1AN9

D-AMINO ACID OXIDASE COMPLEX WITH O-AMINOBENZOATE

Summary for 1AN9

• Entry DOI: 10.2210/pdb1an9/pdb
• Descriptor: D-AMINO ACID OXIDASE, FLAVIN-ADENINE DINUCLEOTIDE, 2-AMINOBENZOIC ACID, ... (4 entities in total)
• Functional Keywords: fad, oxidase, d-amino acid, oxidoreductase, flavoprotein
• Biological source: Sus scrofa (pig)
• Cellular location: Peroxisome: P00371
• Total number of polymer chains: 2
• Total formula weight: 79071.18

Authors

Miura, R.,Setoyama, C.,Nishina, Y.,Shiga, K.,Mizutani, H.,Miyahara, I.,Hirotsu, K. (deposition date: 1997-06-28, release date: 1997-11-12, Last modification date: 2023-11-15)

Primary citation

Miura, R.,Setoyama, C.,Nishina, Y.,Shiga, K.,Mizutani, H.,Miyahara, I.,Hirotsu, K.
Structural and mechanistic studies on D-amino acid oxidase x substrate complex: implications of the crystal structure of enzyme x substrate analog complex.
J.Biochem.(Tokyo), 122:825-833, 1997

PubMed Abstract: As an extension of our recent X-ray crystallographic determination of the tertiary structure of D-amino acid oxidase (DAO) [Mizutani, H. et al. (1996) J. Biochem. 120, 14-17], we solved the crystal structure of the complex of DAO with a substrate analog, o-aminobenzoate (OAB). The alignment between flavin and OAB in the crystal structure of the complex is consistent with charge-transfer interaction through the overlap between the highest occupied molecular orbital of OAB and the lowest unoccupied molecular orbital of flavin. Starting with the atomic coordinates of this complex as the initial model, we carried out molecular mechanics simulation for the DAO-D-leucine complex and thus obtained a model for the enzyme-substrate complex. According to the enzyme-substrate complex model, the alpha-proton is pointed toward N(5) of flavin while the lone-pair of the substrate amino group can approach C(4a) of flavin within an interacting distance. This model as well as DAO-OAB complex enables the evaluation of the substrate-flavin interaction prior to electron transfer from the substrate to flavin and provides two possible mechanisms for the reductive-half reaction of DAO, i.e., the electron-proton-electron transfer mechanism and the ionic mechanism.

PubMed: 9399588

Experimental method

X-RAY DIFFRACTION (2.5 Å)