MOLECULAR-CLONING, SEQUENCING AND EXPRESSION OF CDNA-ENCODING HUMAN COPROPORPHYRINOGEN OXIDASE

被引：46

作者：

TAKETANI, S ^{[1
]}

KOHNO, H ^{[1
]}

FURUKAWA, T ^{[1
]}

YOSHINAGA, T ^{[1
]}

TOKUNAGA, R ^{[1
]}

机构：

[1] KYOTO UNIV,FAC MED,DEPT PUBL HLTH,KYOTO 606,JAPAN

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 1994年 / 1183卷 / 03期

关键词：

CDNA CLONING; COPROPORPHYRINOGEN OXIDASE; HEME SYNTHESIS; MITOCHONDRION; (HUMAN);

D O I：

10.1016/0005-2728(94)90083-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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) 40291). Amino acid sequencing showed that the mature enzyme consists of 323 amino acid residues (M(r) 36842) 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.

引用

页码：547 / 549

页数：3

共 10 条

[1] PURIFICATION AND PROPERTIES OF MOUSE-LIVER COPROPORPHYRINOGEN OXIDASE [J].