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Literature summary extracted from

  • Zhang, L.; Xie, Z.; Liu, Z.; Zhou, S.; Ma, L.; Liu, W.; Huang, J.; Ko, T.; Li, X.; Hu, Y.; Min, J.; Yu, X.; Guo, R.; Chen, C.
    Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase (2020), Nat. Commun., 11, 2676 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.14.1 structure of full-length CYP116B46. The continuous polypeptide chain comprises three functional domains, which align with the direction of electrons traveling from FMN to the heme through the [2Fe-2S] cluster. FMN and the [2Fe-2S] cluster are positioned closely, which facilitates efficient electron shuttling. The edge-to-edge straight-line distance between the [2Fe-2S] cluster and heme is approx. 25.3 A Tepidiphilus thermophilus

Protein Variants

EC Number Protein Variants Comment Organism
1.14.14.1 E723A residue located between [2Fe-2S] cluster and heme, about 15% of wild-type activity Tepidiphilus thermophilus
1.14.14.1 E729A residue located between [2Fe-2S] cluster and heme, no activity detecable Tepidiphilus thermophilus
1.14.14.1 F378A residue located between [2Fe-2S] cluster and heme, no activity detecable Tepidiphilus thermophilus
1.14.14.1 Q725A residue located between [2Fe-2S] cluster and heme, about 100% of wild-type activity Tepidiphilus thermophilus
1.14.14.1 R388A residue located between [2Fe-2S] cluster and heme, no activity detecable Tepidiphilus thermophilus
1.14.14.1 R392A residue located between [2Fe-2S] cluster and heme, about 110% of wild-type activity Tepidiphilus thermophilus
1.14.14.1 R718A residue located between [2Fe-2S] cluster and heme, no activity detecable Tepidiphilus thermophilus
1.14.14.1 S726A residue located between [2Fe-2S] cluster and heme, about 30% of wild-type activity Tepidiphilus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.1 Tepidiphilus thermophilus A0A0K6ITW2
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.1 decanoic acid + [reduced NADPH-hemoprotein reductase] + O2
-
 Tepidiphilus thermophilus ? + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.14.1 CYP116B46
-
 Tepidiphilus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.1 heme
-
 Tepidiphilus thermophilus
1.14.14.1 [2Fe-2S]-center
-
 Tepidiphilus thermophilus