Transamination Overview and Mechanism
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Questions and Answers

What is the primary function of transamination?

  • To produce ATP
  • To synthesize fatty acids
  • To break down glucose
  • To transfer an amino group from an amino acid to an α-keto acid (correct)

Transamination is an irreversible reaction.

False (B)

What is the name of the enzyme that catalyzes transamination reactions?

aminotransferase

The cofactor required for transamination is ______, which is derived from vitamin B6.

<p>pyridoxal phosphate</p> Signup and view all the answers

Match the following enzyme with their specific actions in transamination.

<p>ALT = Catalyzes the reaction of alanine to pyruvate AST = Catalyzes the reaction of aspartate to oxaloacetate</p> Signup and view all the answers

What is the role of glutamate in transamination?

<p>It serves as a temporary reservoir for amino groups (C)</p> Signup and view all the answers

Keto acids produced in transamination can only be used for energy production.

<p>False (B)</p> Signup and view all the answers

What type of molecule is transferred during transamination?

<p>An amino group (-NHâ‚‚) (C)</p> Signup and view all the answers

Transamination is a process that only occurs during amino acid synthesis.

<p>False (B)</p> Signup and view all the answers

Besides converting them to other compounds, what is one fate of the keto acids produced by transamination?

<p>energy production</p> Signup and view all the answers

The enzyme ALT catalyzes the reaction of alanine to ______.

<p>pyruvate</p> Signup and view all the answers

Match the enzyme with the reaction each catalyzes:

<p>ALT = Alanine → Pyruvate AST = Aspartate → Oxaloacetate</p> Signup and view all the answers

What is the primary role of pyridoxal phosphate (PLP) in transamination reactions?

<p>It serves as a cofactor required for the enzyme’s activity. (A)</p> Signup and view all the answers

Glutamate donates its amino group directly to the urea cycle for excretion.

<p>False (B)</p> Signup and view all the answers

What is the main outcome of transamination?

<p>Interconversion of amino acids and keto acids (C)</p> Signup and view all the answers

Transamination plays a critical role in generating non-essential amino acids.

<p>True (A)</p> Signup and view all the answers

What reaction occurs when alanine and α-ketoglutarate undergo transamination?

<p>Pyruvate and Glutamate</p> Signup and view all the answers

The cofactor required for transamination is ______.

<p>Pyridoxal phosphate</p> Signup and view all the answers

Match the following enzymes with the reactions they catalyze:

<p>ALT = Alanine → Pyruvate AST = Aspartate → Oxaloacetate ALDH = Glutamate → α-Ketoglutarate LDH = Pyruvate → Lactate</p> Signup and view all the answers

What role does glutamate play in the urea cycle?

<p>It serves as a temporary reservoir for amino groups (B)</p> Signup and view all the answers

Which of the following statements about transamination is true?

<p>It involves the transfer of an amino group from an amino acid to an α-keto acid. (C)</p> Signup and view all the answers

Name the enzyme responsible for catalyzing the reaction of aspartate to oxaloacetate.

<p>AST (Aspartate Aminotransferase)</p> Signup and view all the answers

Match the following keto acids with their potential fates:

<p>Pyruvate = Used in gluconeogenesis or energy production Oxaloacetate = Precursor for glucose or entry into Krebs Cycle Acetyl-CoA = Used in fatty acid synthesis α-ketoglutarate = Participates in the Krebs cycle</p> Signup and view all the answers

Which process does glutamate undergo to donate the amino group for urea cycle excretion?

<p>Oxidative deamination (C)</p> Signup and view all the answers

What is formed when alanine undergoes transamination with α-ketoglutarate?

<p>Pyruvate and Glutamate</p> Signup and view all the answers

Flashcards

What is transamination?

Transamination is the transfer of an amino group (-NH2) from an amino acid to an α-keto acid. This process allows the body to interconvert amino acids and keto acids.

What enzyme is involved in transamination?

Aminotransferase (also called transaminase) is the enzyme responsible for catalyzing transamination.

What cofactor is required for transamination?

Pyridoxal phosphate (PLP), derived from vitamin B6, acts as a cofactor in transamination.

What is the purpose of transamination?

Transamination is a reversible reaction used in the synthesis and degradation of amino acids. It plays a crucial role in generating non-essential amino acids and preparing amino groups for urea cycle excretion.

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What is the role of glutamate in transamination?

Glutamate acts as a temporary reservoir for amino groups, accepting them during transamination and later donating them to the urea cycle.

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What happens to the keto acid produced in transamination?

The keto acid produced during transamination can be used in energy production (Krebs cycle), or converted into glucose or lipids.

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What are the key enzymes involved in transamination?

Alanine aminotransferase (ALT) catalyzes the reaction of alanine to pyruvate, while aspartate aminotransferase (AST) catalyzes the conversion of aspartate to oxaloacetate.

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What enzyme catalyzes Transamination?

Aminotransferases (also known as transaminases) are enzymes that catalyze the process of transamination. They help facilitate the transfer of the amino group.

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What cofactor is needed for Transamination?

Pyridoxal phosphate (PLP), a derivative of vitamin B6, is a crucial coenzyme in transamination. It assists in the transfer of the amino group.

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Is Transamination reversible?

Transamination is a reversible reaction, meaning it can proceed in both directions. This allows the body to synthesize and break down amino acids as needed.

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What is Glutamate's role in Transamination?

Glutamate acts as a temporary storage container for amino groups. It receives the amino group during transamination and later releases it into the urea cycle for excretion.

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What are examples of enzymes in Transamination?

ALT (Alanine Aminotransferase) and AST (Aspartate Aminotransferase) are two important enzymes involved in transamination, each specific to different amino acids.

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What happens to the keto acid after transamination?

The keto acid produced can be used as fuel for the cell (Krebs cycle), or converted into glucose or lipids.

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Give examples of enzymes involved in transamination?

ALT (Alanine aminotransferase) and AST (Aspartate aminotransferase) are key enzymes in transamination.

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Study Notes

Transamination Overview

  • Transamination is the transfer of an amino group (-NHâ‚‚) from an amino acid to an α-keto acid.
  • This process allows the body to interconvert amino acids and keto acids.
  • The reaction is catalyzed by enzymes called aminotransferases (or transaminases).
  • A cofactor, pyridoxal phosphate (PLP), derived from vitamin B6, is essential for the reaction.

Purpose of Transamination

  • Transamination is a reversible process, used in both the synthesis and degradation of amino acids.
  • It's critical for generating non-essential amino acids.
  • It prepares amino groups for excretion via the urea cycle by transferring them to glutamate.
  • Crucially, this process is used in the synthesis and degradation of amino acids.

Transamination Reaction Mechanism

  • An amino acid reacts with α-ketoglutarate, forming a keto acid and glutamate.
  • Example: Alanine + α-ketoglutarate ↔ Pyruvate + Glutamate

Key Enzymes in Transamination

  • Alanine aminotransferase (ALT) catalyzes the conversion of alanine to pyruvate.
  • Aspartate aminotransferase (AST) catalyzes the conversion of aspartate to oxaloacetate.

Glutamate's Role

  • Glutamate acts as a temporary store for amino groups.
  • It delivers these amino groups to the urea cycle through oxidative deamination.
  • Glutamate serves as a temporary reservoir for amino groups, donating them to the urea cycle.

Fate of Keto Acids

  • Keto acids can be used for energy production in the Krebs cycle.
  • They can also be converted into glucose or lipids.

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Description

This quiz covers the fundamental aspects of transamination, including its purpose, mechanisms, and key enzymes involved in the process. Understand how amino groups are transferred and the significance of this biochemical reaction in the synthesis of non-essential amino acids. Test your knowledge on the role of pyridoxal phosphate and notable enzymes like alanine aminotransferase.

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