arginine and menaquinone 6

arginine has been researched along with menaquinone 6 in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	2 (100.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Evans, CE; French, JB; Lavaud, LJ; Matarlo, JS; Ngo, SC; Rajashankar, KR; Sharma, I; Shek, R; Tan, DS; Tonge, PJ	1
Chen, Y; Dai, X; Guo, Z; Qin, M; Song, H	1

Other Studies

2 other study(ies) available for arginine and menaquinone 6

Article	Year
Mechanism of MenE inhibition by acyl-adenylate analogues and discovery of novel antibacterial agents. Biochemistry, 2015, 10-27, Volume: 54, Issue:42 Topics: Amino Acid Sequence; Animals; Anti-Bacterial Agents; Arginine; Catalytic Domain; Chlorocebus aethiops; Conserved Sequence; Crystallography, X-Ray; Drug Discovery; Escherichia coli K12; Escherichia coli Proteins; Microbial Sensitivity Tests; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenylbutyrates; Protein Conformation; Sequence Homology, Amino Acid; Staphylococcus aureus; Structure-Activity Relationship; Succinate-CoA Ligases; Vero Cells; Vitamin K 2	2015
Two active site arginines are critical determinants of substrate binding and catalysis in MenD: a thiamine-dependent enzyme in menaquinone biosynthesis. The Biochemical journal, 2018, 11-30, Volume: 475, Issue:22 Topics: Arginine; Biocatalysis; Catalytic Domain; Crystallography, X-Ray; Escherichia coli Proteins; Kinetics; Molecular Docking Simulation; Mutagenesis, Site-Directed; Mutation, Missense; Protein Binding; Protein Conformation; Pyruvate Oxidase; Substrate Specificity; Thiamine; Thiamine Pyrophosphate; Vitamin K 2	2018

Article

Year

Mechanism of MenE inhibition by acyl-adenylate analogues and discovery of novel antibacterial agents.

Biochemistry, 2015, 10-27, Volume: 54, Issue:42

Topics: Amino Acid Sequence; Animals; Anti-Bacterial Agents; Arginine; Catalytic Domain; Chlorocebus aethiops; Conserved Sequence; Crystallography, X-Ray; Drug Discovery; Escherichia coli K12; Escherichia coli Proteins; Microbial Sensitivity Tests; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenylbutyrates; Protein Conformation; Sequence Homology, Amino Acid; Staphylococcus aureus; Structure-Activity Relationship; Succinate-CoA Ligases; Vero Cells; Vitamin K 2

2015

Two active site arginines are critical determinants of substrate binding and catalysis in MenD: a thiamine-dependent enzyme in menaquinone biosynthesis.

The Biochemical journal, 2018, 11-30, Volume: 475, Issue:22

Topics: Arginine; Biocatalysis; Catalytic Domain; Crystallography, X-Ray; Escherichia coli Proteins; Kinetics; Molecular Docking Simulation; Mutagenesis, Site-Directed; Mutation, Missense; Protein Binding; Protein Conformation; Pyruvate Oxidase; Substrate Specificity; Thiamine; Thiamine Pyrophosphate; Vitamin K 2

2018