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Chapter 16: Problem 37

Define isoenzymes. Give five isoenzymes for lactase dehydrogenase (LDH).

Short Answer

Expert verified
Isoenzymes are enzyme variants catalyzing the same reaction. LDH has five isoenzymes: LDH-1, LDH-2, LDH-3, LDH-4, and LDH-5.

Step by step solution

01

Understand Isoenzymes

Isoenzymes, also known as isozymes, are different molecular forms of an enzyme that catalyze the same reaction but differ in amino acid sequence and kinetics. They often arise from different genes or from alternative splicing.
02

Identify Isoenzymes for LDH

Lactase dehydrogenase (LDH) is an enzyme that converts pyruvate to lactate when oxygen is absent. LDH has five isoenzymes (LDH-1 to LDH-5), each formed by different combinations of its two subunits: H (heart) and M (muscle).
03

List the Isoenzymes for LDH

The five isoenzymes of LDH are: 1. LDH-1 (H4) 2. LDH-2 (H3M1) 3. LDH-3 (H2M2) 4. LDH-4 (H1M3) 5. LDH-5 (M4)

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

enzyme kinetics
Enzyme kinetics is the study of how enzymes bind to substrates and convert them into products.
It explores how different conditions, such as temperature and pH, affect enzyme activity. Understanding enzyme kinetics helps us to know how fast reactions occur and how enzymes work under different conditions.
In practical applications, enzyme kinetics is crucial when designing drugs or when understanding metabolic pathways.
amino acid sequence
The amino acid sequence of a protein is its unique order of amino acids linked together.
This sequence determines the protein's structure, its properties, and ultimately its function in the biological system.
Different sequences result in different folding patterns and activities. In enzymes, the specific sequence can affect how the enzyme binds to its substrate and how it catalyzes the reaction.
alternative splicing
Alternative splicing is a process by which a single gene can lead to multiple proteins.
During gene expression, certain exons of a gene may be included or excluded from the final messenger RNA (mRNA) produced from that gene. This variation allows a single gene to encode multiple proteins with different functions.
Alternative splicing is an important mechanism for increasing protein diversity without increasing the number of genes.
lactase dehydrogenase (LDH)
Lactase dehydrogenase (LDH) is an important enzyme in the body.
It plays a crucial role in converting pyruvate, a product of glycolysis, into lactate when oxygen levels are low. LDH is present in many tissues, including the heart, liver, and muscles.
Its activity can be measured in the blood and is often used as a diagnostic tool for various conditions, including heart attack and liver disease.
subunits H and M
LDH is composed of two types of subunits: H (heart) and M (muscle).
Each isoenzyme of LDH is made up of different combinations of these subunits. For example, LDH-1 is made up of four H subunits (H4), whereas LDH-5 consists of four M subunits (M4).
These different combinations allow LDH to function optimally in different tissues, reflecting the specific metabolic needs of those tissues.
This structural diversity is what enables LDH's versatility and adaptability in various physiological contexts.

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Most popular questions from this chapter

What is the reactant for each of the following enzymes? a. peptidase b. cellulase c. lactase

Match the terms (1) active site, (2) lock-and-key model, and (3) induced-fit model with each of the following: a. the portion of an enzyme where catalytic activity occurs b. an active site that adapts to the shape of a substrate c. an active site that has a rigid shape

Name the substrate for each of the following enzymes: a. peptidase b. cellulase c. lactase

What are the properties and key functions of fibrous proteins?

Methanol and ethanol are oxidized by alcohol dehydrogenase. In methanol poisoning, ethanol is given intravenously to prevent the formation of formaldehyde that has toxic effects. a. Draw the condensed structural formulas for methanol and ethanol. b. Would ethanol compete for the active site or bind to a different site? c. Would ethanol be a competitive or noncompetitive inhibitor of alcohol dehydrogenase?
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