1.3.3.3: coproporphyrinogen oxidase

This is an abbreviated version!
For detailed information about coproporphyrinogen oxidase, go to the full flat file.

Reaction

Synonyms

copro'gen oxidase, Coprogen oxidase, coproporphyinogen oxidase, coproporphyrinogen III oxidase, coproporphyrinogen oxidase, coproporphyrinogen-III oxidase, coproporphyrinogenase, COX, CPgen oxidase, CPGox, CPO, CPO III oxidase, CPOX, CPOX4, CPX, CPX1, CPX2, HEM13, Hem13p, HemF, HEMN1, KlHEM13, LIN2, LMM2, O2-dependent coproporphyrinogen III oxidase, oxygen-dependent coproporphyrinogen III oxidase, oxygen-dependent coproporphyrinogen-III oxidase, Sll1185

ECTree

     1 Oxidoreductases

         1.3 Acting on the CH-CH group of donors

             1.3.3 With oxygen as acceptor

                1.3.3.3 coproporphyrinogen oxidase

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Results	in table
40	Activating Compound
17573	AA Sequence
16	Application
1	CAS Registry Number
40	Cloned(Commentary)
11	Cofactor
3	Crystallization (Commentary)
210	Disease/ Diagnostics
5	Expression
34	General Information
5	General Stability
1	IC50 Value
71	Inhibitors
10	kcat/KM [mM/s]
1	Ki Value [mM]
108	KM Value [mM]
51	Localization
26	Metals/Ions
45	Molecular Weight [Da]
101	Natural Substrates/ Products (Substrates)
126	Organism
2	Oxidation Stability
9	Pathway
26	PDB ID
21	pH Optimum
3	pH Range
2	pH Stability
1	pI Value
103	Protein Variants
35	Purification (Commentary)
9	Reaction
5	Reaction Type
110	Reference
101	Source Tissue
19	Specific Activity [micromol/min/mg]
6	Storage Stability
201	Substrates and Products (Substrate)
34	Subunits
124	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
1	Temperature Range [°C]
1	Temperature Stability [°C]
58	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.3.3.3 - coproporphyrinogen oxidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

crystal structure analysis

Homo sapiens

-

712835

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

-

656245

crystal structure analysis

Saccharomyces cerevisiae

-

712835