3UCC

Asymmetric complex of human neuron specific enolase-1-PGA/PEP

3UCC の概要

• エントリーDOI: 10.2210/pdb3ucc/pdb
• 関連するPDBエントリー: 1TE6 2AKM 2AKZ 3UCD
• 分子名称: Gamma-enolase, MAGNESIUM ION, 2-PHOSPHOGLYCERIC ACID, ... (5 entities in total)
• 機能のキーワード: lyase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : P09104
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96625.66

構造登録者

Qin, J.,Chai, G.,Brewer, J.,Lovelace, L.,Lebioda, L. (登録日: 2011-10-26, 公開日: 2012-08-22, 最終更新日: 2023-09-13)

主引用文献

Qin, J.,Chai, G.,Brewer, J.M.,Lovelace, L.L.,Lebioda, L.
Structures of asymmetric complexes of human neuron specific enolase with resolved substrate and product and an analogous complex with two inhibitors indicate subunit interaction and inhibitor cooperativity.
J.Inorg.Biochem., 111:187-194, 2012

PubMed Abstract: In the presence of magnesium, enolase catalyzes the dehydration of 2-phospho-d-glycerate (PGA) to phosphoenolpyruvate (PEP) in glycolysis and the reverse reaction in gluconeogensis at comparable rates. The structure of human neuron specific enolase (hNSE) crystals soaked in PGA showed that the enzyme is active in the crystals and produced PEP; conversely soaking in PEP produced PGA. Moreover, the hNSE dimer contains PGA bound in one subunit and PEP or a mixture of PEP and PGA in the other. Crystals soaked in a mixture of competitive inhibitors tartronate semialdehyde phosphate (TSP) and lactic acid phosphate (LAP) showed asymmetry with TSP binding in the same site as PGA and LAP in the PEP site. Kinetic studies showed that the inhibition of NSE by mixtures of TSP and LAP is stronger than predicted for independently acting inhibitors. This indicates that in some cases inhibition of homodimeric enzymes by mixtures of inhibitors ("heteroinhibition") may offer advantages over single inhibitors.

PubMed: 22437160
DOI: 10.1016/j.jinorgbio.2012.02.011

実験手法

X-RAY DIFFRACTION (1.5 Å)