Histidine 210 Mutant of a Trypsin-Type Achromobacter Protease I Shows Broad Optimum pH Range
スポンサーリンク
概要
- 論文の詳細を見る
Achromobacter protease I (API), a lysine-specific serine protease, shows one order of magnitude higher activity than bovine trypsin, while its optimum pH is in the alkaline region at about pH 9. To improve the optimum pH range, mutant enzyme His 210 replaced by Ser (H210S), Ala (H210A), and Lys (H210K) were constructed. The optimum pH of H210S shifted from about pH 9 (wild-type enzyme) to about pH 7, retaining its high activity. The putative electrostatic interaction between His 210 and catalytic Asp 113 was elucidated by the optimum-pH shift of H210K and H210A. These results indicate that this unconserved His 210 in API, which plays a key role in generating the useful peptidase, broadened the optimum-pH range without decreasing lysylendo-peptidase activity.
- 社団法人日本生物工学会の論文
- 2002-03-25
著者
-
Sakiyama F
Osaka Univ. Osaka
-
Sakiyama Fumio
The Institute For Protein Research Osaka University
-
Shiraki K
Institute Of Applied Physics University Of Tsukuba
-
Shiraki Kentaro
The Institute For Protein Research Osaka University
関連論文
- Utilization of Immobilized Archaeal Chaperonin for Enzyme Stabilization
- Biophysical Analysis of Heat-Induced Structural Maturation of Glutamate Dehydrogenase from a Hyperthermophilic Archaeon (ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Mutational Effects on O^6-Methylguanine-DNA Methyltransferase from Hyperthermophile : Contribution of Ion-Pair Network to Protein Thermostability
- Contribution of Protein-Surface Ion Pairs of a Hyperthermophilic Protein on Thermal and Thermodynamic Stability
- Genetic, Enzymatic, and Structural Analyses of Phenylalanyl-tRNA Synthetase from Thermococcus kodakaraensis KOD1
- Biophysical Effect of Amino Acids on the Prevention of Protein Aggregation
- 超好熱菌由来タンパク質のさまざまな変性条件下での構造安定性
- Chelation of cadmium ions by phytochelatin synthas : role of the cystein-rich C-terminal
- Diamines Prevent Thermal Aggregation and Inactivation of Lysozyme(BIOCHEMICAL ENGINEERING)
- Equilibrium and Kinetic Stability of a Hyperthermophilic Protein, O^6-Methylguanine-DNA Methyltransferase under Various Extreme Conditions
- Contribution of an Imidazole-Indole Stack to High Catalytic Potency of a Lysine-Specific Serine Protease, Achromobacter Protease I
- Histidine 210 Mutant of a Trypsin-Type Achromobacter Protease I Shows Broad Optimum pH Range