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Questions and Answers
What is the coenzyme required for transamination reactions?
In transamination, the amino group of the amino acid is first transferred to which coenzyme?
Which vitamin is essential for the production of the coenzyme required in transamination reactions?
What is the ultimate fate of the amino groups collected through transamination reactions?
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Which molecule functions as an amino group donor for further processing of amino groups following transamination?
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What role does pyridoxal phosphate play in the transamination process?
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In a transamination reaction, what is interchanged between an a-amino acid and an a-keto acid?
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Which enzyme is needed for a transamination reaction?
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Which coenzyme is commonly accepted by most aminotransferases in transamination reactions?
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What is the primary chemical change that occurs in transamination reactions?
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What is not lost or gained during a transamination reaction?
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Why is transamination named as such?
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What is the primary function of the enzyme glutamate dehydrogenase discussed in the text?
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Which of the following accurately describes the role of aspartate in the urea cycle?
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What is the product of oxidative deamination of glutamate?
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Why is glutamate dehydrogenase considered unusual among enzymes?
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Which organelles play a significant role in oxidative deamination reactions?
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What is a key role of a-ketoglutarate in the process of oxidative deamination?
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Study Notes
Transamination
- Pyridoxal phosphate (PLP), derived from vitamin B6, is the coenzyme required for transamination reactions.
- In transamination, the amino group of the amino acid is first transferred to pyridoxal phosphate (PLP).
- The amino groups collected through transamination reactions are ultimately converted to urea and excreted.
- Glutamate functions as an amino group donor for further processing of amino groups following transamination.
- Pyridoxal phosphate (PLP) acts as a carrier of the amino group during transamination, forming a Schiff base intermediate with the amino acid.
- In a transamination reaction, an amino group is interchanged between an α-amino acid and an α-keto acid.
- Aminotransferases are the enzymes required for transamination reactions.
- Pyridoxal phosphate (PLP) is the coenzyme commonly accepted by most aminotransferases.
- The primary chemical change in transamination reactions is the transfer of an amino group from an amino acid to an α-keto acid.
- Transamination reactions do not lose or gain carbon atoms.
- Transamination is named as such because it involves the transfer of an amino group.
Oxidative Deamination
- The enzyme glutamate dehydrogenase catalyzes the oxidative deamination of glutamate, producing α-ketoglutarate and ammonia.
- Aspartate serves as a source of nitrogen for the urea cycle.
- The product of oxidative deamination of glutamate is α-ketoglutarate.
- Glutamate dehydrogenase is considered unusual among enzymes because it can use either NAD+ or NADP+ as a cofactor.
- Mitochondria play a significant role in oxidative deamination reactions.
- α-ketoglutarate, the product of glutamate dehydrogenase, is a key intermediate in the citric acid cycle.
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Description
Test your knowledge on the complex steps involved in a transamination reaction, which appears to be a simple transfer of an -NH3+ group between molecules. Understand the key components required for this biochemical process.
