Disorders of Sulfur Amino Acid Metabolism

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00064165%3A_____%2F16%3A10333588" target="_blank" >RIV/00064165:_____/16:10333588 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11110/16:10333588

Result on the web

<a href="http://dx.doi.org/10.1007/978-3-662-49771-5_20" target="_blank" >http://dx.doi.org/10.1007/978-3-662-49771-5_20</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/978-3-662-49771-5_20" target="_blank" >10.1007/978-3-662-49771-5_20</a>

Result language

angličtina

Original language name

Disorders of Sulfur Amino Acid Metabolism

Original language description

The essential amino acid methionine is converted by two methionine adenosyltransferases (MAT I/III and MATII) to S-adenosylmethionine (SAM). The methyl group of SAM is used in numerous biologically important methylation reactions, yielding S-adenosylhomocysteine (SAH); excess SAM is removed from the cycle by glycine N-methyltransferase (GNMT). SAH is cleaved by of S-adenosylhomocysteine hydrolase (SAHH) to homocysteine and adenosine, which is further metabolized by adenosine kinase (ADK). Homocysteine can be converted back to methionine by the remethylation pathway or using betaine as a methyl-group donor, in patients treated with this drug. Alternatively, homocysteine is irreversibly metabolized to sulfate by the transsulfuration pathway. Homocysteine is condensed with serine to form cystathionine, which is subsequently cleaved to form cysteine and α-ketobutyrate; these reactions are catalysed by cystathionine β-synthase (CBS) and cystathionine γ-lyase (CTH), respectively, which can also use cysteine and/or homocysteine to synthesize hydrogen sulfide. Cysteine can be further converted in a series of reactions into taurine, or via the mitochondrial enzymes, aspartate aminotransferase (AST) and 3-mercaptopyruvate sulfurtransferase (MPST), to pyruvate and hydrogen sulfide. Mitochondrial oxidation of hydrogen sulfide involves several steps yielding thiosulfate, sulfite and finally sulfate; the figure only shows sulfur dioxygenase (ETHE1) and sulfite oxidase (SUOX), which requires the molybdenum cofactor, produced by enzymes encoded by molybdenum cofactor synthesis 1 and 2 genes (MOCS1 and 2) and by gephyrin (GPHN).

Czech name

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Czech description

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Type

C - Chapter in a specialist book

CEP classification

FB - Endocrinology, diabetology, metabolism, nutrition

OECD FORD branch

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Project

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Continuities

V - Vyzkumna aktivita podporovana z jinych verejnych zdroju

Publication year

2016

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Book/collection name

Inborn Metabolic Diseases. Diagnosis and Treatment

ISBN

978-3-662-49769-2

Number of pages of the result

12

Pages from-to

309-320

Number of pages of the book

658

Publisher name

Springer

Place of publication

Berlin, Heidelberg

UT code for WoS chapter

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