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1.3.98.3: coproporphyrinogen dehydrogenase

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

Word Map on EC 1.3.98.3

Reaction

Coproporphyrinogen III
+ 2 S-adenosyl-L-methionine =
protoporphyrinogen IX
 + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine

Synonyms

anaerobic coproporphyrinogen III oxidase, At5g63290, AtHEMN1, BtrN, CgoX, Coprogen oxidase, coproporphyrinogen III oxidase, coproporphyrinogen oxidase, coproporphyrinogenase, CPO, EC 1.3.99.22, HemN, HEMN1, HemW, More, oxidase, coproporphyrinogen, oxygen-independent coproporphyrinogen III oxidase, oxygen-independent coproporphyrinogen-III oxidase, oxygen-independent CPO, radical S-adenosyl-L-methionine dehydrogenase, radical SAM enzyme, Sll1876, Sll1917, viperin

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.98 With other, known, physiological acceptors
                1.3.98.3 coproporphyrinogen dehydrogenase

Crystallization

Crystallization on EC 1.3.98.3 - coproporphyrinogen dehydrogenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure
-
crystal structure, co-crystallized with S-adenosyl-L-methionine, hanging-drop vapor diffusion method, X-ray analysis
presence of an unusually coordinated iron-sulfur cluster and two molecules of S-adenosylmethionine, which is of functional importance
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under strictly anaerobic conditions, comparison of the crystal structures of the three radical SAM enzymes HemN, BioB and MoaA show that the enzymes are structurally significantly different
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