Purification and characteristics of a novel cytochrome c dependent glyoxylate dehydrogenase from a wood‐destroying fungus Tyromyces palustris

FEBS Letters

Shimada, Mikio¹  Hattori, Takefumi¹  Tokimatsu, Toshiaki¹  Nagai, Yuko¹ 

[1] Wood Research Institute, Kyoto University, Uji, Kyoto 611-0011, Japan

关键词: Glyoxylate dehydrogenase (cytochrome);    Oxalic acid;    Wood-rotting fungus;    Flavohemoprotein;    Glyoxylate metabolism;   

DOI  :  10.1016/S0014-5793(98)01104-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A new glyoxylate dehydrogenase which catalyzes dehydrogenation of glyoxylate to oxalate in the presence of cytochrome c has been purified as an electrophoretically homogeneous protein from the cell-free extracts of a wood-destroying basidiomycete Tyromyces palustris. The enzymatic reduction of cytochrome c was dependent on glyoxylate which was found to be the best substrate among the compounds tested. The K _m value for glyoxylate was determined to be 2.7 mM at the optimal pH (8.0). The UV-visible spectra of the enzyme in oxidized and reduced forms indicate that the enzyme belongs to a family of flavohemoproteins. The flavin nucleotide isolated from the native enzyme by heat denaturation was identified as FMN. The enzyme (M _r 331 000) consists of six identical homopolymers (M _r of subunit 59 000), which were found to constitute a symmetric octahedral shape by electron-microscopic observation with a negative staining method.

【 授权许可】

Unknown