Coproporphyrinogen oxidase. I. Purification, properties, and activation by phospholipids
- PMID: 7372605
Coproporphyrinogen oxidase. I. Purification, properties, and activation by phospholipids
Abstract
Coproporphyrinogen oxidase (EC 1.3.3.3), which converts coproporphyrinogen III into protoporphyrinogen IX, was purified about 3,200-fold from bovine liver. The most purified preparation had a specific activity of 6,920 units/mg of protein, the highest value so far reported, and was homogeneous in the polyacrylamide gel electrophoresis. The enzyme was monomeric and its molecular weight was approximately 71,600. The purified enzyme was analyzed for the amino acid composition and shown to have an abundance of aromatic amino acid residues amounting to 12% of the total residues. Spectral examination did not reveal the presence of heme and flavin. No metals were detected by atomic absorption spectroscopy either. Sulfhydryl reagents, metals, and metal chelators did not affect the enzyme activity to any significant extent. On the contrary, the purified enzyme was activated by crude phospholipid extracts from liver mitochondria and commercially available phospholipids about 2- to 5-fold. An increase in Vmax by the phospholipid extract as well as phosphatidylethanolamine accompanied a decrease in Km for coproporphyrinogen III from 48 microM to 18 to 25 microM. Synthetic nonionic detergents also exhibited an activation effect, although ionic detergents diminished the activity.
Similar articles
-
Purification and properties of mouse liver coproporphyrinogen oxidase.Eur J Biochem. 1989 May 1;181(2):417-21. doi: 10.1111/j.1432-1033.1989.tb14741.x. Eur J Biochem. 1989. PMID: 2540974
-
Purification and properties of coproporphyrinogen oxidase from the yeast Saccharomyces cerevisiae.Eur J Biochem. 1986 May 2;156(3):579-87. doi: 10.1111/j.1432-1033.1986.tb09617.x. Eur J Biochem. 1986. PMID: 3516695
-
Coproporphyrinogen oxidase. II. Reaction mechanism and role of tyrosine residues on the activity.J Biol Chem. 1980 May 25;255(10):4727-31. J Biol Chem. 1980. PMID: 7372606
-
Terminal steps of haem biosynthesis.Biochem Soc Trans. 2002 Aug;30(4):590-5. doi: 10.1042/bst0300590. Biochem Soc Trans. 2002. PMID: 12196143 Review.
-
Metal alteration of uroporphyrinogen decarboxylase and coproporphyrinogen oxidase.Ann N Y Acad Sci. 1987;514:55-64. doi: 10.1111/j.1749-6632.1987.tb48761.x. Ann N Y Acad Sci. 1987. PMID: 3327437 Review.
Cited by
-
Radical S-adenosylmethionine enzymes.Chem Rev. 2014 Apr 23;114(8):4229-317. doi: 10.1021/cr4004709. Epub 2014 Jan 29. Chem Rev. 2014. PMID: 24476342 Free PMC article. Review. No abstract available.
-
Functional Diversity of HemN-like Proteins.ACS Bio Med Chem Au. 2022 Jan 18;2(2):109-119. doi: 10.1021/acsbiomedchemau.1c00058. eCollection 2022 Apr 20. ACS Bio Med Chem Au. 2022. PMID: 37101745 Free PMC article. Review.
-
Molar absorptivity and A1%1cm values for proteins at selected wavelengths of the visible and ultraviolet regions. XXIV.Appl Biochem Biotechnol. 1985 Aug;11(4):287-316. doi: 10.1007/BF02798443. Appl Biochem Biotechnol. 1985. PMID: 4091547
-
Mouse protoporphyrinogen oxidase. Kinetic parameters and demonstration of inhibition by bilirubin.Biochem J. 1988 Mar 1;250(2):597-603. doi: 10.1042/bj2500597. Biochem J. 1988. PMID: 2451512 Free PMC article.
-
Bacillus subtilis HemY is a peripheral membrane protein essential for protoheme IX synthesis which can oxidize coproporphyrinogen III and protoporphyrinogen IX.J Bacteriol. 1994 Oct;176(19):5962-70. doi: 10.1128/jb.176.19.5962-5970.1994. J Bacteriol. 1994. PMID: 7928957 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
