Literature summary for 1.3.3.3 extracted from

Phillips, J.D.; Whitby, F.G.; Warby, C.A.; Labbe, P.; Yang, C.; Pflugrath, J.W.; Ferrara, J.D.; Robinson, H.; Kushner, J.P.; Hill, C.P.
Crystal structure of the oxygen-dependant coproporphyrinogen oxidase (Hem13p) of Saccharomyces cerevisiae (2004), J. Biol. Chem., 279, 38960-38968.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)	Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment)	Organism
25 mg/ml purified recombinant His-tagged enzyme in 20 mM Tris, pH 7.5, 5% v/v glycerol, sitting drop method, 21°C, for C-form crystals: equal volume of protein and reservoir solution, the latter containing 20% PEG 3000, 0.1 M HEPES, pH 7.5, and 0.2 M sodium acetate, optimized sulfur anomalous scattering, for form 1 crystals: sitting drops of protein and reservoir solution, the latter containing 18% PEG 8000, 0.1 M HEPES, pH 7.5, 2% isopropanol, and 0.2 M sodium acetate at 4°C, 13°C, or 21°C, for form II crystals: sitting drops of protein and reservoir solution in a 2:1 mixture, the latter containing 2.2 M ammonium sulfate, 0.1 M Tris, pH 8.5, 21°C, 10% v/v glycerol as cryoprotectant, X-ray diffraction structure determination and anaylsis at 2.0 A and 2.4 A resolution	Saccharomyces cerevisiae

Crystallization (Comment)

Organism

25 mg/ml purified recombinant His-tagged enzyme in 20 mM Tris, pH 7.5, 5% v/v glycerol, sitting drop method, 21°C, for C-form crystals: equal volume of protein and reservoir solution, the latter containing 20% PEG 3000, 0.1 M HEPES, pH 7.5, and 0.2 M sodium acetate, optimized sulfur anomalous scattering, for form 1 crystals: sitting drops of protein and reservoir solution, the latter containing 18% PEG 8000, 0.1 M HEPES, pH 7.5, 2% isopropanol, and 0.2 M sodium acetate at 4°C, 13°C, or 21°C, for form II crystals: sitting drops of protein and reservoir solution in a 2:1 mixture, the latter containing 2.2 M ammonium sulfate, 0.1 M Tris, pH 8.5, 21°C, 10% v/v glycerol as cryoprotectant, X-ray diffraction structure determination and anaylsis at 2.0 A and 2.4 A resolution

Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
additional information	identification of diverse deleterious enzyme mutations in hereditary coproporphyria, structural effects of mutations, overview	Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
30000	-	2 * 30000, recombinant enzyme, SDS-PAGE	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
coproporphyrinogen-III + O2	Saccharomyces cerevisiae	essential enzyme, catalyzes the 6th step in heme biosynthesis	protoporphyrinogen-IX + 2 CO2 + 2 H2O	-	?
additional information	Saccharomyces cerevisiae	deleterious enzyme mutations can cause hereditary coproporphyria	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography	Saccharomyces cerevisiae

Reaction

Reaction	Comment	Organism	Reaction ID
coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O	active site structure	Saccharomyces cerevisiae	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
coproporphyrinogen-III + O2	essential enzyme, catalyzes the 6th step in heme biosynthesis	Saccharomyces cerevisiae	protoporphyrinogen-IX + 2 CO2 + 2 H2O	-	?
coproporphyrinogen-III + O2	O2-dependent enzyme Hem13p	Saccharomyces cerevisiae	protoporphyrinogen-IX + 2 CO2 + 2 H2O	-	?
additional information	deleterious enzyme mutations can cause hereditary coproporphyria	Saccharomyces cerevisiae	?	-	?

Subunits

Subunits	Comment	Organism
dimer	2 * 30000, recombinant enzyme, SDS-PAGE	Saccharomyces cerevisiae
More	central flat seven-stranded antiparallel sheet flanked by alpha-helices	Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
CPO	-	Saccharomyces cerevisiae
Hem13p	-	Saccharomyces cerevisiae