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Enzymes for Research, Diagnostic and Industrial Use

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coproporphyrinogen dehydrogenase

Cat No.
EXWM-1418
Description
This enzyme differs from EC 1.3.3.3, coproporphyrinogen oxidase, by using S-adenosyl-L-methionine (AdoMet) instead of oxygen as oxidant. It occurs mainly in bacteria, whereas eukaryotes use the oxygen-dependent oxidase. The reaction starts by using an electron from the reduced form of the enzyme's [4Fe-4S] cluster to split AdoMet into methionine and the radical 5'-deoxyadenosin-5'-yl. This radical initiates attack on the 2-carboxyethyl groups, leading to their conversion into vinyl groups. This conversion, -·CH-CH2-COO- → -CH=CH2 + CO2 + e- replaces the electron initially used.
Form
Liquid or lyophilized powder
Enzyme Commission Number
Storage
Store it at +4 ºC for short term. For long term storage, store it at -20 ºC~-80 ºC.
Synonyms
oxygen-independent coproporphyrinogen-III oxidase; HemN; coproporphyrinogen III oxidase
Reaction
coproporphyrinogen III + 2 S-adenosyl-L-methionine = protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
Notes
This item requires custom production and lead time is between 5-9 weeks. We can custom produce according to your specifications.

Our Products Cannot Be Used As Medicines Directly For Personal Use.

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