3Q9T

Crystal structure analysis of formate oxidase

Summary for 3Q9T

• Entry DOI: 10.2210/pdb3q9t/pdb
• Descriptor: Choline dehydrogenase and related flavoproteins, [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3S,4S)-5-(8-formyl-7-methyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl)-2,3,4-trihydroxypentyl dihydrogen diphosphate, (4R)-2-METHYLPENTANE-2,4-DIOL, ... (7 entities in total)
• Functional Keywords: glucose-methanol-choline oxidoreductase family, formate oxidase, 8-formyl-fad, oxidoreductase
• Biological source: Aspergillus oryzae
• Total number of polymer chains: 3
• Total formula weight: 195868.55

Authors

Doubayashi, D.,Ootake, T.,Maeda, Y.,Oki, M.,Tokunaga, Y.,Sakurai, A.,Nagaosa, Y.,Mikami, B.,Uchida, H. (deposition date: 2011-01-09, release date: 2011-09-21, Last modification date: 2023-11-01)

Primary citation

Doubayashi, D.,Ootake, T.,Maeda, Y.,Oki, M.,Tokunaga, Y.,Sakurai, A.,Nagaosa, Y.,Mikami, B.,Uchida, H.
Formate oxidase, an enzyme of the glucose-methanol-choline oxidoreductase family, has a His-Arg pair and 8-formyl-FAD at the catalytic site.
Biosci.Biotechnol.Biochem., 75:1662-1667, 2011

PubMed Abstract: Formate oxidase of Aspergillus oryzae RIB40 contains an 8-replaced FAD with molecular mass of 799 as cofactor. The ¹H-NMR spectrum of the cofactor fraction obtained from the enzyme indicated that the 8-replaced FAD in the fraction was 8-formyl-FAD, present in open form and hemiacetal form. The oxidation-reduction potentials of the open and hemiacetal forms were estimated by cyclic voltammetry to be -47 and -177 mV vs. Normal Hydrogen Electrode respectively. The structure of the enzyme was constructed using diffraction data to 2.24 Å resolution collected from a crystal of the enzyme. His₅₁₁ and Arg₅₅₄ were situated close to the pyrimidine part of the isoalloxazine ring of 8-formyl-FAD in open form. The enzyme had 8-formyl-FAD, the oxidation potential of which was approximately 160 mV more positive than that of FAD, and the His-Arg pair at the catalytic site, unlike the other enzymes belonging to the glucose-methanol-choline oxidoreductase family.

PubMed: 21897046
DOI: 10.1271/bbb.110153

Experimental method

X-RAY DIFFRACTION (2.24 Å)