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Literature summary extracted from

  • Coyle, C.M.; Cheng, J.Z.; OConnor, S.E.; Panaccione, D.G.
    An old yellow enzyme gene controls the branch point between Aspergillus fumigatus and Claviceps purpurea ergot alkaloid pathways (2010), Appl. Environ. Microbiol., 76, 3898-3903.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.99.1 expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) Trypanosoma cruzi

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.6.99.1 purified enzyme, hanging drop vapor diffusion method, mixing of 0.002 ml of protein solution containing 14 mg/mL in 25 mM Tris-HCl, pH 8.0, containing 100 mM NaCl, and 1 mM 2-mercaptoethanol, with 0002 ml of 28% w/v PEG 1500, and 0.3 M ammonium fluoride, equilibration against 0.5 ml of reservoir solution, 19°C, 10 days, crystalline forms I and II, X-ray diffraction structure determination and analysis at 1.27 A and 2.0 A resolution, respectively Trypanosoma cruzi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.6.99.1 additional information Trypanosoma cruzi analysis of binding mode of beta-lapachone, a trypanocidal agent, and other naphthoquinones by molecular docking and dynamics: their binding to TcOYE is stabilized mainly by interactions with the isoalloxazine ring from FMN and residues from the active-site pocket ?
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?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.100 Aspergillus fumigatus
-
-
-
1.3.1.100 Aspergillus fumigatus FGSC A1141
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-
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1.6.99.1 Trypanosoma cruzi Q2TJB8
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-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.99.1 recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography Trypanosoma cruzi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.99.1 additional information analysis of binding mode of beta-lapachone, a trypanocidal agent, and other naphthoquinones by molecular docking and dynamics: their binding to TcOYE is stabilized mainly by interactions with the isoalloxazine ring from FMN and residues from the active-site pocket Trypanosoma cruzi ?
-
?

Subunits

EC Number Subunits Comment Organism
1.6.99.1 monomer TcOYE behaves as a globular monomer in solution Trypanosoma cruzi

Synonyms

EC Number Synonyms Comment Organism
1.3.1.100 EasA
-
Aspergillus fumigatus
1.6.99.1 old yellow enzyme
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Trypanosoma cruzi
1.6.99.1 OYE
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Trypanosoma cruzi

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.100 NADP+
-
Aspergillus fumigatus
1.6.99.1 FMN prosthetic group, detailed binding mode, overview. TcOYE displays a canonical (alpha/bet)8-barrel fold with a FMN prosthetic group located at the large active-site cavity Trypanosoma cruzi

General Information

EC Number General Information Comment Organism
1.3.1.100 malfunction disruption of the easA gene leads to accumulation of chanoclavine-I and chanoclavine-I-aldehyde Aspergillus fumigatus
1.3.1.100 metabolism the enzyme is required for incorporation of chanoclavine-I-aldehyde into more-complex ergot alkaloids, presumably by reducing the double bond conjugated to the aldehyde group, thus facilitating ring closure Aspergillus fumigatus
1.6.99.1 additional information the enzyme shows a classical (alpha/beta)8 fold with the FMN prosthetic group buried at the positively-charged active-site cleft. In solution, TcOYE behaves as a globular monomer, but it exhibits a molecular envelope larger than that observed in the crystal structure, suggesting intrinsic protein flexibility. TcOYE also possesses characteristic extra barrel elements, including (i) the N-terminal beta-hairpin (residues 10-19) that closes the bottom of the barrel, (ii) the capping subdomain (105-164), which participates in the formation of the large active-site pocket, (iii) the alpha-helical motif (196-222) related to substrate recognition, and (iv) the inner allpha-helix (336-341) that contributes to FMN binding Trypanosoma cruzi
1.6.99.1 physiological function the enzyme is clinically relevant due to its role in the action mechanism of some trypanocidal drugs used in the treatment of Chagas' disease by producing reactive oxygen species Trypanosoma cruzi