リン酸モノエステルダイアニオン水解の競合メカニズム
Fernanda Duarte1, Alexandre Barrozo1, Johan Åqvist1
1Science for Life Laboratory, Department of Cell and Molecular Biology, Uppsala University , BMC Box 596, SE-751 24 Uppsala, Sweden.
Journal of the American Chemical Society
|July 30, 2016
まとめ
リン酸モノエステルの水解機構は,脱出グループに依存する. 良質な離散群は溶媒補助経路を好み 劣質な離散群はメカニズム的曖昧さを生み出し 生物学的触媒に影響を与えます
科学分野:
- 生物化学
- コンピュータ化学
- 物理化学
背景:
- リン酸モノエステルの水解は生物学的システムにおいて極めて重要です.
- メカニズムの詳細,特にグループpKaを離れる役割は不明である.
- これらの反応を理解することで 酵素の触媒と薬剤の設計に役立つのです
研究 の 目的:
- フォスファートモノエステルの水解経路にpKaの離脱が及ぼす影響を調査する.
- 溶媒支援メカニズムと基板支援メカニズムの競争を明らかにする.
- これらの反応のための線形自由エネルギー関係を確立する.
主な方法:
- コンピュータによる電子構造の研究
- メチルリン酸と代用されたアリルリン酸モノエステルの比較分析
- 線形自由エネルギー関係構造
主要な成果:
- 脱水メカニズムは 脱出グループの性質によって決定される.
- 解離剤を助けた解離的な経路を好みます
- 離脱群のpKaの増加は経路エネルギー差を減少させ,弱退群の力学的な曖昧さを引き起こします.
結論:
- 異なった経路を保ちながら 順調に変化します
- 生物学的触媒は,良好な脱出グループを持つ基板支援経路に対してより高い障壁に直面します.
- カタリストの優先順位は 貧困層の優先順位が 消去されたために変化します
関連する概念動画
Hydrolysis of ATP
82.9K
The bonds of adenosine triphosphate (ATP) can be broken through the addition of water, releasing one or two phosphate groups in an exergonic process called hydrolysis. This reaction liberates the energy in the bonds for use in the cell—for instance, to synthesize proteins from amino acids.
If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine...
If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine...
82.9K
Hydrolysis of ATP
8.1K
8.1K
Phosphodiester Linkages
113.4K
Overview
Phosphodiester bond forms when a phosphoric acid molecule (H3PO4) links with two hydroxyl groups (–OH) of two other molecules, forming two ester bonds. Two water molecules are released in this process. The phosphodiester bond is commonly found in nucleic acids (DNA and RNA) and plays a critical role in their structure and function.
Phosphodiester Bonds Link Nucleotides Together
DNA and RNA are polynucleotides or long chains of nucleotides that are linked together. A nucleotide is...
Phosphodiester bond forms when a phosphoric acid molecule (H3PO4) links with two hydroxyl groups (–OH) of two other molecules, forming two ester bonds. Two water molecules are released in this process. The phosphodiester bond is commonly found in nucleic acids (DNA and RNA) and plays a critical role in their structure and function.
Phosphodiester Bonds Link Nucleotides Together
DNA and RNA are polynucleotides or long chains of nucleotides that are linked together. A nucleotide is...
113.4K
Phosphate Buffer
5.9K
The phosphate buffer system is a critical biological mechanism for maintaining pH stability in the body. This system operates primarily through two components: sodium dihydrogen phosphate (NaH2PO4), which acts as a weak acid, and sodium hydrogen phosphate (Na2HPO4), which serves as a weak base.
Sodium dihydrogen phosphate does not fully dissociate in neutral or acidic solutions. When a strong base, such as sodium hydroxide (NaOH), is introduced into the solution, sodium dihydrogen phosphate...
Sodium dihydrogen phosphate does not fully dissociate in neutral or acidic solutions. When a strong base, such as sodium hydroxide (NaOH), is introduced into the solution, sodium dihydrogen phosphate...
5.9K
Protein Kinases and Phosphatases
15.4K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
15.4K
ATP Driven Pumps I: An Overview
10.3K
ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and...
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and...
10.3K


