) essential lysine residue(s). The enzyme thus shows great similarity to that from Euglena gracilis.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Uroporfirinogênio III Sintetase
/
Hidroliases
/
Fígado
Limite:
Animals
Idioma:
En
Revista:
Biochem J
Ano de publicação:
1988
Tipo de documento:
Article
País de afiliação:
Irlanda