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Plant and Cell Physiology, 1986, Vol. 27, No. 1 67-74
© 1986

Article

Purification and Characterization of 4,5-Dioxovalerate Reductase (NADPH) from Chlorella regularis

Yuzo Shioi, Michio Doi and Tsutomu Sasa

Division of Biology, Miyazaki Medical College Kiyotake, Miyazaki 889-16, Japan

Two types of 4,5-dioxovalerate reductases (NADPH) were partially purified and characterized from green alga, Chlorella regularis. The enzyme was separated by DEAE-Sephacel chromatography into two peaks: type I (first peak) and type II (second peak). The activity ratio of the type II to type I enzyme varied between 5 to 7 with a starting cell material. Both enzymes had the same pH optimum at 6.0 and pI value of 4.9. The molecular weight estimated by gel filtration was 33,000 for type I and 99,000 for type II enzyme. Both enzymes used only NADPH, but were not specific for 4,5-dioxovaleric acid (DOVA). Type I enzyme reduced glyoxylate 68-fold faster than DOVA, whereas type II enzyme acted more specifically on a variety of aldehydes than DOVA. It is suggested that these enzymes may not function primarily as NADPH-DOVA reductases in the metabolic pathway of DOVA.

(Received June 15, 1985; Accepted October 14, 1985)
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