Question

Question 1:

What is lactated dehydrogenase, and how is it used in the reduction of carbonyl groups?

Explain the manner in which the isoenzymes of LDH can be used as diagnostic tools.

Choose one other diagnostic test not using LDH isoenzymes that might be used for the same application and explain what advantages and disadvantages exist over using LDH isoenzymes.

*type please i have bad vision

Answer 1

1. Lactate dehydrogenase (also known as lactic acid dehydrogenase or LDH) is an enzyme found in nearly every body tissue. The mechanism by which glucose (sugar) from food is converted into usable energy for our cells, also known as cellular respiration; it plays an important role in this.

By using NAD+ as a coenzyme, L-lactate dehydrogenase oxidizes L-lactate's reversible reaction to pyruvate. The class of alcohol becomes the enzyme's carbonyl group. The coenzyme binds L-lactate or pyruvate to the enzyme. The coenzyme therefore always binds first on the enzyme. Certain substrates can also bind to the enzyme. For the role it plays in glycolysis, lactate dehydrogenase is particularly important. NAD+ must be sufficient for glycolysis to occur.Under anaerobic conditions, there is not enough NAD+ available for glycolysis because everything is trapped in the form of NADH (the insufficient amount of oxygen means that there is no oxygen to obtain electrons from the end of the electron transport chain). Lactate dehydrogenase allows glycolysis to occur by helping to transform NADH to NAD+. This is achieved by converting pyruvate to lactate by lactate dehydrogenase.