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Literature summary for 1.14.13.40 extracted from

  • Bergner, T.; Pavkov-Keller, T.; Kreuzer, K.; Kowaliuk, J.; Plank, M.; Runggatscher, K.; Turrini, N.G.; Zucol, B.; Wallner, S.; Faber, K.; Gruber, K.; Macheroux, P.
    Anthranoyl-CoA monooxygenase/reductase from Azoarcus evansii possesses both FMN and FAD in two distinct and independent active sites (2015), Biochim. Biophys. Acta, 1854, 890-896 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 Aromatoleum evansii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
165000
-
-
Aromatoleum evansii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2 Aromatoleum evansii the enzyme participates in a pathway for the degradation of aromatic compounds in Azoarcus evansii 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
-
?

Organism

Organism UniProt Comment Textmining
Aromatoleum evansii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2 the enzyme participates in a pathway for the degradation of aromatic compounds in Azoarcus evansii Aromatoleum evansii 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
-
?
anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2 the enzyme catalyzes the monooxygenation of anthranoyl-CoA to 5-hydroxyl-2-aminobenzoyl-CoA and the subsequent reduction to the dearomatized product 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA. The two reactions occur in separate domains, termed the monooxygenase and reductase domain. Binding studies with 2-aminobenzoyl-CoA and p-hydroxybenzaldehyde as probes for the monooxygenase and reductase domain, respectively, indicate that two functionally distinct and independent active sites exist Aromatoleum evansii 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
-
?

Subunits

Subunits Comment Organism
homodimer it is proposed that the monooxygenase and reductase domain of opposite peptide chains are involved in the transformation of anthranoyl-CoA to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA Aromatoleum evansii

Synonyms

Synonyms Comment Organism
ACMR
-
Aromatoleum evansii
anthranoyl-CoA monooxygenase/reductase
-
Aromatoleum evansii

Cofactor

Cofactor Comment Organism Structure
FAD the monooxygenase domain contains FAD Aromatoleum evansii
FMN the reductase domain utilizes FMN for the reduction of the intermediate 5-hydroxyl-2-aminobenzoyl-CoA Aromatoleum evansii

General Information

General Information Comment Organism
metabolism the enzyme participates in a pathway for the degradation of aromatic compounds in Azoarcus evansii Aromatoleum evansii