1.3.3.3: coproporphyrinogen oxidase
This is an abbreviated version!
For detailed information about coproporphyrinogen oxidase, go to the full flat file.
Word Map on EC 1.3.3.3
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1.3.3.3
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heme
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protoporphyrinogen
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coproporphyria
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protoporphyrin
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porphyria
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ferrochelatase
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uroporphyrinogen
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5-aminolevulinic
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porphobilinogen
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tetrapyrrole
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porphyrinogens
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medicine
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oxygen-independent
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coproporphyrinuria
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mg-protoporphyrin
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ala-pdt
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delta-aminolaevulinic
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uroporphyrin
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cutanea
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analysis
- 1.3.3.3
- heme
- protoporphyrinogen
- coproporphyria
- protoporphyrin
- porphyria
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ferrochelatase
- uroporphyrinogen
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5-aminolevulinic
- porphobilinogen
- tetrapyrrole
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porphyrinogens
- medicine
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oxygen-independent
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coproporphyrinuria
- mg-protoporphyrin
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ala-pdt
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delta-aminolaevulinic
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uroporphyrin
-
cutanea
- analysis
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
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Reaction
Reaction on EC 1.3.3.3 - coproporphyrinogen oxidase
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coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
active site structure
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coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
2 possible catalytic pathways of the reaction, overview, Tyrp274 is catalytically important, the following residues are not important for enzyme activity: Cys167, Tyr135, Tyr160, Tyr170, Tyr213, Tyr240, Tyr276, Trp36, Trp123, Trp166, and Trp198
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coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
analysis of catalytic mechanism, modeling of active site structure
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coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
substrate binding at the active site, structure and mechanism, catalytic mechanism
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coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
substrate binding at the active site, structure and mechanism, catalytic mechanism
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coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
CPO catalyzes two sequential oxidative decarboxylations of propionate moieties on coproporphyrinogen-III forming protoporphyrinogen-IX through the monovinyl intermediate harderoporphyrinogen
coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
reaction starts by O2 addition to the pyrrole substrate yielding a hydroperoxide, which then abstracts a proton from the reactive propionate substituent, and the reaction may then proceed through H2O elimination, followed by decarboxylation
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coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
reaction mechanism, substrate docking study and binding mode, involving residues H131, R135, D274, and R275, and active site analysis using crystal structures, molecular dynamics simulations, overview. Selectivity of the active site, formed by His131, Asn133, and Ser117, toward substituted tetrapyrroles, nonoccurrence of catalysis on the C and D rings of the tetrapyrrole. The carbonyl oxygen of G276 intervenes in the substrate anchoring by hydrogen bonding of the ring D pyrrole NH group. The pyrrole ring is very unlikely to undergo deprotonation during the catalytic cycle
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