PathWhiz ID | Pathway | Meta Data |
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PW000896View Pathway |
beta-Alanine MetabolismEscherichia coli
Beta-Alanine metabolism starts as a product of aspartate metabolism. Aspartate is decarboxylated by aspartate 1-decarboxylase, releasing carbon dioxide and beta-alanine. Beta-Alanine is then metabolized through a pantothenate synthease resulting in pantothenic acid. Pantothenic acid then undergoes phosphorylation through an ATP-driven pantothenate kinase, resulting in D-4-phosphopantothenate. Pantothenate, vitamin B5, is a precursor for synthesis of 4'-phosphopantetheine moiety of coenzyme A and acyl carrier protein. Plants and microorganisms can synthesize pantothenate de novo, but animals must obtain it from diet. Enzymes of beta-alanine metabolism are targets for anti-microbial drugs.
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Creator: miguel ramirez Created On: May 13, 2015 at 11:48 Last Updated: May 13, 2015 at 11:48 |
PW002381View Pathway |
beta-Alanine MetabolismSaccharomyces cerevisiae
The synthesis of beta-alanine starts with the biosynthesis of S-adenosylmethionine (SAM) from methionine. SAM is then used to synthesized S-adenosylmethionineamine which then reacts with putrescine through a spermidine synthase resulting in the release of 5'-methylthioadenosine and spermidine. The latter compound reacts with S-adenosylmethioninamine through spermine synthase resulting in the release of spermine and 5'-methylthioadenosine. Spermine reacts with water and oxygen through a polyamine oxidase resulting in the release of hydrogen peroxide, spermidine, and 3-aminopropanal. The latter compound reacts with an aldehyde dehydrogenase resulting in the release of beta-alanine. The degradation of beta-alanine leads to the production of coenzyme A which reacts with (R)-pantoate through an ATP-driven pantoate-beta-alanine ligase resulting in the release of pantothenic acid. The latter compound is then phosphorylated through a pantothenate kinase resulting in the release of D-4'-phosphopantothenate. This compound then reacts with L-cysteine and cytidine triphosphate through a phosphopantothenate cysteine ligase resulting in the release of cytidine monophosphate and 4'-phosphopantothenoylcysteine. The latter compound is then decarboxylated through a phosphopantothenoylcysteine decarboxylase resulting in the release of carbon dioxide and 4'-phosphopantethiene. The latter compound is then converted into dephospho-CoA through a pantetheine phosphate adenyltransferase. Dephospho-CoA is finally phosphorylated by a dephospho-CoA kinase resulting in the production of coenzyme A.
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Creator: miguel ramirez Created On: December 08, 2015 at 15:03 Last Updated: December 08, 2015 at 15:03 |
PW088199View Pathway |
beta-Alanine MetabolismBos taurus
Beta-alanine, 3-aminopropanoic acid, is a non-essential amino acid. Beta-Alanine is formed by the proteolytic degradation of beta-alanine containing dipeptides: carnosine, anserine, balenine, and pantothenic acid (vitamin B5). These dipeptides are consumed from protein-rich foods such as chicken, beef, pork, and fish. Beta-Alanine can also be formed in the liver from the breakdown of pyrimidine nucleotides into uracil and dihydrouracil and then metabolized into beta-alanine and beta-aminoisobutyrate. Beta-Alanine can also be formed via the action of aldehyde dehydrogenase on beta-aminoproionaldehyde which is generated from various aliphatic polyamines. Under normal conditions, beta-alanine is metabolized to aspartic acid through the action of glutamate decarboxylase. It addition, it can be converted to malonate semialdehyde and thereby participate in propanoate metabolism. Beta-Alanine is not a proteogenic amino acid. This amino acid is a common athletic supplementation due to its belief to improve performance by increased muscle carnosine levels.
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Creator: Ana Marcu Created On: August 10, 2018 at 11:05 Last Updated: August 10, 2018 at 11:05 |
PW088303View Pathway |
beta-Alanine MetabolismRattus norvegicus
Beta-alanine, 3-aminopropanoic acid, is a non-essential amino acid. Beta-Alanine is formed by the proteolytic degradation of beta-alanine containing dipeptides: carnosine, anserine, balenine, and pantothenic acid (vitamin B5). These dipeptides are consumed from protein-rich foods such as chicken, beef, pork, and fish. Beta-Alanine can also be formed in the liver from the breakdown of pyrimidine nucleotides into uracil and dihydrouracil and then metabolized into beta-alanine and beta-aminoisobutyrate. Beta-Alanine can also be formed via the action of aldehyde dehydrogenase on beta-aminoproionaldehyde which is generated from various aliphatic polyamines. Under normal conditions, beta-alanine is metabolized to aspartic acid through the action of glutamate decarboxylase. It addition, it can be converted to malonate semialdehyde and thereby participate in propanoate metabolism. Beta-Alanine is not a proteogenic amino acid. This amino acid is a common athletic supplementation due to its belief to improve performance by increased muscle carnosine levels.
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Creator: Ana Marcu Created On: August 10, 2018 at 13:31 Last Updated: August 10, 2018 at 13:31 |
PW064574View Pathway |
beta-Alanine MetabolismMus musculus
Beta-alanine, 3-aminopropanoic acid, is a non-essential amino acid. Beta-Alanine is formed by the proteolytic degradation of beta-alanine containing dipeptides: carnosine, anserine, balenine, and pantothenic acid (vitamin B5). These dipeptides are consumed from protein-rich foods such as chicken, beef, pork, and fish. Beta-Alanine can also be formed in the liver from the breakdown of pyrimidine nucleotides into uracil and dihydrouracil and then metabolized into beta-alanine and beta-aminoisobutyrate. Beta-Alanine can also be formed via the action of aldehyde dehydrogenase on beta-aminoproionaldehyde which is generated from various aliphatic polyamines. Under normal conditions, beta-alanine is metabolized to aspartic acid through the action of glutamate decarboxylase. It addition, it can be converted to malonate semialdehyde and thereby participate in propanoate metabolism. Beta-Alanine is not a proteogenic amino acid. This amino acid is a common athletic supplementation due to its belief to improve performance by increased muscle carnosine levels.
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Creator: Carin Li Created On: January 21, 2018 at 20:20 Last Updated: January 21, 2018 at 20:20 |
PW088451View Pathway |
beta-Alanine MetabolismCaenorhabditis elegans
Beta-alanine, 3-aminopropanoic acid, is a non-essential amino acid. Beta-Alanine is formed by the proteolytic degradation of beta-alanine containing dipeptides: carnosine, anserine, balenine, and pantothenic acid (vitamin B5). These dipeptides are consumed from protein-rich foods such as chicken, beef, pork, and fish. Beta-Alanine can also be formed in the liver from the breakdown of pyrimidine nucleotides into uracil and dihydrouracil and then metabolized into beta-alanine and beta-aminoisobutyrate. Beta-Alanine can also be formed via the action of aldehyde dehydrogenase on beta-aminoproionaldehyde which is generated from various aliphatic polyamines. Under normal conditions, beta-alanine is metabolized to aspartic acid through the action of glutamate decarboxylase. It addition, it can be converted to malonate semialdehyde and thereby participate in propanoate metabolism. Beta-Alanine is not a proteogenic amino acid. This amino acid is a common athletic supplementation due to its belief to improve performance by increased muscle carnosine levels.
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Creator: Ana Marcu Created On: August 10, 2018 at 17:01 Last Updated: August 10, 2018 at 17:01 |
PW124152View Pathway |
beta-Alanine MetabolismArabidopsis thaliana
β-Alanine, otherwise known as 3-aminopropanoic acid, is a naturally occurring beta amino acid with its amino group located on the beta position of the carboxylate group. Beta-Alanine is a non-proteinogenic with zero stereocenter. β-Alanine can be formed naturally during plant’s protein synthesis through degradation of dihydrouracil, pantothenic acid and carnosine for varies purposes, such as antibacterial & antiherbivore responses. Beta-Alanine can also be formed from Beta-Aminopropionaldehyde catalyzed by Precursor of CEP12. Formation of Beta-Alanine can also be occurred though N-Carbamoyl Beta-Alanine catalyzed by Beta-Ureidopropionase. Beta-Alanine can also be generated from various other pathways such as Arginine, Proline Cyanoamino Acid, Alanine, Aspartate, and glutamate metabolisms. For further reactions, Beta-Alanine can be used in Pantothenate and CoA syntheses though the conversion to (R)-Pantothenate. It can also be converted to Malonate semialdehyde to participate in Propanoate metabolism.
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Creator: Yu Heng Zheng Created On: September 09, 2020 at 22:38 Last Updated: September 09, 2020 at 22:38 |
PW127161View Pathway |
disease
beta-Aminoisobutyric AciduriaHomo sapiens
Hyper-beta-aminoisobutyric aciduria or BAIB urinary excretion is a common, autosomal recessive condition characterized by high levels of excretion of beta-aminoisobutyric acid in the urine. It is probably the most common mendelian metabolic variant in man. BAIB is a nonprotein amino acid, but it is an end product of pyrimidine metabolism. High excretion is frequent in Pacific populations that also show a high frequency of hyperuricemia. Impairment of R-BAIB catabolism due to deficient activity of a pyruvate-requiring transaminase, namely D-beta-aminoisobutyrate:pyruvate aminotransferase. This enzyme deficiency means that high BAIB excretors have impaired ability to degrade BAIB and thymine.
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Creator: Ray Kruger Created On: October 28, 2022 at 10:13 Last Updated: October 28, 2022 at 10:13 |
PW121813View Pathway |
disease
beta-Aminoisobutyric AciduriaMus musculus
Hyper-beta-aminoisobutyric aciduria or BAIB urinary excretion is a common, autosomal recessive condition characterized by high levels of excretion of beta-aminoisobutyric acid in the urine. It is probably the most common mendelian metabolic variant in man. BAIB is a nonprotein amino acid, but it is an end product of pyrimidine metabolism. High excretion is frequent in Pacific populations that also show a high frequency of hyperuricemia. Impairment of R-BAIB catabolism due to deficient activity of a pyruvate-requiring transaminase, namely D-beta-aminoisobutyrate:pyruvate aminotransferase. This enzyme deficiency means that high BAIB excretors have impaired ability to degrade BAIB and thymine.
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Creator: Ana Marcu Created On: September 10, 2018 at 15:49 Last Updated: September 10, 2018 at 15:49 |
PW000468View Pathway |
disease
beta-Aminoisobutyric AciduriaHomo sapiens
Hyper-beta-aminoisobutyric aciduria or BAIB urinary excretion is a common, autosomal recessive condition characterized by high levels of excretion of beta-aminoisobutyric acid in the urine. It is probably the most common mendelian metabolic variant in man. BAIB is a nonprotein amino acid, but it is an end product of pyrimidine metabolism. High excretion is frequent in Pacific populations that also show a high frequency of hyperuricemia. Impairment of R-BAIB catabolism due to deficient activity of a pyruvate-requiring transaminase, namely D-beta-aminoisobutyrate:pyruvate aminotransferase. This enzyme deficiency means that high BAIB excretors have impaired ability to degrade BAIB and thymine.
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Creator: WishartLab Created On: August 29, 2013 at 10:38 Last Updated: August 29, 2013 at 10:38 |