Molecular cloning, sequencing and expression of cDNA encoding human coproporphyrinogen oxidase.

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.

• Authors: S Taketani, H Kohno, T Furukawa, T Yoshinaga, R Tokunaga
• Journal: Biochimica et biophysica acta (Biochim Biophys Acta) Vol. 1183 Issue 3 Pg. 547-9 (Jan 04 1994) ISSN: 0006-3002 [Print] Netherlands
• PMID: 8286403 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• DNA, Complementary
• Coproporphyrinogen Oxidase

Topics

• Amino Acid Sequence
• Animals
• Base Sequence
• Cloning, Molecular
• Coproporphyrinogen Oxidase (chemistry, genetics)
• DNA, Complementary (chemistry, isolation & purification)
• Gene Expression
• Humans
• Mice
• Molecular Sequence Data