Determination of phosphorylated amino acid residues of Rab8 fromBombyx mori

2007 ◽  
Vol 66 (2) ◽  
pp. 89-97 ◽  
Author(s):  
Tomohide Uno ◽  
Takuya Nakada ◽  
Sota Okamaoto ◽  
Masahiko Nakamura ◽  
Mamoru Matsubara ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Phosphorylated Amino Acid

Determination of Amino Acid Residues Responsible for Specific Interaction of Protein Kinases with Small Molecule Inhibitors

2018 ◽  
Vol 52 (3) ◽  
pp. 478-487 ◽  
Author(s):  
D. A. Karasev ◽  
A. V. Veselovsky ◽  
A. A. Lagunin ◽  
D. A. Filimonov ◽  
B. N. Sobolev
Keyword(s):  
Amino Acid ◽  
Protein Kinases ◽  
Small Molecule ◽  
Small Molecule Inhibitors ◽  
Specific Interaction ◽  
Amino Acid Residues

scholarly journals Establishment of a Two-Dimensional HPLC-MS/MS Method Combined with DCl/D2O Hydrolysis for the Determination of Trace Amounts of D-Amino Acid Residues in Proteins

2015 ◽  
Vol 36 (2) ◽  
pp. 45-50 ◽  
Author(s):  
Shoto ISHIGO ◽  
Eiichi NEGISHI ◽  
Yurika MIYOSHI ◽  
Hirohisa ONIGAHARA ◽  
Masashi MITA ◽  
...  
Keyword(s):  
Amino Acid ◽  
Two Dimensional ◽  
Amino Acid Residues

Rapid Spectrophotometric Determination of Hypothermia Protection Activity of Sericin Peptides on Lactobacillus bulgaricus

2013 ◽  
Vol 634-638 ◽  
pp. 1287-1293
Author(s):  
Yan Fu Zhou ◽  
Jin Hong Wu ◽  
Shao Yun Wang ◽  
Xiao Qing Guo ◽  
Zheng Wu Wang
Keyword(s):  
Amino Acid ◽  
Survival Rate ◽  
Spectrophotometric Method ◽  
Lactobacillus Bulgaricus ◽  
Freezing Stress ◽  
Amino Acid Residues ◽  
Protection Effect ◽  
Hydrophilic Amino Acid ◽  
Protection Activity

Sericin peptides have a high proportion of hydrophilic amino acid residues, which are considered to protect cells from freezing stress due to the maintenance of water in the cells. In this paper, the hypothermia protection effect of sericin peptides was studied by reading optical density of cells at 600 nm, which was detailedly optimized to be a direct and practical spectrophotometric method. The survival rate of Lactobacillus bulgaricus after frozen storaged with addition of 0.1 mg/mL sericin peptides was close to that of 10% (v/v) glycerol (p > 0.05). The survival rate of 5 mg/mL sericin peptides was up to 64.17%.

Studies on determination of active site amino acid residues in glyoxylate synthetase from potato tuber chloroplasts

1999 ◽  
Vol 37 (2) ◽  
pp. 121-129 ◽  
Author(s):  
Machhindra T. Janave ◽  
N.Krishnan Ramaswamy ◽  
P.Madhusudanan Nair
Keyword(s):  
Amino Acid ◽  
Potato Tuber ◽  
Active Site ◽  
Amino Acid Residues

scholarly journals Determination of three amino acids causing alteration of proteolytic activities of staphylococcal glutamyl endopeptidases

2009 ◽  
Vol 390 (3) ◽  
Author(s):  
Takayuki K. Nemoto ◽  
Toshio Ono ◽  
Yu Shimoyama ◽  
Shigenobu Kimura ◽  
Yuko Ohara-Nemoto
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protease Activity ◽  
Binding Pocket ◽  
Catalytic Triad ◽  
Amino Acid Residues ◽  
Proteolytic Activities ◽  
Hydrophobic Amino Acids ◽  
The Difference

Abstract Staphylococcus aureus, Staphylococcus epidermidis, and Staphylococcus warneri secrete glutamyl endopeptidases, designated GluV8, GluSE, and GluSW, respectively. The order of their protease activities is GluSE<GluSW<<GluV8. In the present study, we investigated the mechanism that causes these differences. Expression of chimeric proteins between GluV8 and GluSE revealed that the difference is primarily attributed to amino acid residues 170–195, which define the intrinsic protease activity, and additionally to residues 119–169, which affect the proteolytic sensitivity. Among nine substitutions present in residues 170–195 of the three proteases, the substitutions at positions 185, 188, and 189 were responsible for the changes in their activities, and the combination of W185, V188, and P189, which naturally occurs in GluV8, exerts the highest protease activity. W185 and P189 were indispensable for full activity, but V188 could be replaced by hydrophobic amino acids. These three amino acid residues appear to create a substrate-binding pocket together with the catalytic triad and the N-terminal V1, and therefore define the K m values of the proteases. We also describe a method to produce a chimeric form of GluSE and GluV8 that is resistant to proteolysis, and therefore possesses 4-fold higher activity than the wild-type recombinant GluV8.

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