Properties of S-adenosyl-L-methionine-magnesium-protoporphyrin IX methyltransferase from barley

スポンサーリンク

概要

• 論文の詳細を見る

• S-Adenosyl-L-methionine-magnesium-protoporphyrin IX methyltransferase (EC 2.1.1.11) is present in greening barley seedlings associated with the particulate fraction. This enzyme was purified 20 fold using protamine and ammonium sulfate precipitation. The enzyme was active over a wide pH range with highest activity at pH 7.5. The Km values for Mg-protoporphyrin IX and S-adenosylmethionine were 48 and 39 μM, respectively; S-adenosylethionine and S-adenosylhomocysteine were competitive inhibitors with respect to S-adenosylmethionine; hemin inhibition was non-competitive with respect to Mg-protoporphyrin IX; thiol compounds exhibited a stimulatory effect on enzyme activity. The properties of the enzyme are discussed and compared with the enzyme from other organisms.

• 日本植物生理学会の論文

著者

• Miller Gene

  Biology Department Utah State University

• Shieh Jii

  Biology Department, Utah State University

• Psenak Mikulas

  Biology Department, Utah State University

• Shieh Jii

  Biology Department Utah State University:(present)department Of Chemistry Boston University

• Psenak Mikulas

  Biology Department Utah State University:(present)department Of Biochemistry And Microbiology Facult

関連論文

• Light-induced delta-aminolevulinic acid in dark-grown barley seedlings
• Properties of S-adenosyl-L-methionine-magnesium-protoporphyrin IX methyltransferase from barley

スポンサーリンク