Steady-state and pre-steady-state kinetic analysis of Mycobacterium smegmatis cysteine ligase (MshC)

Keyphrases

• Steady State 100%
• Cysteine 100%
• Steady-state Kinetics 100%
• Mycobacterium Smegmatis 100%
• Ligase 100%
• MshC 100%
• Steady-state Kinetic Analysis 100%
• Oxidative Stress 20%
• Kcat 20%
• Inhibition Constant 20%
• ATP Binding 20%
• Mycobacterium Tuberculosis (M. tb) 20%
• Cell Growth 20%
• Kinetic Parameters 20%
• Inhibitor Design 20%
• Adenosine 20%
• Substrate Analog 20%
• Kinetic Mechanism 20%
• Condensation 20%
• Competitive Inhibition 20%
• Biosynthetic Pathway 20%
• Acetylation 20%
• ATP-dependent 20%
• Actinomycetes 20%
• D-glucopyranosides 20%
• Rapid Quench 20%
• Pre-steady State 20%
• Km Value 20%
• Single Turnover 20%
• Adenylates 20%
• Half Reaction 20%
• Initial Velocity Studies 20%
• Inhibition Studies 20%
• Mycothiol 20%
• Kinetic Characterization 20%
• Mechanistic Characterization 20%
• Biosynthetic Enzymes 20%
• Ping-pong Effect 20%
• Amido 20%
• Antibiotic Stress 20%
• MshA 20%
• Steady State Approach 20%
• Non-competitive Inhibition 20%

Biochemistry, Genetics and Molecular Biology

• Adenosine Triphosphate 100%
• Steady State 100%
• Mycobacterium Smegmatis 100%
• Ligase 100%
• Cysteine 100%
• Melanocyte-Stimulating Hormone 60%
• Enzyme 40%
• Anabolism 40%
• Adenosine Monophosphate 40%
• Competitive Inhibition 20%
• Turnover Number 20%
• Cell Growth 20%
• Kinetic Parameter 20%
• Mycobacterium Tuberculosis 20%
• Enzyme Kinetics 20%
• Actinobacteria 20%
• Mycothiol 20%
• Adenosine 20%