The 2.1 Å structure of Aerococcus viridans L-lactate oxidase (LOX)

被引：42

作者：

Leiros, Ingar

Wang, Ellen

Rasmussen, Tonni

Oksanen, Esko

Repo, Heidi

Petersen, Steffen B.

Heikinheimo, Pirkko

Hough, Edward ^{[1
]}

机构：

[1] Univ Tromso, Inst Kjemi, N-9037 Tromso, Norway

[2] Univ Tromso, NorStruct, N-9037 Tromso, Norway

[3] Univ Aalborg, Dept Phys & Nanotechnol, DK-9220 Aalborg, Denmark

[4] Univ Helsinki, Inst Biotechnol, FIN-00014 Helsinki, Finland

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2006年 / 62卷

关键词：

D O I：

10.1107/S1744309106044678

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The crystal structure of L-lactate oxidase (LOX) from Aerococcus viridans has been determined at 2.1 angstrom resolution. LOX catalyzes the flavin mononucleotide (FMN) dependent oxidation of lactate to pyruvate and hydrogen peroxide. LOX belongs to the alpha-hydroxy-acid oxidase flavoenzyme family; members of which bind similar substrates and to some extent have conserved catalytic properties and structural motifs. LOX crystallized as two tightly packed tetramers in the asymmetric unit, each having fourfold symmetry. The present structure shows a conserved FMN coordination, but also reveals novel residues involved in substrate binding compared with other family members.

引用

页码：1185 / 1190

页数：6

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