p-Hydroxybenzoate Hydroxylase from Pseudomonas desmolytica : Relative Molecular Mass, Amino Acid Composition, and Reactivity of Sulfhydryl Groups(Biological Chemistry)
スポンサーリンク
概要
- 論文の詳細を見る
The relative molecular mass (M_r) of p-hydroxybenzoate hydroxylase from Pseudomonas desmolytica was measured by SDS-PAGE and gel filtration. The enzyme was a dimer of identical subunits with M_r of 44,000 and with one mole of FAD per subunit. The isoelectric point was 4.9. The amino acid composition was also identified. The enzyme contained 6 sulfhydryl groups per FAD. Modification of the groups with p-chloromercuribenzoate accompanied inactivation which obeyed a biphasic kinetics. The faster reaction corresponded to 80% of the total inactivation. p-Hydroxybenzoate and chloride ion (an inhibitor with respect to NADPH) increased the rate of the faster inactivation reaction, but NADPH had a protective effect. p-Hydroxybenzoate markedly restricted the amount of sulfhydryl groups reactive to p-chloromercuribenzoate. The fast phase inactivation could be ascribed to modification of a single sulfhydryl group. The results are highly indicative of the existence of a sulfhydryl group in the NADPH-binding site.
- 社団法人日本農芸化学会の論文
- 1990-02-23
著者
-
SHOUN Hirofumi
Institute of Applied Biochemistry, University of Tsukuba
-
Shoun Hirofumi
Institute Of Applied Biochemistry University Of Tsukuba
関連論文
- A Novel C1-Using Denitrifier Alcaligenes sp. STC1 and Its Genes for Copper-containing Nitrite Reductase and Azurin
- Unique Nitrate/Nitrite-inducible Cytochrome P-450 in Fusarium oxysporum and Related Fungal Species(Microbiology & Fermentation Industry)
- Diauxic Growth of Fusarium oxysporum during Aerobic Culture in the Presence of Nitrate/Nitrite
- p-Hydroxybenzoate Hydroxylase from Pseudomonas desmolytica : Relative Molecular Mass, Amino Acid Composition, and Reactivity of Sulfhydryl Groups(Biological Chemistry)
- Purification and Characterization of an Intracellular α-D-Xylosidase from Penicillium wortmannii IFO 7237
- Involvement of Formate as an Intespecies Electron Carrier in a Syntrophic Acetate-Oxidizing Anaerobic Microorganism in Coculture with Methanogens
- Levoglucosan Dehydrogenase Involved in the Assimilation of Levoglucosan in Arthrobacter sp. I-552
- N-Terminal Processing and Amino Acid Sequence of Two Isoforms of Nitric Oxide Reductase Cytochrome P450nor from Fusarium oxysporum
- Analysis of NAD(P)H Binding Site of Cytochrome P450nor
- Cytochrome P450foxy, a Catalytically Self-Sufficient Fatty Acid Hydroxylase of the Fungus Fusarium oxysporum^1
- N-Terminal Processing and Amino Acid Sequence of Two Isoforms of Nitric Oxide Reductase Cytochrome P450nor from Fusarium oxysporum.