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Catecholamine Synthesis Lab Report

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Words 989
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Maria Rahim
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BIMS 6322 – Gunasekera
September 7, 2014

Abstract: Inborn Errors of Catecholamine Synthesis Catecholamines are an integral part of the pathway that relay neurotransmitters from the adrenal medulla of the brain to associated tissues within the body that can transmit or receive hormones and adrenergic receptors. Their biosynthesis begins with three aromatic amino acids: phenylalanine, tyrosine and tryptophan that lead to the production the catecholamines, dopamine and serotonin. Dopamine is further synthesized into norepinephrine and epinephrine. Devastating clinical features can arise from inborn errors of catecholamine synthesis which stem from three key regulatory enzymes within the pathway: GTP cyclohydrolase I, tyrosine hydroxylase and aromatic L-amino acid decarboxylase. Unlike its well known counterpart, phenylketonuria which arises from metabolizing deficiencies of …show more content…
Tyrosine hydroxylase converts tyrosine to L-dopa. Like the gene mutation associated with GCH1, the mutation of TH is thought to be located with the regulatory domain of the tetrameric protein that controls the amount and activity of the enzyme. Tyrosine hydroxylase is first in the cascade of enzymes used in catecholamine biosynthesis and thus is highly regulated. Feedback inhibition through the end products of the pathway controls the activity of TH. Tyrosine hydroxylase deficiencies result in low enzyme activity and subsequently low levels of catecholamine synthesis required in the brain. Deficient levels of tyrosine hydroxylase are unable to convert tyrosine to L-dopa resulting in deficiencies of dopamine and epinephrine. Knock out studies conducted in mice which target tyrosine hydroxylase have proved lethal and justified the importance of TH in the catecholamine pathway and cerebral

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