Molecular cloning, sequencing and expression of cDNA encoding human coproporphyrinogen oxidase.
Biochim Biophys Acta
; 1183(3): 547-9, 1994 Jan 04.
Article
em En
| MEDLINE
| ID: mdl-8286403
ABSTRACT
A complete cDNA clone encoding human coproporphyrinogen (coprogen) oxidase, the sixth enzyme in the heme biosynthetic pathway, has been isolated from a human placenta cDNA library. The cDNA had an open reading frame of 1062 base pairs encoding a protein of 354 amino acid residues (M(r) 40,291). Amino acid sequencing showed that the mature enzyme consists of 323 amino acid residues (M(r) 36,842) with a putative leader peptide of 31 amino acid residues. The human enzyme showed an 86% identity to the mouse enzyme. In addition, the recombinant enzyme which did not contain leader peptide was actively expressed in Escherichia coli. The isolation and expression of cDNA for human coprogen oxidase should facilitate studies of the structure of the gene as well as characterization of molecular lesions causing hereditary coproporphyria.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
DNA Complementar
/
Coproporfirinogênio Oxidase
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1994
Tipo de documento:
Article
País de afiliação:
Japão