Practical Investigations and Enzyme Helpers
When investigating enzyme activity experimentally, precision matters! You'll need to control temperature using a thermostatic water bath, maintain pH with buffer solutions, and ensure reliability by repeating tests multiple times and calculating means.
Your control experiment should omit the enzyme entirely - this proves that no reaction occurs without the catalyst present. Don't forget to stir solutions regularly for even distribution and consider what level of precision is appropriate for your measurements.
Coenzymes and cofactors act as enzyme helpers, though they work differently. Coenzymes are larger organic molecules (often made from B vitamins) that transfer substances between enzymes - like coenzyme A in respiration and NAD in hydrogen transport.
Cofactors are inorganic metal ions that bind to active sites, making enzyme-substrate complex formation quicker and easier. Examples include chloride ions in amylase and zinc ions in carbonic anhydrase.
Competitive inhibitors are the troublemakers of enzyme chemistry! These molecules have similar shapes to the natural substrate and compete for the same active site, reducing reaction rates by blocking substrate access.
Quick Check: The amount of competitive inhibition depends on the relative concentrations of inhibitor versus substrate - more inhibitor means more blocked active sites!