適合運動は,関連するタンパク質チロシンフォスファタゼにおけるフォスフォリル伝搬を調節する
Sean K Whittier1, Alvan C Hengge, J Patrick Loria
1Department of Molecular Biophysics and Biochemistry, Yale University, 260 Whitney Avenue, New Haven, CT 06520, USA.
Science (New York, N.Y.)
|August 24, 2013
まとめ
タンパク質チロシンフォスファタゼ (PTP) の活性部位のループ閉塞は,触媒速度に直接影響する. 化学反応に不可欠なこの形状の変化は,YopHのようなPTPとPTP1B.のようなPTPの運動的差異を説明する.
科学分野:
- バイオケミストリー バイオケミストリー
- 酵素学 酵素学とは
- 構造生物学 構造生物学とは
背景:
- 酵素における適合運動は,基質結合と産物放出に影響することが知られている.
- 化学反応のステップ内におけるこれらの運動の直接的な役割は,タンパク質チロシンフォスファタゼ (PTPs) についてほとんど説明されていないままである.
研究 の 目的:
- PTPの触媒機構におけるアクティブサイトループ運動の役割を調査する.
- ループ閉塞の運動学と,異なるPTPにおける化学反応速度を相関させる.
主な方法:
- 核磁共振 (NMR) 光譜を用いて,アクティブサイトのループダイナミクスを監視した.
- 2つの異なるPTP:YopHとPTP1B.B.の触媒速度とループ閉鎖運動を比較しました.
主要な成果:
- YopHとPTP1Bの両方の活性部位のループ閉塞は,それらのフォスフォチロジン分裂動態を反映した速度で起こることが観察されました.
- アクティブサイトループには,触媒分解に不可欠な触媒酸残留物が含まれていることが判明しました.
結論:
- アクティブサイトループの閉塞は,基板結合または製品放出だけでなく,PTPの化学反応ステップと密接に関連しています.
- 触媒酸から陽子移転を含むループ閉鎖の速度は,YopHとPTP1Bの異なる触媒効率を説明します.
関連する概念動画
01:02Phosphorylation
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
01:02Phosphorylation
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
02:54Protein Kinases and Phosphatases
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...
02:54Protein Kinases and Phosphatases
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...
02:04Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
02:04Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.