Purification and characterization of 4,5-dioxovalerate reductase (NADPH) from chlorella regularis

Yuzo Shioi, Michio Doi, Tsutomu Sasa

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)67-74
Number of pages8
JournalPlant and Cell Physiology
Volume27
Issue number1
Publication statusPublished - Jan 1986

All Science Journal Classification (ASJC) codes

  • Physiology
  • Plant Science
  • Cell Biology

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