4Z17

Thermostable enolase from Chloroflexus aurantiacus

4Z17 の概要

• エントリーDOI: 10.2210/pdb4z17/pdb
• 関連するPDBエントリー: 4YWS 4Z1Y
• 分子名称: Enolase, MAGNESIUM ION, PHOSPHOENOLPYRUVATE, ... (4 entities in total)
• 機能のキーワード: enolase, thermostability, thermophilic origin, phylogeny, lyase
• 由来する生物種: Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92325.03

構造登録者

Zadvornyy, O.A.,Peters, J.W. (登録日: 2015-03-26, 公開日: 2015-07-01, 最終更新日: 2023-09-27)

主引用文献

Zadvornyy, O.A.,Boyd, E.S.,Posewitz, M.C.,Zorin, N.A.,Peters, J.W.
Biochemical and Structural Characterization of Enolase from Chloroflexus aurantiacus: Evidence for a Thermophilic Origin.
Front Bioeng Biotechnol, 3:74-74, 2015

PubMed Abstract: Enolase catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate during both glycolysis and gluconeogenesis, and is required by all three domains of life. Here, we report the purification and biochemical and structural characterization of enolase from Chloroflexus aurantiacus, a thermophilic anoxygenic phototroph affiliated with the green non-sulfur bacteria. The protein was purified as a homodimer with a subunit molecular weight of 46 kDa. The temperature optimum for enolase catalysis was 80°C, close to the measured thermal stability of the protein which was determined to be 75°C, while the pH optimum for enzyme activity was 6.5. The specific activities of purified enolase determined at 25 and 80°C were 147 and 300 U mg(-1) of protein, respectively. K m values for the 2-phosphoglycerate/phosphoenolpyruvate reaction determined at 25 and 80°C were 0.16 and 0.03 mM, respectively. The K m values for Mg(2+) binding at these temperatures were 2.5 and 1.9 mM, respectively. When compared to enolase from mesophiles, the biochemical and structural properties of enolase from C. aurantiacus are consistent with this being thermally adapted. These data are consistent with the results of our phylogenetic analysis of enolase, which reveal that enolase has a thermophilic origin.

PubMed: 26082925
DOI: 10.3389/fbioe.2015.00074

実験手法

X-RAY DIFFRACTION (2.65 Å)