Concept explainers
To tell:
How much nitrogen is needed to produce amino acids through amination?
Introduction:
Some microorganisms (fungi, pathogenic bacteria, and food-spoilage bacteria) catabolize proteins as a vital source of metabolites and energy. Maximum cells catabolize amino acids and proteins, only when there is a lack of carbon sources like fat and glucose. In general, proteins are macromolecules that pass through cytoplasmic membranes. Thus, prokaryotic organisms carry out protein catabolism (outside the cell) through discharging an enzyme protease, which splits the proteins into amino acids. Later, the amino acids are shifted to the cell, and again get split into amino groups, by a process which is termed as deamination. This modified molecule reaches the Krebs cycle, where it can be recycled to form other amino groups or be defecated as ammonia or nitrogenous wastes.
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Microbiology with Diseases by Body System (5th Edition)
- How is acetyl coenzyme A formed?arrow_forwardWhat amino acids are obtained from the same metabolic intermediates when the amino acids are synthesized in the laboratory?arrow_forwardWhich of the following statements about the transamination and deamination steps of amino acid degradation is true? (A) a-ketoglutarate is always formed during a transamination between an amino acid and glutamate. (B) Transamination reactions produce glutamate that is deaminated after entering the urea cycle. (C) Free ammonia is removed from glutamate using glutamate dehydrogenase and NAD+ as an oxidizing agent. (D) The free NH4+ that is removed from glutamate during the deamination reaction is used to form glucose.(E) The carbon backbone that results from transamination enters the mitochondria to be used in the urea cycle.arrow_forward
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