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Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.3.98.3 E145A appears colorless, the [4Fe-4S] cluster content is slightly reduced, no detectable S-adenosylmethionine cleavage, no detectable CPO activity Escherichia coli
1.3.98.3 E145I appears colorless, the [4Fe-4S] cluster content is slightly reduced, no detectable S-adenosylmethionine cleavage, no detectable CPO activity Escherichia coli
1.3.98.3 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
1.3.98.3 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
1.3.98.3 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
1.3.98.3 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
1.3.98.3 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
1.3.98.3 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
1.3.98.3 Y56A appears colorless, the [4Fe-4S] cluster content is slightly reduced, no detectable S-adenosylmethionine cleavage, no detectable CPO activity Escherichia coli
1.3.98.3 Y56L appears colorless, the [4Fe-4S] cluster content is slightly reduced, no detectable S-adenosylmethionine cleavage, no detectable CPO activity Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.3.98.3 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.98.3 by affinity chromatography Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

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