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Literature summary for 1.3.98.3 extracted from

  • Layer, G.; Grage, K.; Teschner, T.; Schuenemann, V.; Breckau, D.; Masoumi, A.; Jahn, M.; Heathcote, P.; Trautwein, A.X.; Jahn, D.
    Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-L-methionines (2005), J. Biol. Chem., 280, 29038-29046.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
mutated enzymes expressed in Escherichia coli BL21(DE3) Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
presence of an unusually coordinated iron-sulfur cluster and two molecules of S-adenosylmethionine, which is of functional importance Escherichia coli

Protein Variants

Protein Variants Comment Organism
E145A appears colorless, the [4Fe-4S] cluster content is slightly reduced, no detectable S-adenosylmethionine cleavage, no detectable CPO activity Escherichia coli
E145I appears colorless, the [4Fe-4S] cluster content is slightly reduced, no detectable S-adenosylmethionine cleavage, no detectable CPO activity Escherichia coli
F310A is slightly yellow, the [4Fe-4S] cluster content is slightly reduced, cleaves only one S-adenosylmethionine molecule per molecule protein, residual CPO activity Escherichia coli
F310L is slightly yellow, the [4Fe-4S] cluster content is slightly reduced, cleaves only one S-adenosylmethionine molecule per molecule protein, no detectable CPO activity Escherichia coli
I329A contains the same amount of iron-sulfur cluster as the wild-type HemN, but cleaves only one S-adenosylmethionine molecule per molecule protein, no detectable CPO activity Escherichia coli
I329A exhibits the same yellow-brown color as wild-type HemN, but the [4Fe-4S] cluster content is slightly reduced and cleaves only one S-adenosylmethionine molecule per molecule protein, no detectable CPO activity Escherichia coli
Q311A contains the same amount of iron-sulfur cluster as the wild-type HemN, but cleaves only one S-adenosylmethionine molecule per molecule protein, no detectable CPO activity Escherichia coli
Q311A exhibits the same yellow-brown color as wild-type HemN, but the [4Fe-4S] cluster content is slightly reduced and cleaves only one S-adenosylmethionine molecule per molecule protein, no detectable CPO activity Escherichia coli
Y56A appears colorless, the [4Fe-4S] cluster content is slightly reduced, no detectable S-adenosylmethionine cleavage, no detectable CPO activity Escherichia coli
Y56L appears colorless, the [4Fe-4S] cluster content is slightly reduced, no detectable S-adenosylmethionine cleavage, no detectable CPO activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by affinity chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
coproporphyrinogen-III + S-adenosyl-L-methionine
-
 Escherichia coli protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
-
 ?

Synonyms

Synonyms Comment Organism
HemN
-
 Escherichia coli
oxygen-independent coproporphyrinogen III oxidase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine cosubstrate of coproporphyrinogen-III Escherichia coli