Deamination | Oxidative and non-oxidative deamination

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#deamination #oxidation #aminoacids #metabolism

Deamination is the removal of an amino group from a molecule. Enzymes that catalyse this reaction are called deaminases.

In the human body, deamination takes place primarily in the liver, however glutamate is also deaminated in the kidneys. In situations of excess protein intake, deamination is used to break down amino acids for energy. The amine group is removed from the amino acid and converted to ammonia. The rest of the amino acid is made up of mostly carbon and hydrogen, and is recycled or oxidized for energy. Ammonia is toxic to the human system, and enzymes convert it to urea or uric acid by addition of carbon dioxide molecules (which is not considered a deamination process) in the urea cycle, which also takes place in the liver. Urea and uric acid can safely diffuse into the blood and then be excreted in urine.

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If this is not your first lecture then dont try to speed ...change your method sir ...

Easy.Editz__
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Too good ! You literally made me understand the concept . Please never stop making videos.

Dr.Karmaveer
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Well explanation it is very helpful, thank you 👍

iam_hassanali
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Everything is right. But deamination of cysteine by desulfhydrase liberates hydrogen sulfide not water.

zaturitzeik
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Thanks for this sir thory time me boht kch bta dia...

muhammadyahya
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What is the histidase structure names???

Aha_music
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Bro u have written as Desulphydrase and removed H20 like that of dehydrase!

fancyworld
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When cysteine involved in non oxidative deamination where is going to sulphur

MotivativeAlakh
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What is the name of last product and substrate

jamin
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Plz improve your pronunciation.speek slowly. Otherwise u r owesome.

rakhitiwari
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Why there is a specific enzyme only for glutamate deamination?

metch
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