A metabolite in the principal biochemical pathway of lysine. It antagonizes neuroexcitatory activity modulated by the glutamate receptor, N-METHYL-D-ASPARTATE; (NMDA).
An essential amino acid. It is often added to animal feed.
A nutritional condition produced by a deficiency of VITAMIN B 6 in the diet, characterized by dermatitis, glossitis, cheilosis, and stomatitis. Marked deficiency causes irritability, weakness, depression, dizziness, peripheral neuropathy, and seizures. In infants and children typical manifestations are diarrhea, anemia, and seizures. Deficiency can be caused by certain medications, such as isoniazid.
The 4-methanol form of VITAMIN B 6 which is converted to PYRIDOXAL PHOSPHATE which is a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. Although pyridoxine and Vitamin B 6 are still frequently used as synonyms, especially by medical researchers, this practice is erroneous and sometimes misleading (EE Snell; Ann NY Acad Sci, vol 585 pg 1, 1990).
Substances used for their pharmacological actions on any aspect of neurotransmitter systems. Neurotransmitter agents include agonists, antagonists, degradation inhibitors, uptake inhibitors, depleters, precursors, and modulators of receptor function.
This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE).
An enzyme catalyzing the deamination of pyridoxaminephosphate to pyridoxal phosphate. It is a flavoprotein that also oxidizes pyridoxine-5-phosphate and pyridoxine. EC 1.4.3.5.
The removal of a carboxyl group, usually in the form of carbon dioxide, from a chemical compound.
The 4-carboxyaldehyde form of VITAMIN B 6 which is converted to PYRIDOXAL PHOSPHATE which is a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid.

Aspartate kinase-independent lysine synthesis in an extremely thermophilic bacterium, Thermus thermophilus: lysine is synthesized via alpha-aminoadipic acid not via diaminopimelic acid. (1/119)

An aspartate kinase-deficient mutant of Thermus thermophilus, AK001, was constructed. The mutant strain did not grow in a minimal medium, suggesting that T. thermophilus contains a single aspartate kinase. Growth of the mutant strain was restored by addition of both threonine and methionine, while addition of lysine had no detectable effect on growth. To further elucidate the lysine biosynthetic pathway in T. thermophilus, lysine auxotrophic mutants of T. thermophilus were obtained by chemical mutagenesis. For all lysine auxotrophic mutants, growth in a minimal medium was not restored by addition of diaminopimelic acid, whereas growth of two mutants was restored by addition of alpha-aminoadipic acid, a precursor of lysine in biosynthetic pathways of yeast and fungi. A BamHI fragment of 4.34 kb which complemented the lysine auxotrophy of a mutant was cloned. Determination of the nucleotide sequence suggested the presence of homoaconitate hydratase genes, termed hacA and hacB, which could encode large and small subunits of homoaconitate hydratase, in the cloned fragment. Disruption of the chromosomal copy of hacA yielded mutants showing lysine auxotrophy which was restored by addition of alpha-aminoadipic acid or alpha-ketoadipic acid. All of these results indicated that in T. thermophilus, lysine was not synthesized via the diaminopimelic acid pathway, believed to be common to all bacteria, but via a pathway using alpha-aminoadipic acid as a biosynthetic intermediate.  (+info)

In Saccharomyces cerevisae, feedback inhibition of homocitrate synthase isoenzymes by lysine modulates the activation of LYS gene expression by Lys14p. (2/119)

Expression of the structural genes for lysine biosynthesis responds to an induction mechanism mediated by the transcriptional activator Lys14p in the presence of alpha-aminoadipate semialdehyde (alphaAASA), an intermediate of the pathway acting as a coinducer. This activation is reduced by the presence of lysine in the growth medium, leading to apparent repression. In this report we demonstrate that Saccharomyces cerevisiae possesses two genes, LYS20 and LYS21, encoding two homocitrate synthase isoenzymes which are located in the nucleus. Each isoform is inhibited by lysine with a different sensitivity. Lysine-overproducing mutants were isolated as resistant to aminoethylcysteine, a toxic lysine analog. Mutations, LYS20fbr and LYS21fbr, are allelic to LYS20 and LYS21, and lead to desensitization of homocitrate synthase activity towards lysine and to a loss of apparent repression by this amino acid. There is a fair correlation between the I0.5 of homocitrate synthase for lysine, the intracellular lysine pool and the levels of Lys enzymes, confirming the importance of the activity control of the first step of the pathway for the expression of LYS genes. The data are consistent with the conclusion that inhibition by lysine of Lys14p activation results from the control of alphaAASA production through the feedback inhibition of homocitrate synthase activity.  (+info)

RIT 2214, a new biosynthetic penicillin produced by a mutant of Cephalosporium acremonium. (3/119)

A number of lysine-requiring auxotrophs of Cephalosporium acremonium were investigated for incorporation of side-chain precursors and for accumulation of beta-lactam compounds. One of the auxotrophs, Acremonium chrysogenum ATCC 20389, producing cephalosporin C and penicillin N only if grown in media supplemented with DL-alpha-amino-adipic acid (DL-alpha-AAA), was found to use L-S-carboxymethylcysteine (L-CMC) as a side-chain precursor for the synthesis of a new penicillin (RIT 2214). No corresponding cephalosporin was detected. The penicillin present in the culture filtrate, was concentrated by adsorption on activated carbon and successive column chromatography on Amberlite IRA-68 and Amberlite XAD-4. Final purification was achieved by cellulose column chromatography. RIT 2214 was identified as 6-(D)-[(2-amino-2-carboxy)-ethylthio]-acetamido]-penicillanic acid by spectral analysis, bioactivity spectrum, elucidation of side-chain structure and finally by semisynthesis. Its biological properties were also evaluated.  (+info)

Nonlinear disposition kinetics of a novel antifolate, MX-68, in rats. (4/119)

The excretion and tissue distribution kinetics of a novel antifolate, MX-68, were evaluated under conditions of a continuous steady-state infusion in Sprague-Dawley rats (SDRs). The biliary excretion clearance defined with respect to the hepatic concentration (CL(bile, h)) was much lower in Eisai hyperbilirubinemic rats with a hereditary deficiency in canalicular multispecific organic anion transporter than that in SDRs, suggesting the involvement of canalicular multispecific organic anion transporter in its transport across the bile canalicular membrane. The CL(bile, h) in SDRs increased as the infusion rate increased; this can be largely explained by saturation of the intracellular binding of MX-68. On the other hand, the urinary excretion clearance defined with respect to the renal concentration (CL(urine, k)) was comparable for the two strains but showed an increase and subsequent decrease as the renal concentration increased. This nonlinear profile was also found even when the CL(urine, k) was normalized by the unbound fraction in kidney. Therefore, this kinetic profile represents the saturation of both reabsorption and secretion. Reabsorption of MX-68 in kidney was supported by its saturable transport by renal brush border membrane vesicles at an inward H(+) gradient. The liver-to-plasma unbound concentration ratio decreased as the steady-state plasma concentration increased, suggesting that MX-68 is taken up by a saturable mechanism or mechanisms. Thus, the saturation of transport systems across several plasma membranes and intracellular binding in both the liver and kidney produce the nonlinear disposition of MX-68.  (+info)

A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: a key to the evolution of amino acid biosynthesis. (5/119)

In previous studies we determined the nucleotide sequence of the gene cluster containing lys20, hacA (lys4A), hacB (lys4B), orfE, orfF, rimK, argC, and argB of Thermus thermophilus, an extremely thermophilic bacterium. In this study, we characterized the role of each gene in the cluster by gene disruption and examined auxotrophy in the disruptants. All disruptants except for the orfE disruption showed a lysine auxotrophic phenotype. This was surprising because this cluster consists of genes coding for unrelated proteins based on their names, which had been tentatively designated by homology analysis. Although the newly found pathway contains alpha-aminoadipic acid as a lysine biosynthetic intermediate, this pathway is not the same as the eukaryotic one. When each of the gene products was phylogenetically analyzed, we found that genes evolutionarily-related to the lysine biosynthetic genes in T. thermophilus were all present in a hyperthermophilic and anaerobic archaeon, Pyrococcus horikoshii, and formed a gene cluster in a manner similar to that in T. thermophilus. Furthermore, this gene cluster was analogous in part to the present leucine and arginine biosyntheses pathways. This lysine biosynthesis cluster is assumed to be one of the origins of lysine biosynthesis and could therefore become a key to the evolution of amino acid biosynthesis.  (+info)

The catabolic function of the alpha-aminoadipic acid pathway in plants is associated with unidirectional activity of lysine-oxoglutarate reductase, but not saccharopine dehydrogenase. (6/119)

Whereas plants and animals use the alpha-aminoadipic acid pathway to catabolize lysine, yeast and fungi use the very same pathway to synthesize lysine. These two groups of organisms also possess structurally distinct forms of two enzymes in this pathway, namely lysine-oxoglutarate reductase (lysine-ketoglutarate reductase; LKR) and saccharopine dehydrogenase (SDH): in plants and animals these enzymes are linked on to a single bifunctional polypeptide, while in yeast and fungi they exist as separate entities. In addition, yeast LKR and SDH possess bi-directional activities, and their anabolic function is regulated by complex transcriptional and post-transcriptional controls, which apparently ascertain differential accumulation of intermediate metabolites; in plants, the regulation of the catabolic function of these two enzymes is not known. To elucidate the regulation of the catabolic function of plant bifunctional LKR/SDH enzymes, we have used yeast as an expression system to test whether a plant LKR/SDH also possesses bi-directional LKR and SDH activities, similar to the yeast enzymes. The Arabidopsis enzyme complemented a yeast SDH, but not LKR, null mutant. Identical results were obtained when deletion mutants encoding only the LKR or SDH domains of this bifunctional polypeptide were expressed individually in the yeast cells. Moreover, activity assays showed that the Arabidopsis LKR possessed catabolic, but not anabolic, activity, and its uni-directional activity stems from its structure rather than its linkage to SDH. Our results suggest that the uni-directional activity of LKR plays an important role in regulating the catabolic function of the alpha-amino adipic acid pathway in plants.  (+info)

Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis. (7/119)

BACKGROUND: The biosynthesis of the essential amino acid lysine in higher fungi and cyanobacteria occurs via the alpha-aminoadipate pathway, which is completely different from the lysine biosynthetic pathway found in plants and bacteria. The penultimate reaction in the alpha-aminoadipate pathway is catalysed by NADPH-dependent saccharopine reductase. We set out to determine the structure of this enzyme as a first step in exploring the structural biology of fungal lysine biosynthesis. RESULTS: We have determined the three-dimensional structure of saccharopine reductase from the plant pathogen Magnaporthe grisea in its apo form to 2.0 A resolution and as a ternary complex with NADPH and saccharopine to 2.1 A resolution. Saccharopine reductase is a homodimer, and each subunit consists of three domains, which are not consecutive in amino acid sequence. Domain I contains a variant of the Rossmann fold that binds NADPH. Domain II folds into a mixed seven-stranded beta sheet flanked by alpha helices and is involved in substrate binding and dimer formation. Domain III is all-helical. The structure analysis of the ternary complex reveals a large movement of domain III upon ligand binding. The active site is positioned in a cleft between the NADPH-binding domain and the second alpha/beta domain. Saccharopine is tightly bound to the enzyme via a number of hydrogen bonds to invariant amino acid residues. CONCLUSIONS: On the basis of the structure of the ternary complex of saccharopine reductase, an enzymatic mechanism is proposed that includes the formation of a Schiff base as a key intermediate. Despite the lack of overall sequence homology, the fold of saccharopine reductase is similar to that observed in some enzymes of the diaminopimelate pathway of lysine biosynthesis in bacteria. These structural similarities suggest an evolutionary relationship between two different major families of amino acid biosynthetic pathway, the glutamate and aspartate families.  (+info)

Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. (8/119)

Metal-catalyzed oxidation results in loss of function and structural alteration of proteins. The oxidative process affects a variety of side amino acid groups, some of which are converted to carbonyl compounds. Spectrophotometric measurement of these moieties, after their reaction with 2,4-dinitrophenylhydrazine, is a simple, accurate technique that has been widely used to reveal increased levels of protein carbonyls in aging and disease. We have initiated studies aimed at elucidating the chemical nature of protein carbonyls. Methods based on gas chromatography/mass spectrometry with isotopic dilution were developed for the quantitation of glutamic and aminoadipic semialdehydes after their reduction to hydroxyaminovaleric and hydroxyaminocaproic acids. Analysis of model proteins oxidized in vitro by Cu2+/ascorbate revealed that these two compounds constitute the majority of protein carbonyls generated. Glutamic and aminoadipic semialdehydes were also detected in rat liver proteins, where they constitute approximately 60% of the total protein carbonyl value. Aminoadipic semialdehyde was also measured in protein extracts from HeLa cells, and its level increased as a consequence of oxidative stress to cell cultures. These results indicate that glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins, and that this reaction is a major route leading to the generation of protein carbonyls in biological samples.  (+info)

2-Aminoadipic acid (2-AAA) is a naturally occurring amino acid that is involved in the metabolism of the amino acid lysine. It is also used as a precursor in the synthesis of certain polymers, such as polyamide-6,6, and as a chelating agent for heavy metals. In the medical field, 2-AAA has been studied for its potential therapeutic effects in a number of conditions. For example, it has been shown to have anti-inflammatory and analgesic properties, and has been used to treat pain and inflammation in animal models. It has also been studied for its potential to protect against neurodegenerative diseases, such as Alzheimer's and Parkinson's disease, by reducing oxidative stress and inflammation in the brain. In addition, 2-AAA has been used as a diagnostic tool in the detection of certain genetic disorders, such as homocystinuria, which is a condition characterized by high levels of homocysteine in the blood. In this context, 2-AAA is used as a substrate in a diagnostic test to measure the activity of the enzyme cystathionine beta-synthase, which is involved in the metabolism of homocysteine.

Lysine is an essential amino acid that is required for the growth and maintenance of tissues in the human body. It is one of the nine essential amino acids that cannot be synthesized by the body and must be obtained through the diet. Lysine plays a crucial role in the production of proteins, including enzymes, hormones, and antibodies. It is also involved in the absorption of calcium and the production of niacin, a B vitamin that is important for energy metabolism and the prevention of pellagra. In the medical field, lysine is used to treat and prevent various conditions, including: 1. Herpes simplex virus (HSV): Lysine supplements have been shown to reduce the frequency and severity of outbreaks of HSV-1 and HSV-2, which cause cold sores and genital herpes, respectively. 2. Cold sores: Lysine supplements can help reduce the frequency and severity of cold sore outbreaks by inhibiting the replication of the herpes simplex virus. 3. Depression: Lysine has been shown to increase levels of serotonin, a neurotransmitter that regulates mood, in the brain. 4. Hair loss: Lysine is important for the production of hair, and deficiency in lysine has been linked to hair loss. 5. Wound healing: Lysine is involved in the production of collagen, a protein that is important for wound healing. Overall, lysine is an important nutrient that plays a crucial role in many aspects of human health and is used in the treatment and prevention of various medical conditions.

Vitamin B6 deficiency is a condition that occurs when the body does not have enough of the vitamin B6 nutrient. Vitamin B6 is an essential nutrient that plays a crucial role in many bodily functions, including the production of red blood cells, the breakdown of amino acids, and the metabolism of fats and carbohydrates. Symptoms of vitamin B6 deficiency can include fatigue, weakness, irritability, depression, confusion, and anemia. In severe cases, vitamin B6 deficiency can lead to neurological problems, such as convulsions, seizures, and even death. Vitamin B6 deficiency can occur due to a lack of dietary intake, malabsorption of the nutrient, or increased。It is important to note that vitamin B6 deficiency is relatively rare in developed countries, but it can occur in individuals with certain medical conditions, such as Crohn's disease, celiac disease, or alcoholism.

Pyridoxine, also known as vitamin B6, is a water-soluble vitamin that plays a crucial role in various bodily functions. It is involved in the metabolism of amino acids, carbohydrates, and lipids, as well as the production of neurotransmitters such as serotonin and dopamine. Pyridoxine is also essential for the proper functioning of the immune system and the prevention of anemia. In the medical field, pyridoxine is used to treat a variety of conditions, including: 1. Anemia: Pyridoxine is used to treat anemia caused by a deficiency in vitamin B6. 2. Morning sickness: Pyridoxine is sometimes used to treat morning sickness during pregnancy. 3. Depression: Pyridoxine may be used as an adjunct therapy for depression, as it is involved in the production of neurotransmitters. 4. Alcoholism: Pyridoxine may be used to treat alcoholism, as it can help prevent the formation of acetaldehyde, a toxic substance produced during alcohol metabolism. 5. Pernicious anemia: Pyridoxine is used in combination with other vitamins to treat pernicious anemia, a type of anemia caused by a deficiency in vitamin B12. Pyridoxine is available in various forms, including tablets, capsules, and injections. It is generally well-tolerated, but high doses may cause side effects such as nausea, dizziness, and confusion.

Pyridoxal phosphate (PLP) is a coenzyme form of vitamin B6 (pyridoxine) that plays a crucial role in various metabolic processes in the body. It is involved in the metabolism of amino acids, lipids, and carbohydrates, as well as in the synthesis of neurotransmitters and hemoglobin. In the medical field, PLP deficiency can lead to a variety of health problems, including anemia, seizures, and neurological disorders. It is also used as a dietary supplement to treat or prevent vitamin B6 deficiency and related conditions. In addition, PLP is used in the treatment of certain types of cancer, such as leukemia, and in the management of certain neurological disorders, such as Alzheimer's disease and Parkinson's disease.

Pyridoxaminephosphate oxidase (PMP oxidase) is an enzyme that plays a crucial role in the metabolism of vitamin B6 (pyridoxine). It catalyzes the oxidation of pyridoxamine phosphate (PMP) to pyridoxal phosphate (PLP), which is the active form of vitamin B6 that is involved in various metabolic reactions in the body. PMP oxidase is primarily found in the liver, but it is also present in other tissues such as the brain, kidneys, and red blood cells. Deficiency of PMP oxidase can lead to a condition called pyridoxine-dependent epilepsy, which is a rare genetic disorder characterized by seizures and developmental delays. In this condition, the body is unable to convert PMP to PLP, leading to a deficiency of PLP and an accumulation of PMP in the brain. In addition to its role in vitamin B6 metabolism, PMP oxidase has also been implicated in the metabolism of other compounds such as dopamine and serotonin. Therefore, research on PMP oxidase is important for understanding the metabolism of these compounds and their role in various diseases.

Pyridoxal is a form of vitamin B6 that is found in small amounts in some foods and is also available as a dietary supplement. It is a water-soluble vitamin that plays a role in many important bodily functions, including the metabolism of amino acids, the production of red and white blood cells, and the maintenance of the nervous system. Pyridoxal is also used in the treatment of certain medical conditions, such as anemia, depression, and nerve damage. It is important to note that pyridoxal is not the same as pyridoxine, which is another form of vitamin B6 that is more commonly used in dietary supplements and medications.

Jones EE, Broquist HP (June 1965). "Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. Ii. ... Trupin JS, Broquist HP (June 1965). "Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. I. ... Alpha-aminoadipic semialdehyde synthase is an enzyme encoded by the AASS gene in humans and is involved in their major lysine ... Alpha-aminoadipic semialdehyde synthase is encoded for by the AASS gene, and mutations in this gene lead to hyperlysinemia. ...
α-Aminoadipic acid is the conjugate acid of α-aminoadipate, the latter of which is the prevalent form at physiological pH. A ... Alpha-Amino acids, Metabolism, Biosynthesis, Metabolic pathways, Dicarboxylic acids, All stub articles, Biochemistry stubs). ... Adipic acid Zabriskie TM, Jackson MD (2000). "Lysine biosynthesis and metabolism in fungi". Natural Product Reports. 17 (1): 85 ... The α-aminoadipate pathway is a biochemical pathway for the synthesis of the amino acid L-lysine. In the eukaryotes, this ...
L-Lys undergoes a transamination to form α-aminoadipic acid. α-aminoadipic acid undergoes a ring closure and then a reduction ... which reduces to L-pipecolic acid. HSCoA and then malonyl-CoA react in a Claisen reaction with L-pipecolic acid to form SCoA ... "Biochemical Principles and Functional Aspects of Pipecolic Acid Biosynthesis in Plant Immunity". Plant Physiology. 174 (1): 124 ... "Biochemical Principles and Functional Aspects of Pipecolic Acid Biosynthesis in Plant Immunity". Plant Physiology. 174 (1): 124 ...
Saunders PP, Broquist HP (1966). "Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. IV. ... 2-oxoglutarate + NADH + H+ The 3 substrates of this enzyme are N6-(L-1,3-dicarboxypropyl)-L-lysine, NAD+, and H2O, whereas its ... glutar-2-yl)-L-lysine:NAD oxidoreductase (L-lysine-forming), 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase, and (L- ... L-glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine, forming), N6-( ...
... metabolic disorder characterized by an increased urinary excretion of alpha-ketoadipic acid and alpha-aminoadipic acid. It is ... Alpha-aminoadipic and alpha-ketoadipic aciduria is an autosomal recessive ... "DHTKD1 mutations cause 2-aminoadipic and 2-oxoadipic aciduria". American Journal of Human Genetics. 91 (6): 1082-7. doi:10.1016 ...
The DHTKD1 gene encodes a protein that has 919 amino acids, and is one of two isoforms within the 2-oxoglutarate-dehydrogenase ... Mutations in the DHTKD1 gene are associated with alpha-aminoadipic and alpha-ketoadipic aciduria, an autosomal recessive inborn ... "Genetic basis of alpha-aminoadipic and alpha-ketoadipic aciduria". Journal of Inherited Metabolic Disease. 38 (5): 873-9. doi: ... 71 (2): 874-90. doi:10.1002/prot.21766. PMID 18004749. S2CID 23882203. Danhauser K, Sauer SW, Haack TB, Wieland T, Staufner C, ...
This decrease in activity was due to the replacement of the D-α-aminoadipic acid side chain with phenylacetic acid. ... Cephalosporin C strongly absorbs ultraviolet light, is stable to acid, is non-toxic and has in vivo activity in mice. ... 79 (2): 377-393. doi:10.1042/bj0790377. PMC 1205850. PMID 13681080. Kardos, Nelson; Demain, Arnold L. (November 2011). " ...
... an intermediate of the aminoadipic acid pathway of lysine biosynthesis. 3. Aminoadipic semialdehyde-glutamate reductase". J. ... aminoadipic semialdehyde-glutamic reductase, aminoadipate semialdehyde-glutamate reductase, aminoadipic semialdehyde-glutamate ... L-2-aminoadipate 6-semialdehyde + NADPH + H+ The 3 substrates of this enzyme are N6-(L-1,3-dicarboxypropyl)-L-lysine, NADP+, ... and H2O, whereas its 4 products are L-glutamate, L-2-aminoadipate 6-semialdehyde, NADPH, and H+. This enzyme belongs to the ...
... a New Antibiotic containing Sulphur and D-α-Aminoadipic Acid". Nature. 175 (4456): 548. doi:10.1038/175548a0. PMID 14370161. ... Abraham showed that modification of the 7-amino-cephalosporanic acid nucleus was able to increase the potency of this ... Loder, Bronwen; Newton, G. G. F.; Abraham, E. P. (1 May 1961). "The cephalosporin C nucleus (7-aminocephalosporanic acid) and ... 79 (2): 408-416. doi:10.1042/bj0790408. ISSN 0264-6021. PMC 1205853. PMID 13763020. Hale, C. W.; Newton, G. G. F.; Abraham, E. ...
... ic acid.) Most natural amino acids are α-amino acids in the L conformation, but some exceptions exist. Some non-α-amino acids ... Chemically synthesized amino acids can be called unnatural amino acids. Unnatural amino acids can be synthetically prepared ... Whereas glutamic acid possess one γ-carboxyl group, Carboxyglutamic acid possess two. Hydroxyproline. This imino acid differs ... and a carboxylic acid (-COOH) functional group is an amino acid. The proteinogenic amino acids are small subset of this group ...
Calvert AF, Rodwell VW (1966). "Metabolism of pipecolic acid in a Pseudomonas species. 3 L-alpha-aminoadipate delta- ... 241 (2): 409-14. PMID 4285660. Portal: Biology v t e (EC 1.2.1, NADPH-dependent enzymes, NADH-dependent enzymes, Enzymes of ... The systematic name of this enzyme class is L-2-aminoadipate-6-semialdehyde:NAD(P)+ 6-oxidoreductase. Other names in common use ... In enzymology, a L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) is an enzyme that catalyzes the chemical reaction L-2- ...
... quinic acid MeSH D02.241.511.852 - shikimic acid MeSH D02.241.511.902 - sugar acids MeSH D02.241.511.902.107 - ascorbic acid ... edetic acid MeSH D02.241.081.038.455 - egtazic acid MeSH D02.241.081.038.581 - iodoacetic acid MeSH D02.241.081.038.581.400 - ... hexuronic acids MeSH D02.241.081.844.915.400.500 - iduronic acid MeSH D02.241.081.901.177 - aconitic acid MeSH D02.241.081.901. ... muramic acids MeSH D02.241.081.844.562 - neuraminic acids MeSH D02.241.081.844.562.668 - sialic acids MeSH D02.241.081.844. ...
The following amino acid residues are affected: prolyl to pyrrolidone glutamyl to glutamic semialdehyde lysyl to aminoadipic ... acid semialdehyde threonyl to amino ketobutyric acid Carbonylation is typically assumed to be the result of reactive oxygen ... 10 (2): 389-406. doi:10.1111/j.1582-4934.2006.tb00407.x. PMC 3933129. PMID 16796807. Grimsrud, P. A.; Xie, H.; Griffin, T. J.; ...
It has an important function in lysine metabolism and catalyses a reaction in the alpha-Aminoadipic acid pathway. This pathway ... Kumar VP, West AH, Cook PF (June 2012). "Supporting role of lysine 13 and glutamate 16 in the acid-base mechanism of ... is an enzyme involved in the metabolism of the amino acid lysine, via an intermediate substance called saccharopine. The ... 240 (2): 373-9. doi:10.1111/j.1432-1033.1996.0373h.x. PMID 8841401. Andi B, Xu H, Cook PF, West AH (November 2007). "Crystal ...
... lysine is synthesized via alpha-aminoadipic acid not via diaminopimelic acid". Journal of Bacteriology. 181 (6): 1713-1718. doi ... Proteinogenic amino acids, Ketogenic amino acids, Alpha-Amino acids, Basic amino acids, Essential amino acids, Diamines). ... Since the two amino acids are taken up in the intestine, reclaimed in the kidney, and moved into cells by the same amino acid ... Wu G (May 2009). "Amino acids: metabolism, functions, and nutrition". Amino Acids. 37 (1): 1-17. doi:10.1007/s00726-009-0269-0 ...
... and l-α-aminoadipic acid by ACV synthetase (ACVS, a nonribosomal peptide synthetase) and then cyclization of this formed ... Spratt BG, Jobanputra V, Zimmermann W (1977). "Binding of Thienamycin and Clavulanic Acid to the Penicillin-Binding Proteins of ... doi:10.1007/978-1-4614-1400-1_2. ISBN 978-1-4614-1400-1. Kahan JS, Kahan FM, Goegelman R, et al. (1979). "Thienamycin, a new ... "Chapter 2, Rational approaches to antibiotic discovery: pre-genomic directed and phenotypic screening". In Dougherty, T.; Pucci ...
Luna C, Arjona A, Dueñas C, Estevez M (March 2021). "Allysine and α-Aminoadipic Acid as Markers of the Glyco-Oxidative Damage ... Alpha-Amino acids, Aldehydes, Aldehydic acids, All stub articles, Biochemistry stubs). ... The free amino acid does not exist, but the allysine residue does. It is produced by aerobic oxidation of lysine residues by ... Amino Acids. 25 (3-4): 221-226. doi:10.1007/s00726-003-0012-1. PMID 14661085. S2CID 28837698. Eyre, David R.; Paz, Mercedes A ...
In the protein, two amino acid residues, Glu121 and Arg301, are attributed for the binding and catalyzing one of its substrates ... alpha-aminoadipic semialdehyde (α-AASA). Antiquitin shares 60% homology with the 26g pea turgor protein, also referred to as ... Furthermore, antiquitin functions as an aldehyde dehydrogenase for α-AASA in the pipecolic acid pathway of lysine catabolism. ... "Folinic acid-responsive seizures are identical to pyridoxine-dependent epilepsy". Annals of Neurology. 65 (5): 550-6. doi: ...
Plasma and cerebrospinal fluid levels of pipecolic acid are frequently elevated in patients with PDE, though it is a non- ... The ALDH7A1 gene encodes for the enzyme antiquitin or α-aminoadipic semialdehyde dehydrogenase, which is involved with the ... 104 (1-2): 48-60. doi:10.1016/j.ymgme.2011.05.014. PMID 21704546. Shih, JJ; Kornblum, H; Shewmon, DA (September 1996). "Global ...
... aspartic acid MeSH D12.125.067.500.150 - d-aspartic acid MeSH D12.125.067.500.275 - isoaspartic acid MeSH D12.125.067.500.400 ... aspartic acid MeSH D12.125.119.170.150 - d-aspartic acid MeSH D12.125.119.170.275 - isoaspartic acid MeSH D12.125.119.170.400 ... aspartic acid MeSH D12.125.427.300 - glutamic acid MeSH D12.125.481.100 - allylglycine MeSH D12.125.481.700 - n-substituted ... imino acids MeSH D12.125.072.401.200 - azetidinecarboxylic acid MeSH D12.125.072.401.623 - proline MeSH D12.125.072.401.623.270 ...
The first step is the condensation of three amino acids-L-α-aminoadipic acid, L-cysteine, L-valine into a tripeptide. Before ... α-ketoglutarate + AcCoA → homocitrate → L-α-aminoadipic acid → L-lysine + β-lactam The Penicillium cells are grown using a ... 6-Aminopenicillanic acid (6-APA) is a compound derived from penicillin G. 6-APA contains the beta-lactam core of penicillin G, ... Penicillin V can be taken by mouth because it is relatively resistant to stomach acid. Doses higher than 500 mg are not fully ...
... and synthesis of lysine by the α-amino adipic acid (AAA) pathway. Chytrids are saprobic, degrading refractory materials such as ... 67 (2): 91-105. doi:10.3354/ame01592. Freeman, K.R. (2009). "Evidence that chytrids dominate fungal communities in high- ... 77 (2): 113-118. doi:10.3354/dao01838. PMID 17972752. "A salty cure for a deadly frog disease". Australian Broadcasting ... 107 (2): 419-431. doi:10.3852/14-223. PMID 25572098. S2CID 24144836. Retrieved 23 August 2016. Dee, J.M.; Mollicone, M.; ...
Cephalosporin C contains a side-chain which is derived from D-aminoadipic acid. Modification of side chains on the relevant ... The amino acid sequence of D-alanyl-D-alanine is recognized by the transpeptidase at the end of the peptide chain. The enzyme ... The core itself can also be referred to as 7-aminocephalosporanic acid which can be derived by hydrolysis from the natural ... 7-ACA is analogous to 6-aminopenicillanic acid (6-APA), a starting block for making several derivatives of penicillins. In 1959 ...
... particularly branched-chain amino acids, keto acids, and other catabolism metabolites. ... The LR diet increased concentrations of fecal and plasma total short-chain fatty acids, primarily acetate, and there was a ... Plasma and fecal short-chain fatty acids were targeted and quantified. Fecal microbiota was analyzed using genomic sequencing. ... n-caproic acid, heptanoic acid, sorbic acid, benzoic acid, DL-lactic acid, succinic acid, and hippuric acid. Total fecal ...
The AASS gene provides instructions for making an enzyme called aminoadipic semialdehyde synthase. Learn about this gene and ... Aminoadipic semialdehyde synthase is involved in the breakdown of the amino acid lysine, a building block of most proteins. It ... Most of these mutations change single amino acids in aminoadipic semialdehyde synthase. These mutations are thought to decrease ... The AASS gene provides instructions for making an enzyme called aminoadipic semialdehyde synthase. This enzyme is found in most ...
Association of alpha-aminoadipic acid (2-AAA) with cardiometabolic risk factors in healthy and high-risk individuals. ... Association of alpha-aminoadipic acid with cardiometabolic risk factors in healthy and high-risk individuals. ... Plasma levels of the metabolite alpha-aminoadipic acid (2-AAA) have been associated with risk of type 2 diabetes (T2D) and ... Introduction: Plasma levels of the metabolite alpha-aminoadipic acid (2-AAA) have been associated with risk of type 2 diabetes ...
... amino acid, heme, and neurotransmitter metabolism. Pyridoxine deficiency causes blood, skin, and nerve changes. ... Disorders of beta- and gamma-amino acids in free and peptide-linked forms. Scriver CR, Beaudet A, Sly W, et al, eds. The ... 7] Consensus guidelines have been issued for the diagnosis and management of pyridoxine-dependent epilepsy due to α-aminoadipic ... PLP is a cofactor for glutamic acid decarboxylase, the enzyme that produces GABA, such that PLP deficiency results in ...
99mTc-Dimercaptosuccinic Acid use Technetium Tc 99m Dimercaptosuccinic Acid 99mTc-DMSA use Technetium Tc 99m Dimercaptosuccinic ... 12-S-HETE use 12-Hydroxy-5.8,10,14-eicosatetraenoic Acid 12-S-Hydroxyeicosatetraenoic Acid use 12-Hydroxy-5.8,10,14- ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... 99mTc-Diethyl IDA use Technetium Tc 99m Diethyl-iminodiacetic Acid ...
99mTc-Dimercaptosuccinic Acid use Technetium Tc 99m Dimercaptosuccinic Acid 99mTc-DMSA use Technetium Tc 99m Dimercaptosuccinic ... 12-S-HETE use 12-Hydroxy-5.8,10,14-eicosatetraenoic Acid 12-S-Hydroxyeicosatetraenoic Acid use 12-Hydroxy-5.8,10,14- ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... 99mTc-Diethyl IDA use Technetium Tc 99m Diethyl-iminodiacetic Acid ...
99mTc-Dimercaptosuccinic Acid use Technetium Tc 99m Dimercaptosuccinic Acid 99mTc-DMSA use Technetium Tc 99m Dimercaptosuccinic ... 12-S-HETE use 12-Hydroxy-5.8,10,14-eicosatetraenoic Acid 12-S-Hydroxyeicosatetraenoic Acid use 12-Hydroxy-5.8,10,14- ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... 99mTc-Diethyl IDA use Technetium Tc 99m Diethyl-iminodiacetic Acid ...
99mTc-Dimercaptosuccinic Acid use Technetium Tc 99m Dimercaptosuccinic Acid 99mTc-DMSA use Technetium Tc 99m Dimercaptosuccinic ... 12-S-HETE use 12-Hydroxy-5.8,10,14-eicosatetraenoic Acid 12-S-Hydroxyeicosatetraenoic Acid use 12-Hydroxy-5.8,10,14- ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... 99mTc-Diethyl IDA use Technetium Tc 99m Diethyl-iminodiacetic Acid ...
99mTc-Dimercaptosuccinic Acid use Technetium Tc 99m Dimercaptosuccinic Acid 99mTc-DMSA use Technetium Tc 99m Dimercaptosuccinic ... 12-S-HETE use 12-Hydroxy-5.8,10,14-eicosatetraenoic Acid 12-S-Hydroxyeicosatetraenoic Acid use 12-Hydroxy-5.8,10,14- ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... 99mTc-Diethyl IDA use Technetium Tc 99m Diethyl-iminodiacetic Acid ...
99mTc-Dimercaptosuccinic Acid use Technetium Tc 99m Dimercaptosuccinic Acid 99mTc-DMSA use Technetium Tc 99m Dimercaptosuccinic ... 12-S-HETE use 12-Hydroxy-5.8,10,14-eicosatetraenoic Acid 12-S-Hydroxyeicosatetraenoic Acid use 12-Hydroxy-5.8,10,14- ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... 99mTc-Diethyl IDA use Technetium Tc 99m Diethyl-iminodiacetic Acid ...
99mTc-Dimercaptosuccinic Acid use Technetium Tc 99m Dimercaptosuccinic Acid 99mTc-DMSA use Technetium Tc 99m Dimercaptosuccinic ... 12-S-HETE use 12-Hydroxy-5.8,10,14-eicosatetraenoic Acid 12-S-Hydroxyeicosatetraenoic Acid use 12-Hydroxy-5.8,10,14- ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... 99mTc-Diethyl IDA use Technetium Tc 99m Diethyl-iminodiacetic Acid ...
99mTc-Dimercaptosuccinic Acid use Technetium Tc 99m Dimercaptosuccinic Acid 99mTc-DMSA use Technetium Tc 99m Dimercaptosuccinic ... 12-S-HETE use 12-Hydroxy-5.8,10,14-eicosatetraenoic Acid 12-S-Hydroxyeicosatetraenoic Acid use 12-Hydroxy-5.8,10,14- ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... 99mTc-Diethyl IDA use Technetium Tc 99m Diethyl-iminodiacetic Acid ...
99mTc-Dimercaptosuccinic Acid use Technetium Tc 99m Dimercaptosuccinic Acid 99mTc-DMSA use Technetium Tc 99m Dimercaptosuccinic ... 12-S-HETE use 12-Hydroxy-5.8,10,14-eicosatetraenoic Acid 12-S-Hydroxyeicosatetraenoic Acid use 12-Hydroxy-5.8,10,14- ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... 99mTc-Diethyl IDA use Technetium Tc 99m Diethyl-iminodiacetic Acid ...
99mTc-Dimercaptosuccinic Acid use Technetium Tc 99m Dimercaptosuccinic Acid 99mTc-DMSA use Technetium Tc 99m Dimercaptosuccinic ... 12-S-HETE use 12-Hydroxy-5.8,10,14-eicosatetraenoic Acid 12-S-Hydroxyeicosatetraenoic Acid use 12-Hydroxy-5.8,10,14- ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... 99mTc-Diethyl IDA use Technetium Tc 99m Diethyl-iminodiacetic Acid ...
99mTc-Dimercaptosuccinic Acid use Technetium Tc 99m Dimercaptosuccinic Acid 99mTc-DMSA use Technetium Tc 99m Dimercaptosuccinic ... 12-S-HETE use 12-Hydroxy-5.8,10,14-eicosatetraenoic Acid 12-S-Hydroxyeicosatetraenoic Acid use 12-Hydroxy-5.8,10,14- ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... 99mTc-Diethyl IDA use Technetium Tc 99m Diethyl-iminodiacetic Acid ...
99mTc-Dimercaptosuccinic Acid use Technetium Tc 99m Dimercaptosuccinic Acid 99mTc-DMSA use Technetium Tc 99m Dimercaptosuccinic ... 12-S-HETE use 12-Hydroxy-5.8,10,14-eicosatetraenoic Acid 12-S-Hydroxyeicosatetraenoic Acid use 12-Hydroxy-5.8,10,14- ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... 99mTc-Diethyl IDA use Technetium Tc 99m Diethyl-iminodiacetic Acid ...
99mTc-Dimercaptosuccinic Acid use Technetium Tc 99m Dimercaptosuccinic Acid 99mTc-DMSA use Technetium Tc 99m Dimercaptosuccinic ... 12-S-HETE use 12-Hydroxy-5.8,10,14-eicosatetraenoic Acid 12-S-Hydroxyeicosatetraenoic Acid use 12-Hydroxy-5.8,10,14- ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... 99mTc-Diethyl IDA use Technetium Tc 99m Diethyl-iminodiacetic Acid ...
L-alpha-aminoadipic acid, induces depressive-like symptoms in rats, suggesting that astroglial loss is pathogenic in MDD [41]. ... microglia quinolinic acid that is Th1 response-mediated or astroglial kynurenic acid (KYNA) (Figure 1) that is Th2 response- ... Table 1 Clinical features of anti-synaptic and anti-glutamic acid decarboxylase autoimmune encephalitides Full size table. ... omega-3 supplements containing eicosapentaenoic acid ≥60% (dose range 200 to 2,200 mg/d in excess of the docosahexaenoic acid ...
Genetic Architecture of Plasma Alpha-Aminoadipic Acid Reveals a Relationship With High-Density Lipoprotein Cholesterol. Journal ... Nature communications 2022 2 13 (1): 855. Boua Palwende Romuald, Brandenburg Jean-Tristan, Choudhury Ananyo, Sorgho Hermann, ... Multiethnic Genome-Wide Association Study of Subclinical Atherosclerosis in Individuals With Type 2 Diabetes. Circulation. ... Kidney international 2021 4 100 (2): 430-439. Luo Shengyuan, Feofanova Elena V, Tin Adrienne, Tung Sarah, Rhee Eugene P, Coresh ...
Responsible for the balance between formation of cholic acid and chenodeoxycholic acid. Has a rather broad substrate ... Involved in bile acid synthesis and is responsible for the conversion of 7 alpha-hydroxy-4-cholesten-3-one into 7 alpha, 12 ... Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl ... Acetyl-coenzyme A synthetase 2-like, mitochondrial. Gene Name: ACSS1. Important for maintaining normal body temperature during ...
VIGADRONE may increase the amount of amino acids in the urine, possibly leading to a false positive test for certain rare ... genetic metabolic diseases (e.g., alpha aminoadipic aciduria).. Drug Abuse And Dependence. Controlled Substance. Vigabatrin is ... The chemical name of vigabatrin, a racemate consisting of two enantiomers, is (±) 4-amino-5-hexenoic acid. The molecular ... but it is believed to be the result of its action as an irreversible inhibitor of γ-aminobutyric acid transaminase (GABA-T), ...
branched-chain keto acid dehydrogenase kinase deficiency Branchiogenic-Deafness Syndrome branchiooculofacial syndrome ... Annotations: Rat: (2) Mouse: (2) Human: (2) Chinchilla: (2) Bonobo: (2) Dog: (2) Squirrel: (2) Pig: (2) ... autosomal recessive pyridoxine-refractory sideroblastic anemia 2 autosomal recessive pyridoxine-refractory sideroblastic anemia ... Developmental Delay with Short Stature, Dysmorphic Facial Features, and Sparse Hair 2 ...
... aminoadipic and $\gamma$-glutamic semialdehyde residues", Analytical and bioanalytical chemistry, vol. 398, pp. 2905-2914, 2010 ... relationships of the main bioactive constituents of Euodia ruticarpa on aryl hydrocarbon receptor activation and bile acid ... 2-c] pyrimidine and benzo [4, 5] imidazo [1, 2-a] pyrazine derivatives as anaplastic lymphoma kinase inhibitors", Bioorganic & ... "Site-specific proteomic analysis of lipoxidation adducts in cardiac mitochondria reveals chemical diversity of 2-alkenal ...
"Cover crop-altered vine nitrogen status and its effect on growth hormones and amino acid content of Pinot Noir berries", Food ... aminoadipic and $\gamma$-glutamic semialdehyde residues", Analytical and bioanalytical chemistry, vol. 398, pp. 2905-2914, 2010 ... "Site-specific proteomic analysis of lipoxidation adducts in cardiac mitochondria reveals chemical diversity of 2-alkenal ...
  • The AASS gene provides instructions for making an enzyme called aminoadipic semialdehyde synthase. (medlineplus.gov)
  • Aminoadipic semialdehyde synthase is involved in the breakdown of the amino acid lysine, a building block of most proteins. (medlineplus.gov)
  • Most of these mutations change single amino acids in aminoadipic semialdehyde synthase. (medlineplus.gov)
  • Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities. (medlineplus.gov)
  • Subsequent studies showed elevated pipecolic acid levels in the plasma and cerebrospinal fluid of affected patients and this led to the recognition of a defect in aaminoadipic semialdehyde (a-AASA) dehydrogenase (antiquitin) in the cerebral lysine degradation pathway, and mutations in the antiquitin gene (ALDH7A1) on chromosome 5q31. (medscape.com)
  • Circulation 2023 2 147 (12): 942-955. (cdc.gov)
  • Introduction: Plasma levels of the metabolite alpha-aminoadipic acid (2-AAA) have been associated with risk of type 2 diabetes (T2D) and atherosclerosis. (bvsalud.org)
  • We examined associations between plasma 2-AAA and markers of cardiometabolic health within each cohort. (bvsalud.org)
  • The AASS gene provides instructions for making an enzyme called aminoadipic semialdehyde synthase. (medlineplus.gov)
  • Aminoadipic semialdehyde synthase is involved in the breakdown of the amino acid lysine, a building block of most proteins. (medlineplus.gov)
  • Most of these mutations change single amino acids in aminoadipic semialdehyde synthase. (medlineplus.gov)
  • Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities. (medlineplus.gov)
  • 3. Deletion of 2-aminoadipic semialdehyde synthase limits metabolite accumulation in cell and mouse models for glutaric aciduria type 1. (nih.gov)
  • [ 1 ] Products of these reactions include chlorinated compounds, such as 3-chlorotyrosine, 2-chlorotryptophan, or chlorinated lysine residues, as well as hydroxylated compounds such as 3-hydroxyphenylalanine and hydroxytryptophan. (medscape.com)
  • Subsequent studies showed elevated pipecolic acid levels in the plasma and cerebrospinal fluid of affected patients and this led to the recognition of a defect in aaminoadipic semialdehyde (a-AASA) dehydrogenase (antiquitin) in the cerebral lysine degradation pathway, and mutations in the antiquitin gene (ALDH7A1) on chromosome 5q31. (medscape.com)
  • 2. Therapeutic modulation of cerebral L-lysine metabolism in a mouse model for glutaric aciduria type I. (nih.gov)
  • 4. Elevated glutaric acid levels in Dhtkd1-/Gcdh- double knockout mice challenge our current understanding of lysine metabolism. (nih.gov)
  • 14. Safety, efficacy and physiological actions of a lysine-free, arginine-rich formula to treat glutaryl-CoA dehydrogenase deficiency: focus on cerebral amino acid influx. (nih.gov)
  • This gene encodes a component of a mitochondrial 2-oxoglutarate-dehydrogenase-complex-like protein involved in the degradation pathways of several amino acids, including lysine. (nih.gov)
  • Mutations in this gene are associated with 2-aminoadipic 2-oxoadipic aciduria and Charcot-Marie-Tooth Disease Type 2Q. (nih.gov)
  • Thus, many of the oxidized amino acids are nonspecific advanced oxidation products of proteins (AOPPs). (medscape.com)
  • They found an increase in the levels of halogenated proteins in the renal glomerular and tubular regions in two mouse models of type 2 and type 1 diabetes, respectively. (medscape.com)
  • Previous work with the nephrotoxic and mitochondrial-targeting toxicant S-(1,2-dichlorovinyl)-L-cysteine (DCVC) confirmed that a large proportion (43%) of proteins recovered in the extracellular medium was of mitochondrial origin. (nih.gov)
  • 9. The measurement of urinary Δ¹-piperideine-6-carboxylate, the alter ego of α-aminoadipic semialdehyde, in Antiquitin deficiency. (nih.gov)
  • In vivo, bleach formation requires an enzyme bound Fe(IV)-oxo complex, H 2 O 2 , and halogen ions. (medscape.com)
  • The importance of bleach in biology has been known for almost 50 years, starting with the discovery of myeloperoxidase (MPO), an enzyme that uses H 2 O 2 to oxidize chloride, yielding the potent bactericidal agent, HOCl. (medscape.com)
  • This mechanism involves bleach, H 2 O 2 , and VPO-1/peroxidasin, an enzyme that was discovered in drosophila just 10 years ago. (medscape.com)
  • It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). (nih.gov)
  • The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). (nih.gov)
  • In diabetes, the H 2 O 2 comes from mitochondria or NADPH oxidase, as well as from plasma amine oxidase and xanthine oxidase. (medscape.com)
  • To investigate the potential impact of hypohalous acids on renal basement membrane collagen in diabetes, Brown et al. (medscape.com)
  • This triggered the question of whether collateral damage to other amino acids of the NC1 hexamer complex occurs in the diabetic kidney. (medscape.com)