An enzyme that catalyzes the decarboxylation of S-adenosyl-L-methionine to yield 5'-deoxy-(5'-),3-aminopropyl-(1), methylsulfonium salt. It is one of the enzymes responsible for the synthesis of spermidine from putrescine. EC
Antineoplastic agent effective against myelogenous leukemia in experimental animals. Also acts as an inhibitor of animal S-adenosylmethionine decarboxylase.
Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.
Polyamines are organic compounds with more than one amino group, involved in various biological processes such as cell growth, differentiation, and apoptosis, and found to be increased in certain diseases including cancer.
A toxic diamine formed by putrefaction from the decarboxylation of arginine and ornithine.
Physiologic methyl radical donor involved in enzymatic transmethylation reactions and present in all living organisms. It possesses anti-inflammatory activity and has been used in treatment of chronic liver disease. (From Merck, 11th ed)
A pyridoxal-phosphate protein, believed to be the rate-limiting compound in the biosynthesis of polyamines. It catalyzes the decarboxylation of ornithine to form putrescine, which is then linked to a propylamine moiety of decarboxylated S-adenosylmethionine to form spermidine.
A polyamine formed from putrescine. It is found in almost all tissues in association with nucleic acids. It is found as a cation at all pH values, and is thought to help stabilize some membranes and nucleic acid structures. It is a precursor of spermine.
Organic chemicals which have two amino groups in an aliphatic chain.
5'-S-(3-Amino-3-carboxypropyl)-5'-thioadenosine. Formed from S-adenosylmethionine after transmethylation reactions.
A pyridoxal-phosphate protein that catalyzes the alpha-decarboxylation of L-glutamic acid to form gamma-aminobutyric acid and carbon dioxide. The enzyme is found in bacteria and in invertebrate and vertebrate nervous systems. It is the rate-limiting enzyme in determining GAMMA-AMINOBUTYRIC ACID levels in normal nervous tissues. The brain enzyme also acts on L-cysteate, L-cysteine sulfinate, and L-aspartate. EC
One of the AROMATIC-L-AMINO-ACID DECARBOXYLASES, this enzyme is responsible for the conversion of DOPA to DOPAMINE. It is of clinical importance in the treatment of Parkinson's disease.
An enzyme that catalyzes the decarboxylation of histidine to histamine and carbon dioxide. It requires pyridoxal phosphate in animal tissues, but not in microorganisms. EC
A sulfur-containing essential L-amino acid that is important in many body functions.
Addition of methyl groups. In histo-chemistry methylation is used to esterify carboxyl groups and remove sulfate groups by treating tissue sections with hot methanol in the presence of hydrochloric acid. (From Stedman, 25th ed)
An enzyme that catalyzes the decarboxylation of UROPORPHYRINOGEN III to coproporphyrinogen III by the conversion of four acetate groups to four methyl groups. It is the fifth enzyme in the 8-enzyme biosynthetic pathway of HEME. Several forms of cutaneous PORPHYRIAS are results of this enzyme deficiency as in PORPHYRIA CUTANEA TARDA; and HEPATOERYTHROPOIETIC PORPHYRIA.
Orotidine-5'-phosphate carboxy-lyase. Catalyzes the decarboxylation of orotidylic acid to yield uridylic acid in the final step of the pyrimidine nucleotide biosynthesis pathway. EC
A pyridoxal-phosphate protein that catalyzes the conversion of L-tyrosine to tyramine and carbon dioxide. The bacterial enzyme also acts on 3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine. (From Enzyme Nomenclature, 1992) EC
An inhibitor of ORNITHINE DECARBOXYLASE, the rate limiting enzyme of the polyamine biosynthetic pathway.
An enzyme group with broad specificity. The enzymes decarboxylate a range of aromatic amino acids including dihydroxyphenylalanine (DOPA DECARBOXYLASE); TRYPTOPHAN; and HYDROXYTRYPTOPHAN.

A new method for the assay of tissue. S-adenosylhomocysteine and S-adenosylmethione. Effect of pyridoxine deficiency on the metabolism of S-adenosylhomocysteine, S-adenosylmethionine and polyamines in rat liver. (1/292)

The hepatic synthesis and accumulation of S-adenosylhomocysteine, S-adenosylmethionine and polyamines were studied in normal and vitamin B-6-deficient male albino rats. A method involving a single chromatography on a phosphocellulose column was developed for the determination of S-adenosylhomocysteine and S-adenosylmethionine from tissue samples. Feeding the rat with pyridoxine-deficient diet for 3 or 6 weeks resulted in a four- to five-fold increase in the concentration of S-adenosylhomocysteine, whereas that of S-adenosylmethionine was only slighly elevated. The concentration of putrescine was decreased to half, that of spermidine was somewhat decreased and that of spermine remained fairly constant. The activities of L-ornithine decarboxylase, S-adenosyl-L-methionine decarboxylase, L-methionine adenosyltransferase and S-adenosyl-L-homocysteine hydrolase were moderately increased. S-Adenosylmethionine decarboxylase showed no requirement for pyridoxal 5'-phosphate. The major effect of pyridoxine deficiency of S-adenosylmethionine metabolism seems to be a block in the utilization of S-adenosylhomocysteine, resulting in the accumulation of this metabolite to a concentration that may inhibit biological methylation reactions.  (+info)

Agmatine modulates polyamine content in hepatocytes by inducing spermidine/spermine acetyltransferase. (2/292)

Agmatine has been proposed as the physiological ligand for the imidazoline receptors. It is not known whether it is also involved in the homoeostasis of intracellular polyamine content. To show whether this is the case, we have studied the effect of agmatine on rat liver cells, under both periportal and perivenous conditions. It is shown that agmatine modulates intracellular polyamine content through its effect on the synthesis of the limiting enzyme of the interconversion pathway, spermidine/spermine acetyltransferase (SSAT). Increased SSAT activity is accompanied by depletion of spermidine and spermine, and accumulation of putrescine and N1-acetylspermidine. Immunoblotting with a specific polyclonal antiserum confirms the induction. At the same time S-adenosylmethionine decarboxylase activity is significantly increased, while ornithine decarboxylase (ODC) activity and the rate of spermidine uptake are reduced. This is not due to an effect on ODC antizyme, which is not significantly changed. All these modifications are observed in HTC cells also, where they are accompanied by a decrease in proliferation rate. SSAT is also induced by low oxygen tension which mimics perivenous conditions. The effect is synergic with that promoted by agmatine.  (+info)

Mechanistic studies of the processing of human S-adenosylmethionine decarboxylase proenzyme. Isolation of an ester intermediate. (3/292)

Human S-adenosylmethionine decarboxylase is synthesized as a proenzyme that undergoes an autocatalytic cleavage reaction generating the alpha and beta subunits and forming the pyruvate prosthetic group, which is derived from an internal Ser residue (Ser-68). The mechanism of this processing reaction was studied using site-directed mutagenesis of conserved residues (His-243 and Ser-229) located close to the cleavage site. Mutant S229A failed to process, and mutant S229C cleaved very slowly, whereas mutant S229T processed normally, suggesting that the hydroxyl group of residue 229 is required for the processing reaction where Ser-229 may act as a proton acceptor. Mutant His-243A cleaved very slowly, forming a small amount of the correctly processed pyruvoyl enzyme but a much larger proportion of the alpha subunit with an amino-terminal Ser. The cleavage to form the latter was greatly enhanced by hydroxylamine. This result suggests that the N-O acyl shift needed for ester formation occurs normally in this mutant but that the next step, which is a beta-elimination reaction leading to the two subunits, does not occur. His-243 may therefore act as the basic residue that extracts the hydrogen of the alpha-carbon of Ser-68 in the ester in order to facilitate this reaction. The availability of the recombinant H243A S-adenosylmethionine decarboxylase proenzyme provides a useful model system to examine the processing reaction in vitro and test the design of specific inactivators aimed at blocking the production of the pyruvoyl prosthetic group.  (+info)

Identification of functionally important residues of Arabidopsis thaliana S-adenosylmethionine decarboxylase. (4/292)

The Arabidopsis thaliana S-adenosylmethionine decarboxylase (AdoMetDC) cDNA (GenBank(TM) U63633) was cloned, and the AdoMetDC protein was expressed, purified, and characterized. The K(m) value for S-adenosylmethionine (AdoMet) is 23.1 microM and the K(i) value for methylglyoxal bis-(guanylhydrazone) (MGBG) is 0.15 microM. Site-specific mutagenesis was performed on the AdoMetDC to introduce mutations at conserved cysteine (Cys(50), Cys(83), and Cys(230)) and lysine(81) residues, chosen by examination of the conserved sequence and proved to be involved in enzymatic activity by chemical modification. The AdoMetDC mutants K81A and C83A retained up to 60 and 10% of wild type activity, respectively, demonstrating that lysyl and sulfhydryl groups are required for full catalytic activity. However, changing Cys(50) and Cys(230) to alanine had minimal effects on the catalytic activity. Changing Lys(81) to alanine produced an altered substrate specificity. When lysine was used as a substrate instead of AdoMet, the substrate specificity for lysine increased 6-fold. The K(m) value for AdoMet is 11-fold higher than that of the wild type, but the V(max) value is more than 60%. Taken together, the results suggest that the lysine(81) residue is critical for substrate binding.  (+info)

Putrescine does not support the migration and growth of IEC-6 cells. (5/292)

The migration of IEC-6 cells is inhibited when the cells are depleted of polyamines by inhibiting ornithine decarboxylase with alpha-difluoromethylornithine (DFMO). Exogenous putrescine, spermidine, and spermine completely restore cell migration inhibited by DFMO. Because polyamines are interconverted during their synthesis and catabolism, the specific role of individual polyamines in intestinal cell migration, as well as growth, remains unclear. In this study, we used an inhibitor of S-adenosylmethionine decarboxylase, diethylglyoxal bis(guanylhydrazone)(DEGBG), to block the synthesis of spermidine and spermine from putrescine. We found that exogenous putrescine does not restore migration and growth of IEC-6 cells treated with DFMO plus DEGBG, whereas exogenous spermine does. In addition, the normal distribution of actin filaments required for migration, which is disrupted in polyamine-deficient cells, could be achieved by adding spermine but not putrescine along with DFMO and DEGBG. These results indicate that putrescine, by itself, is not essential for migration and growth, but that it is effective because it is converted into spermidine and/or spermine.  (+info)

Tumor progression is accompanied by significant changes in the levels of expression of polyamine metabolism regulatory genes and clusterin (sulfated glycoprotein 2) in human prostate cancer specimens. (6/292)

Using Northern blotting, the expression levels of the genes for polyamine metabolism regulatory proteins and clusterin have been measured in a series of 23 human prostate cancers (CaPs) dissected from radical prostatectomy specimens. Patient matched, nontumor tissue was dissected from benign areas of the gland. The results indicate that transcripts encoding ornithine decarboxylase (ODC), ODC antizyme, adenosylmethionine decarboxylase, and spermidine/spermine N1-acetyltransferase (SSAT) were significantly higher, whereas clusterin (sulfated glycoprotein 2) mRNA was significantly lower in tumors compared with the benign tissue. All mRNA levels were compared with those of histone H3 and growth arrest-specific gene 1, markers of cell proliferation and cell quiescence, respectively, and glyceraldehyde 3-phosphate dehydrogenase, a housekeeping gene. In poorly differentiated and locally invasive CaPs and in tumors with unfavorable prognosis or total prostate-specific antigen (PSA) levels > 10.0 ng/ml at diagnosis, an overall increase in the levels of H3 mRNA and a decrease in growth arrest-specific gene 1 mRNA was detected, indicative of higher proliferation activity, whereas the differences in expression levels for the polyamine metabolism and clusterin genes were higher. ODC and SSAT changes were positively correlated in normal tissue but not in high-grade cancer, whereas ODC antizyme and SSAT changes were positively correlated in more malignant CaPs but not in normal tissue. Tumor classification based on the changes in expression levels of all of the genes studied could be correlated to differentiation grade and local invasiveness classification systems in 72.2 and 83.3% of the cases, respectively. In a 1-year follow-up period, three patients whose CaPs ranked as less aggressive according to clinical staging, but classified as advanced cancers with the proposed molecular classification, showed increases in total PSA levels, indicative of tumor relapse. Thus, molecular classification, based on gene expression, may enhance the available prognostic tools for prostate tumors.  (+info)

Changes in gene expression in response to polyamine depletion indicates selective stabilization of mRNAs. (7/292)

We used differential display analysis to identify mRNAs responsive to changes in polyamine synthesis. As an overproducing model we used the kidneys of transgenic hybrid mice overexpressing ornithine decarboxylase and S-adenosylmethionine decarboxylase, two key enzymes in polyamine biosynthesis. To identify mRNAs that respond to polyamine starvation, we treated Rat-2 cells with alpha-difluoromethylornithine, a specific inhibitor of polyamine biosynthesis. We isolated 41 partial cDNA clones, representing 37 differentially expressed mRNAs. Of these, 15 have similarity with known genes, five appear to be similar to reported expressed sequence tags and seventeen clones were novel sequences. Of the 35 mRNAs expressed differentially after alpha-difluoromethylornithine treatment, 26 were up-regulated. The expression of only three mRNAs was altered in the transgenic animals and all three were down-regulated. Determination of mRNA half-life of three of the mRNAs up-regulated in response to polyamine depletion revealed that the accumulation results from stabilization of the messages. Because most of the transcripts identified from Rat-2 cells suffering polyamine starvation were accumulated, we conclude that polyamine depletion, while blocking cell growth, is stabilizing mRNAs. This may be due to the lack of spermidine for post-translational modification of the eukaryotic initiation factor 5A, which plays a major role in mRNA turnover. The coupling of mRNA stabilization with cell-growth arrest in response to polyamine starvation provides cells with an economical way to resume growth after recovery from polyamine deficiency.  (+info)

In the human malaria parasite Plasmodium falciparum, polyamines are synthesized by a bifunctional ornithine decarboxylase, S-adenosylmethionine decarboxylase. (8/292)

The polyamines putrescine, spermidine, and spermine are crucial for cell differentiation and proliferation. Interference with polyamine biosynthesis by inhibition of the rate-limiting enzymes ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) has been discussed as a potential chemotherapy of cancer and parasitic infections. Usually both enzymes are individually transcribed and highly regulated as monofunctional proteins. We have isolated a cDNA from the malaria parasite Plasmodium falciparum that encodes both proteins on a single open reading frame, with the AdoMetDC domain in the N-terminal region connected to a C-terminal ODC domain by a hinge region. The predicted molecular mass of the entire transcript is 166 kDa. The ODC/AdoMetDC coding region was subcloned into the expression vector pASK IBA3 and transformed into the AdoMetDC- and ODC-deficient Escherichia coli cell line EWH331. The resulting recombinant protein exhibited both AdoMetDC and ODC activity and co-eluted after gel filtration on Superdex S-200 at approximately 333 kDa, which is in good agreement with the molecular mass of approximately 326 kDa determined for the native protein from isolated P. falciparum. SDS-polyacrylamide gel electrophoresis analysis of the recombinant ODC/AdoMetDC revealed a heterotetrameric structure of the active enzyme indicating processing of the AdoMetDC domain. The data presented describe the occurrence of a unique bifunctional ODC/AdoMetDC in P. falciparum, an organization which is possibly exploitable for the design of new antimalarial drugs.  (+info)

Adenosylmethionine decarboxylase (AdoMetDC) is an enzyme that plays a crucial role in the biosynthesis of polyamines, which are essential molecules for cell growth and differentiation. The enzyme catalyzes the decarboxylation of S-adenosylmethionine (SAM) to produce decarboxylated SAM, also known as deoxyadenosylcobalamin or coenzyme M.

Decarboxylated SAM serves as an aminopropyl group donor in the biosynthesis of polyamines such as spermidine and spermine. These polyamines are involved in various cellular processes, including DNA replication, transcription, translation, protein synthesis, and cell signaling.

AdoMetDC is a pyridoxal-5'-phosphate (PLP)-dependent enzyme that requires the cofactor vitamin B12 for its activity. It is found in various organisms, including bacteria, yeast, plants, and animals. In humans, AdoMetDC is encoded by the AMD1 gene and is localized mainly in the cytosol of cells.

Dysregulation of AdoMetDC activity has been implicated in several diseases, such as cancer, neurodegenerative disorders, and cardiovascular diseases. Therefore, targeting AdoMetDC with inhibitors or activators has emerged as a potential therapeutic strategy for treating these conditions.

Mitoguazone is not typically referred to as a medical "definition" but rather it is a chemical compound that has been investigated for its potential therapeutic benefits. It's also known as NSC 3852 and is an antineoplastic agent, which means it is used to treat cancer.

Mitoguazone works by inhibiting the synthesis of DNA, RNA, and proteins in cancer cells, which can ultimately lead to cell death. It has been studied in clinical trials for the treatment of various types of cancer, including brain tumors and leukemia. However, its development as a therapeutic agent was discontinued due to its toxicity and lack of efficacy in later-stage clinical trials.

Therefore, while mitoguazone is not a medical definition per se, it is a chemical compound with known pharmacological properties and a history of investigation for cancer therapy.

Carboxy-lyases are a class of enzymes that catalyze the removal of a carboxyl group from a substrate, often releasing carbon dioxide in the process. These enzymes play important roles in various metabolic pathways, such as the biosynthesis and degradation of amino acids, sugars, and other organic compounds.

Carboxy-lyases are classified under EC number 4.2 in the Enzyme Commission (EC) system. They can be further divided into several subclasses based on their specific mechanisms and substrates. For example, some carboxy-lyases require a cofactor such as biotin or thiamine pyrophosphate to facilitate the decarboxylation reaction, while others do not.

Examples of carboxy-lyases include:

1. Pyruvate decarboxylase: This enzyme catalyzes the conversion of pyruvate to acetaldehyde and carbon dioxide during fermentation in yeast and other organisms.
2. Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO): This enzyme is essential for photosynthesis in plants and some bacteria, as it catalyzes the fixation of carbon dioxide into an organic molecule during the Calvin cycle.
3. Phosphoenolpyruvate carboxylase: Found in plants, algae, and some bacteria, this enzyme plays a role in anaplerotic reactions that replenish intermediates in the citric acid cycle. It catalyzes the conversion of phosphoenolpyruvate to oxaloacetate and inorganic phosphate.
4. Aspartate transcarbamylase: This enzyme is involved in the biosynthesis of pyrimidines, a class of nucleotides. It catalyzes the transfer of a carboxyl group from carbamoyl aspartate to carbamoyl phosphate, forming cytidine triphosphate (CTP) and fumarate.
5. Urocanase: Found in animals, this enzyme is involved in histidine catabolism. It catalyzes the conversion of urocanate to formiminoglutamate and ammonia.

Polyamines are organic compounds with more than one amino group (-NH2) and at least one carbon atom bonded to two or more amino groups. They are found in various tissues and fluids of living organisms and play important roles in many biological processes, such as cell growth, differentiation, and apoptosis (programmed cell death). Polyamines are also involved in the regulation of ion channels and transporters, DNA replication and gene expression. The most common polyamines found in mammalian cells are putrescine, spermidine, and spermine. They are derived from the decarboxylation of amino acids such as ornithine and methionine. Abnormal levels of polyamines have been associated with various pathological conditions, including cancer and neurodegenerative diseases.

Putrescine is an organic compound with the chemical formula NH2(CH2)4NH2. It is a colorless, viscous liquid that is produced by the breakdown of amino acids in living organisms and is often associated with putrefaction, hence its name. Putrescine is a type of polyamine, which is a class of organic compounds that contain multiple amino groups.

Putrescine is produced in the body through the decarboxylation of the amino acid ornithine by the enzyme ornithine decarboxylase. It is involved in various cellular processes, including the regulation of gene expression and cell growth. However, at high concentrations, putrescine can be toxic to cells and has been implicated in the development of certain diseases, such as cancer.

Putrescine is also found in various foods, including meats, fish, and some fruits and vegetables. It contributes to the unpleasant odor that develops during spoilage, which is why putrescine is often used as an indicator of food quality and safety.

S-Adenosylmethionine (SAMe) is a physiological compound involved in methylation reactions, transulfuration pathways, and aminopropylation processes in the body. It is formed from the coupling of methionine, an essential sulfur-containing amino acid, and adenosine triphosphate (ATP) through the action of methionine adenosyltransferase enzymes.

SAMe serves as a major methyl donor in various biochemical reactions, contributing to the synthesis of numerous compounds such as neurotransmitters, proteins, phospholipids, nucleic acids, and other methylated metabolites. Additionally, SAMe plays a crucial role in the detoxification process within the liver by participating in glutathione production, which is an important antioxidant and detoxifying agent.

In clinical settings, SAMe supplementation has been explored as a potential therapeutic intervention for various conditions, including depression, osteoarthritis, liver diseases, and fibromyalgia, among others. However, its efficacy remains a subject of ongoing research and debate within the medical community.

Ornithine decarboxylase (ODC) is a medical/biochemical term that refers to an enzyme (EC involved in the metabolism of amino acids, particularly ornithine. This enzyme catalyzes the decarboxylation of ornithine to form putrescine, which is a precursor for the synthesis of polyamines, such as spermidine and spermine. Polyamines play crucial roles in various cellular processes, including cell growth, differentiation, and gene expression.

Ornithine decarboxylase is a rate-limiting enzyme in polyamine biosynthesis, meaning that its activity regulates the overall production of these molecules. The regulation of ODC activity is tightly controlled at multiple levels, including transcription, translation, and post-translational modifications. Dysregulation of ODC activity has been implicated in several pathological conditions, such as cancer, neurodegenerative disorders, and inflammatory diseases.

Inhibitors of ornithine decarboxylase have been explored as potential therapeutic agents for various diseases, including cancer, due to their ability to suppress polyamine synthesis and cell proliferation. However, the use of ODC inhibitors in clinical settings has faced challenges related to toxicity and limited efficacy.

Spermidine is a polycationic polyamine that is found in various tissues and fluids, including semen, from which it derives its name. It is synthesized in the body from putrescine, another polyamine, through the action of the enzyme spermidine synthase.

In addition to its role as a metabolic intermediate, spermidine has been shown to have various cellular functions, including regulation of gene expression, DNA packaging and protection, and modulation of enzymatic activities. It also plays a role in the process of cell division and differentiation.

Spermidine has been studied for its potential anti-aging effects, as it has been shown to extend the lifespan of various organisms, including yeast, flies, and worms, by activating autophagy, a process by which cells break down and recycle their own damaged or unnecessary components. However, more research is needed to determine whether spermidine has similar effects in humans.

'Diamines' are organic compounds containing two amino groups (-NH2) in their molecular structure. The term 'diamine' itself does not have a specific medical definition, but it is used in the context of chemistry and biochemistry.

Diamines can be classified based on the number of carbon atoms between the two amino groups. For example, ethylenediamine and propylenediamine are diamines with one and two methylene (-CH2-) groups, respectively.

In medicine, certain diamines may have biological significance. For instance, putrescine and cadaverine are polyamines that are produced during the decomposition of animal tissues and can be found in necrotic or infected tissues. These compounds have been implicated in various pathological processes, including inflammation, oxidative stress, and cancer progression.

It is important to note that while some diamines may have medical relevance, the term 'diamines' itself does not have a specific medical definition.

S-Adenosylhomocysteine (SAH) is a metabolic byproduct formed from the demethylation of various compounds or from the breakdown of S-adenosylmethionine (SAM), which is a major methyl group donor in the body. SAH is rapidly hydrolyzed to homocysteine and adenosine by the enzyme S-adenosylhomocysteine hydrolase. Increased levels of SAH can inhibit many methyltransferases, leading to disturbances in cellular metabolism and potential negative health effects.

Glutamate decarboxylase (GAD) is an enzyme that plays a crucial role in the synthesis of the neurotransmitter gamma-aminobutyric acid (GABA) in the brain. GABA is an inhibitory neurotransmitter that helps to balance the excitatory effects of glutamate, another neurotransmitter.

Glutamate decarboxylase catalyzes the conversion of glutamate to GABA by removing a carboxyl group from the glutamate molecule. This reaction occurs in two steps, with the enzyme first converting glutamate to glutamic acid semialdehyde and then converting that intermediate product to GABA.

There are two major isoforms of glutamate decarboxylase, GAD65 and GAD67, which differ in their molecular weight, subcellular localization, and function. GAD65 is primarily responsible for the synthesis of GABA in neuronal synapses, while GAD67 is responsible for the synthesis of GABA in the cell body and dendrites of neurons.

Glutamate decarboxylase is an important target for research in neurology and psychiatry because dysregulation of GABAergic neurotransmission has been implicated in a variety of neurological and psychiatric disorders, including epilepsy, anxiety, depression, and schizophrenia.

Dopa decarboxylase (DDC) is an enzyme that plays a crucial role in the synthesis of dopamine and serotonin, two important neurotransmitters in the human body. This enzyme is responsible for converting levodopa (L-DOPA), an amino acid precursor, into dopamine, a critical neurotransmitter involved in movement regulation, motivation, reward, and mood.

The gene that encodes dopa decarboxylase is DDC, located on chromosome 7p12.2-p12.1. The enzyme is widely expressed throughout the body, including the brain, kidneys, liver, and gut. In addition to its role in neurotransmitter synthesis, dopa decarboxylase also contributes to the metabolism of certain drugs, such as levodopa and carbidopa, which are used in the treatment of Parkinson's disease.

Deficiencies or mutations in the DDC gene can lead to various neurological disorders, including aromatic L-amino acid decarboxylase deficiency (AADCD), a rare autosomal recessive disorder characterized by decreased levels of dopamine and serotonin. Symptoms of AADCD may include developmental delay, movement disorders, seizures, autonomic dysfunction, and oculogyric crises.

Histidine Decarboxylase is a medical term that refers to an enzyme found in various organisms, including humans. This enzyme plays a crucial role in the conversion of the amino acid L-histidine into histamine, which is a biogenic amine that acts as a neurotransmitter and inflammatory mediator in the human body.

Histidine decarboxylase is found in several tissues, including the central nervous system, gastrointestinal tract, and skin. It requires pyridoxal 5'-phosphate (PLP) as a cofactor for its enzymatic activity. Abnormal levels or activity of histidine decarboxylase have been implicated in several medical conditions, including allergic reactions, inflammation, and neuropsychiatric disorders.

Inhibitors of histidine decarboxylase are being investigated as potential therapeutic agents for the treatment of various diseases, such as mast cell-mediated disorders, gastrointestinal disorders, and neurological conditions associated with abnormal histamine levels.

Methionine is an essential amino acid, which means that it cannot be synthesized by the human body and must be obtained through the diet. It plays a crucial role in various biological processes, including:

1. Protein synthesis: Methionine is one of the building blocks of proteins, helping to create new proteins and maintain the structure and function of cells.
2. Methylation: Methionine serves as a methyl group donor in various biochemical reactions, which are essential for DNA synthesis, gene regulation, and neurotransmitter production.
3. Antioxidant defense: Methionine can be converted to cysteine, which is involved in the formation of glutathione, a potent antioxidant that helps protect cells from oxidative damage.
4. Homocysteine metabolism: Methionine is involved in the conversion of homocysteine back to methionine through a process called remethylation, which is essential for maintaining normal homocysteine levels and preventing cardiovascular disease.
5. Fat metabolism: Methionine helps facilitate the breakdown and metabolism of fats in the body.

Foods rich in methionine include meat, fish, dairy products, eggs, and some nuts and seeds.

Methylation, in the context of genetics and epigenetics, refers to the addition of a methyl group (CH3) to a molecule, usually to the nitrogenous base of DNA or to the side chain of amino acids in proteins. In DNA methylation, this process typically occurs at the 5-carbon position of cytosine residues that precede guanine residues (CpG sites) and is catalyzed by enzymes called DNA methyltransferases (DNMTs).

DNA methylation plays a crucial role in regulating gene expression, genomic imprinting, X-chromosome inactivation, and suppression of repetitive elements. Hypermethylation or hypomethylation of specific genes can lead to altered gene expression patterns, which have been associated with various human diseases, including cancer.

In summary, methylation is a fundamental epigenetic modification that influences genomic stability, gene regulation, and cellular function by introducing methyl groups to DNA or proteins.

Uroporphyrinogen decarboxylase is a vital enzyme in the biosynthetic pathway of heme, which is a crucial component of hemoglobin in red blood cells. This enzyme is responsible for catalyzing the decarboxylation of uroporphyrinogen III, a colorless porphyrinogen, to produce coproporphyrinogen III, a brownish-red porphyrinogen.

The reaction involves the sequential removal of four carboxyl groups from the four acetic acid side chains of uroporphyrinogen III, resulting in the formation of coproporphyrinogen III. This enzyme's activity is critical for the normal biosynthesis of heme, and any defects or deficiencies in its function can lead to various porphyrias, a group of metabolic disorders characterized by the accumulation of porphyrins and their precursors in the body.

The gene responsible for encoding uroporphyrinogen decarboxylase is UROD, located on chromosome 1p34.1. Mutations in this gene can lead to a deficiency in the enzyme's activity, causing an autosomal recessive disorder known as congenital erythropoietic porphyria (CEP), also referred to as Günther's disease. This condition is characterized by severe photosensitivity, hemolytic anemia, and scarring or thickening of the skin.

Orotidine-5’-phosphate decarboxylase (ODC) is an enzyme that is involved in the synthesis of pyrimidines, which are essential nucleotides required for the production of DNA and RNA. The gene that encodes this enzyme is called UMPS.

ODC catalyzes the decarboxylation of orotidine-5’-phosphate (OMP) to form uridine monophosphate (UMP), which is a precursor to other pyrimidines such as cytidine triphosphate (CTP) and thymidine triphosphate (TTP). This reaction is the fifth step in the de novo synthesis of pyrimidines.

Defects in the ODC enzyme can lead to a rare genetic disorder called orotic aciduria, which is characterized by an accumulation of orotic acid and orotidine in the urine, as well as neurological symptoms such as developmental delay, seizures, and ataxia. Treatment for this condition typically involves supplementation with uridine and a low-protein diet to reduce the production of excess orotic acid.

Tyrosine decarboxylase is an enzyme that catalyzes the decarboxylation of the amino acid tyrosine to form the biogenic amine tyramine. The reaction occurs in the absence of molecular oxygen and requires pyridoxal phosphate as a cofactor. Tyrosine decarboxylase is found in various bacteria, fungi, and plants, and it plays a role in the biosynthesis of alkaloids and other natural products. In humans, tyrosine decarboxylase is not normally present, but its activity has been detected in some tumors and is associated with the production of neurotransmitters in neuronal cells.

Eflornithine is a antiprotozoal medication, which is used to treat sleeping sickness (human African trypanosomiasis) caused by Trypanosoma brucei gambiense in adults and children. It works by inhibiting the enzyme ornithine decarboxylase, which is needed for the growth of the parasite. By doing so, it helps to control the infection and prevent further complications.

Eflornithine is also used as a topical cream to slow down excessive hair growth in women due to a condition called hirsutism. It works by interfering with the growth of hair follicles.

It's important to note that Eflornithine should be used under the supervision of a healthcare professional, and it may have side effects or interactions with other medications.

Aromatic-L-amino-acid decarboxylases (ALADs) are a group of enzymes that play a crucial role in the synthesis of neurotransmitters and biogenic amines in the body. These enzymes catalyze the decarboxylation of aromatic L-amino acids, such as L-dopa, L-tryptophan, and L-phenylalanine, to produce corresponding neurotransmitters or biogenic amines, including dopamine, serotonin, and histamine, respectively.

There are two main types of ALADs in humans: dopa decarboxylase (DDC) and tryptophan hydroxylase (TPH). DDC is responsible for the conversion of L-dopa to dopamine, which is a crucial neurotransmitter involved in movement regulation. TPH, on the other hand, catalyzes the rate-limiting step in serotonin synthesis by converting L-tryptophan to 5-hydroxytryptophan (5-HTP), which is then converted to serotonin by another enzyme called aromatic amino acid decarboxylase.

Deficiencies or mutations in ALADs can lead to various neurological and psychiatric disorders, such as Parkinson's disease, dopa-responsive dystonia, and depression. Therefore, understanding the function and regulation of ALADs is essential for developing effective therapies for these conditions.

The enzyme adenosylmethionine decarboxylase (EC catalyzes the conversion of S-adenosyl methionine to S- ... S-adenosylmethionine decarboxylase (AdoMetDC) plays an essential regulatory role in the polyamine biosynthetic pathway by ... Pegg AE, Xiong H, Feith DJ, Shantz LM (November 1998). "S-adenosylmethionine decarboxylase: structure, function and regulation ... Unlike many amino acid decarboxylases AdoMetDC uses a covalently bound pyruvate residue as a cofactor rather than the more ...
It is produced by decarboxylation of S-adenosyl methionine. Adenosylmethionine decarboxylase Spermidine synthase Spermine ...
Here, SAM is decarboxylated by adenosylmethionine decarboxylase (EC to form S-adenosylmethioninamine. This compound ... S-Adenosyl methionine (SAM), also known under the commercial names of SAMe, SAM-e, or AdoMet, is a common cosubstrate involved ... S-Adenosyl methionine consists of the adenosyl cation attached to the sulfur of methionine. It is synthesized from ATP and ... Chiang P, Gordon R, Tal J, Zeng G, Doctor B, Pardhasaradhi K, McCann P (1996). "S-Adenosylmethionine and methylation". FASEB J ...
... and S-adenosylmethionine decarboxylase. Tabor was elected to the National Academy of Sciences in 1977. In 1986, Tabor and his ... The research has concentrated on the structure and regulation of ornithine decarboxylase, spermidine synthase, spermine ...
"Comparison of androgen regulation of ornithine decarboxylase and S-adenosylmethionine decarboxylase gene expression in rodent ... Ornithine decarboxylase at Ornithine+decarboxylase at the U.S. National Library of Medicine Medical Subject ... In humans, ornithine decarboxylase (ODC) is expressed by the gene ODC1. The protein ODC is sometimes referred to as "ODC1" in ... The enzyme ornithine decarboxylase (EC, ODC) catalyzes the decarboxylation of ornithine (a product of the urea cycle) ...
The genes presumably regulated by ldcC RNAs are decarboxylases of arginine, ornithine, S-adenosylmethionine or other substrates ...
"Adenovirus-mediated expression of both antisense ornithine decarboxylase and S-adenosylmethionine decarboxylase inhibits lung ... "Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor but not an arginine decarboxylase" (PDF). The ... Antizyme inhibitor 2 (AzI2) also erroneously known as arginine decarboxylase (ADC) is a protein that in humans is encoded by ... Pitkänen LT, Heiskala M, Andersson LC (October 2001). "Expression of a novel human ornithine decarboxylase-like protein in the ...
... adenosylmethionine decarboxylase MeSH D08.811.520.224.125.100 - aromatic-L-amino-acid decarboxylase MeSH D08.811.520.224. ... glutamate decarboxylase MeSH D08.811.520.224.125.300 - histidine decarboxylase MeSH D08.811.520.224.125.350 - indole-3-glycerol ... ornithine decarboxylase MeSH D08.811.520.224.125.450 - orotidine-5'-phosphate decarboxylase MeSH D08.811.520.224.125.500 - ... tyrosine decarboxylase MeSH D08.811.520.224.125.900 - uroporphyrinogen decarboxylase MeSH D08.811.520.224.187 - ...
Spermine synthase Adenosylmethionine decarboxylase Ikeguchi Y, Bewley MC, Pegg AE (January 2006). "Aminopropyltransferases: ... No known spermidine synthase can use S-adenosyl methionine. This is prevented by a conserved aspartatyl residue in the active ... The putrescine-N-methyl transferase whose substrates are putrescine and S-adenosyl methionine, and which is evolutionary ... site, which is thought to repel the carboxyl moiety of S-adenosyl methionine. ...
... especially decarboxylases such as S-adenosylmethionine decarboxylase (SAMDC) that exploit the electron-withdrawing power of the ...
... adenosylmethionine decarboxylase EC 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase EC 6- ... aspartate 1-decarboxylase EC aspartate 4-decarboxylase EC deleted EC valine decarboxylase EC 4.1. ... cis-aconitate decarboxylase EC benzoylformate decarboxylase EC oxalyl-CoA decarboxylase EC malonyl- ... phosphate decarboxylase EC aminobenzoate decarboxylase EC tyrosine decarboxylase EC Now included ...
... because O-methylation of the excessive amounts of L-Dopa can deplete methyl donors such as S-adenosyl methionine and ... which encodes an enzyme called aromatic L-amino acid decarboxylase. Babies with severe aromatic L-amino acid decarboxylase ... The aromatic L-amino acid decarboxylase deficiency enzyme is involved in the synthesis of dopamine and serotonin, both of which ... July 2021). "Gene therapy for aromatic L-amino acid decarboxylase deficiency by MR-guided direct delivery of AAV2-AADC to ...
Thereafter the enzyme spermidine synthase effects two N-alkylation by decarboxy-S-Adenosyl methionine. The intermediate is ... Spermine biosynthesis in animals starts with decarboxylation of ornithine by the enzyme Ornithine decarboxylase in the presence ...
Plants that had been inoculated with P. indica had presented an excess of arginine decarboxylase. This is used in the process ... Spermidine synthase uses putrescine and S-adenosylmethioninamine (decarboxylated S-adenosyl methionine) to produce spermidine. ... Putrescine is synthesized in small quantities by healthy living cells by the action of ornithine decarboxylase. Putrescine is ... The conversion is catalyzed by the enzyme arginine decarboxylase (ADC). Agmatine is transformed into N-carbamoylputrescine by ...
A decarboxylase with cofactor pyridoxal phosphate (PLP) removes CO2 from 5-hydroxy-L-tryptophan to produce 5-hydroxytryptamine ... N-Acetylserotonin is methylated at the hydroxyl position by S-adenosyl methionine (SAM) to produce S-adenosyl homocysteine (SAH ... Hydroxyindole O-methyltransferase and S-adenosyl methionine convert N-acetylserotonin into melatonin through methylation of the ... This intermediate (5-HTP) is decarboxylated by pyridoxal phosphate and 5-hydroxytryptophan decarboxylase to produce serotonin. ...
These create dopamine, which then experiences methylation by a catechol-O-methyltransferase (COMT) by an S-adenosyl methionine ... Tyrosine can either undergo a decarboxylation via tyrosine decarboxylase to generate tyramine and subsequently undergo an ... monophenol hydroxylase or first be hydroxylated by tyrosine hydroxylase to form L-DOPA and decarboxylated by DOPA decarboxylase ...
Then it is subsequently decarboxylated to give dopamine by DOPA decarboxylase (aromatic L-amino acid decarboxylase). Dopamine ... This reaction is catalyzed by the enzyme phenylethanolamine N-methyltransferase (PNMT), which utilizes S-adenosyl methionine ( ...
Ornithine and S-adenosylmethionine are precursors of polyamines. Aspartate, glycine, and glutamine are precursors of ... L-DOPA (L-dihydroxyphenylalanine) for Parkinson's treatment, Eflornithine inhibits ornithine decarboxylase and used in the ... through the transsulfuration pathway or by the demethylation of methionine via the intermediate metabolite S-adenosylmethionine ...
When given with an inhibitor of dopa decarboxylase (carbidopa or benserazide), levodopa is optimally saved. This "triple ... which is donated by S-adenosyl methionine (SAM). Any compound having a catechol structure, like catecholestrogens and catechol- ...
"Lack of enhancement of dimethyltryptamine formation in rat brain and rabbit lung in vivo by methionine or S-adenosylmethionine ... the biosynthesis begins with its decarboxylation by an aromatic amino acid decarboxylase (AADC) enzyme (step 1). The resulting ... catalyzes the transfer of a methyl group from cofactor S-adenosylmethionine (SAM), via nucleophilic attack, to tryptamine. This ... is biosynthesized by aromatic L-amino acid decarboxylase (AADC) and indolethylamine-N-methyltransferase (INMT). Studies have ...
2005). "Evidence for a second class of S-adenosylmethionine riboswitches and other regulatory RNA motifs in alpha- ... the majority of species analysed it is located in the leader of an operon containing the speF gene an ornithine decarboxylase ...
Guidotti A, Ruzicka W, Grayson DR, Veldic M, Pinna G, Davis JM, Costa E (January 2007). "S-adenosyl methionine and DNA ... "GABAergic dysfunction in schizophrenia and mood disorders as reflected by decreased levels of glutamic acid decarboxylase 65 ... As one study shows, S-adenosyl methionine (SAM) concentration in patients' prefrontal cortex is twice as high as in the ... "Histone hyperacetylation induces demethylation of reelin and 67-kDa glutamic acid decarboxylase promoters". Proceedings of the ...
This is a S-adenosylmethionine (SAM) precursor. SAM is a common reagent in biological methylation reactions. For example, it ... which is catalyzed by a serine decarboxylase. The synthesis of choline from ethanolamine may take place in three parallel ... Choline is required to produce acetylcholine - a neurotransmitter - and S-adenosylmethionine (SAM), a universal methyl donor. ... S-adenosylmethionine). SAM is the substrate for almost all methylation reactions in mammals. It has been suggested that ...
Cohen-Addad C, Pares S, Sieker L, Neuburger M, Douce R (1995). "The lipoamide arm in the glycine decarboxylase complex is not ... chloroplasts are autonomous for de novo methionine synthesis and can import S-adenosyl methionine from the cytosol". J Biol ... Douce R, Bourguignon J, Neuburger M, Rébeillé F (2001). "The glycine decarboxylase system: a fascinating complex". Trends Plant ... in particular of the proteins involved in photorespiration and the subunits of the glycine-decarboxylase complex. Chloroplasts ...
Radical S-Adenosylmethionine Enzymes: Radical S-Adenosylmethionine (SAM) Enzymes in Cofactor Biosynthesis: A Treasure Trove of ... a radical S-adenosyl-L-methionine decarboxylase involved in the blasticidin S biosynthetic pathway". PLOS ONE. 8 (7): e68545. ... Pierrel F, Douki T, Fontecave M, Atta M (November 2004). "MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme ... Grell TA, Goldman PJ, Drennan CL (February 2015). "SPASM and twitch domains in S-adenosylmethionine (SAM) radical enzymes". The ...
Finally, DAP decarboxylase LysA mediates the last step of the lysine synthesis and is common for all studied bacterial species ... On the other hand, PurR, a protein which plays a role in purine synthesis and S-adeno-sylmethionine are known to down regulate ... The repressor protein MetJ, in cooperation with the corepressor protein S-adenosyl-methionine, mediates the repression of ...
DDC acting as decarboxylase inhibitor makes COMT main metabolic pathway catalyzing this conversion of Levodopa. This process is ... The necessary cofactor for this enzymatic reaction is s-adenosyl methionine (SAM). Its half-life (approximately 15 hours) is ... On the other hand, the possibility of blocking peripheral decarboxylation by adding an aromatic amino acid decarboxylase (AADC ... This reaction happen in the process of decarboxylation by aromatic amino acid decarboxylase (AADC) also called dopa- ...
Phosphatidylserine decarboxylase is the enzyme that is used to decarboxylate phosphatidylserine in the first pathway. The ... S-Adenosyl methionine can subsequently methylate the amine of phosphatidylethanolamines to yield phosphatidylcholines. ...
... for example histidine decarboxylase and tyrosine decarboxylase. Battersby married Margaret Ruth née Hart in 1949. She was a ... were investigated using methyl-labelled S-adenosyl methionine. It was not until a genetically-engineered strain of Pseudomonas ...
Category:EC 3.3 Adenosylmethionine hydrolase S-adenosyl-L-homocysteine hydrolase Alkenylglycerophosphocholine hydrolase ... Aromatic-L-amino-acid decarboxylase (EC RubisCO (EC Category:EC 4.1.2 Fructose-bisphosphate aldolase (EC ... EC 4.1.1 Ornithine decarboxylase (EC Uridine monophosphate synthetase (EC ...
The enzyme adenosylmethionine decarboxylase (EC catalyzes the conversion of S-adenosyl methionine to S- ... S-adenosylmethionine decarboxylase (AdoMetDC) plays an essential regulatory role in the polyamine biosynthetic pathway by ... Pegg AE, Xiong H, Feith DJ, Shantz LM (November 1998). "S-adenosylmethionine decarboxylase: structure, function and regulation ... Unlike many amino acid decarboxylases AdoMetDC uses a covalently bound pyruvate residue as a cofactor rather than the more ...
Protein target information for S-adenosylmethionine decarboxylase proenzyme (Pseudomonas aeruginosa LESB58). Find diseases ...
Order ELISA Kit FOR Bovine S-adenosylmethionine decarboxylase proenzyme AMD1 01012038761 at Gentaur FOR S-adenosylmethionine ... S-adenosylmethionine decarboxylase proenzyme. Targets other names. Bos taurus, Bovine, S-adenosylmethionine decarboxylase ...
In response to SS, ornithine decarboxylase, diamine oxidase and S-adenosylmethionine decarboxylase activities increased in both ... S-adenosylmethionine decarboxylase (SAMDC). CAA58762. Tritordeum. O. sativa. Salt stress. [151]. Trehalose-6-phosphate synthase ... S-adenosylmethionine decarboxylase (SAMDC) is a key enzyme in PA biosynthesis, and it plays an important role in plant ... Roy, M.; Wu, R. Overexpression of S-adenosylmethionine decarboxylase gene in rice increases polyamine level and enhances sodium ...
Discovery of new S-adenosylmethionine decarboxylase inhibitors for the treatment of Human African Trypanosomiasis (HAT). In: ... Dive into the research topics of Discovery of new S-adenosylmethionine decarboxylase inhibitors for the treatment of Human ... Discovery of new S-adenosylmethionine decarboxylase inhibitors for the treatment of Human African Trypanosomiasis (HAT). ... Discovery of new S-adenosylmethionine decarboxylase inhibitors for the treatment of Human African Trypanosomiasis (HAT). / ...
TargetS-adenosylmethionine decarboxylase proenzyme(Rattus norvegicus). TBA. Curated by ChEMBL. Ligand. BDBM28422((2S)-2-amino-4 ... TargetS-adenosylmethionine decarboxylase proenzyme(Rattus norvegicus). TBA. Curated by ChEMBL. Ligand. BDBM28422((2S)-2-amino-4 ... Affinity DataKi: 3.00E+5nMAssay Description:In vitro inhibitory activity against S-adenosyl-L-methionine decarboxylase using ... S-Adenosylmethionine::S-adenosyl-L-[carboxy-14C]methionine::[14COOH]AdoMet ...
S-adenosylmethionine decarboxylase of Bacillus subtilis is closely related to archaebacterial counterparts. Sekowska, A., ...
Adenosylmethionine decarboxylase. Model: iECOK1_1307. Reaction:. amet_c + h_c → ametam_c + co2_c ...
Adenosylmethionine decarboxylase. Model: iIS312_Epimastigote. Reaction:. amet_c + h_c → ametam_c + co2_c ...
... coding for S-adenosylmethionine decarboxylase 2), Psma7 (encoding proteasome subunit α7), Syt1 (encoding synaptotagmin 1), ...
US-adenosylmethionine decarboxylase proenzyme. Not Available. Humans. UPutrescine-binding periplasmic protein. Not Available. ... Known drug targets of putrescine include putrescine-binding periplasmic protein, ornithine decarboxylase, and S- ...
S-adenosylmethionine decarboxylase proenzyme. -. 3e-1. At3g02468. CPuORF9 (Conserved peptide upstream open reading frame 9). O. ...
... ornithine decarboxylase, S-adenosylmethionine decarboxylase, gamma-glutamyl transpeptidase and transglutaminase to skin. ...
Caenorhabditis elegans S-adenosylmethionine decarboxylase is highly stimulated by putrescine but exhibits a low specificity for ... S-adenosylmethionine decarboxylase degradation by the 26 S proteasome is accelerated by substrate-mediated transamination. ... S-adenosylmethionine decarboxylase activity increases 7-fold and the concentration of decarboxylated S-adenosylmethionine 450- ... Decarboxylated-S-adenosylmethionine excretion: a biochemical marker of ornithine decarboxylase inhibition by alpha- ...
Auxin-induced protein (AIP), cinnamoyl-CoA reductase (CCR), and S-adenosylmethionine decarboxylase (SAMDC) fit the negative ... Characterisation of the S-adenosylmethionine decarboxylase (SAMDC) gene of potato. Plant Mol Biol. 1994;26:327-38. ... S-adenosylmethionine decarboxylase; EIL3, ethylene-insensitive 3-like 3 protein; HIR1, hypersensitive-induced response protein ... SAMDC and S-adenosylmethionine synthetase (SAMS) are important genes for polyamine biosynthesis [101, 102]. Previous studies ...
... such as Adenosylmethionine Decarboxylase 1 (AMD1) and uncovers novel enzymes predicted to be relevant for polyamine homeostasis ...
S-adenosylmethionine synthetase; S-adenosylmethionine decarboxylase; methionine aminotransferase; methionine-gamma-lyase. ... Arginine decarboxylase; arginine deiminase. Lysine. 4,806. 3,172. 5,156. Lysine decarboxylase; lysine 2,3-aminomutase; L-lysine ... Tyrosine decarboxylase; protein-tyrosine phosphatase; protein-tyrosine kinase; tyrosine phenol-lyase. Phenylalanine. 930. 824. ... Glutamate synthase (ferredoxin); glutamate synthase (NADPH/NADH); glutamate N-acetyltransferase; glutamate decarboxylase; ...
adenosylmethionine decarboxylase 1. 6q21. CV:PGCnp. DMG:Wockner_2014. 7128. TNFAIP3. A20 , AISBL , OTUD7C , TNFA1P2. TNF alpha ...
adenosylmethionine decarboxylase 1.... ARHGAP15. 55843. ARHGAP15. Rho GTPase activating protein 15 [.... ATP13A1. 57130. ...
adenosylmethionine decarboxylase activity. GO:0016831. carboxy-lyase activity. GO:0016829. lyase activity. ...
CDS with a similar description: S-adenosylmethionine decarboxylase proenzyme. CDS description. CDS accession. Island. Host ... S-adenosylmethionine decarboxylase proenzyme. NC_000854:50407:54129. NC_000854:50407. Aeropyrum pernix K1, complete genome. ... S-adenosylmethionine decarboxylase proenzyme. NC_014837:809911:834845. NC_014837:809911. Pantoea sp. At-9b chromosome, complete ... S-adenosylmethionine decarboxylase proenzyme. NC_012214:124337:130464. NC_012214:124337. Erwinia pyrifoliae Ep1/96, complete ...
S-adenosylmethionine decarboxylase proenzyme. Enzyme. *S-Adenosylmethioninamine. *S-Adenosylmethionine. *S-Adenosyl-L- ... S-Adenosylmethionine. 29908-03-0. [(3S)-3-amino-3-carboxypropyl]({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan- ...
adenosylmethionine decarboxylase family protein; FUNCTIONS IN: adenosylmethionine decarboxylase activity; INVOLVED IN: ... S-ADENOSYLMETHIONINE DECARBOXYLASE); adenosylmethionine decarboxylase (TAIR:AT3G02470.4); Has 830 Blast hits to 816 proteins in ... S-adenosylmethionine decarboxylase, core (InterPro:IPR016067), S-adenosylmethionine decarboxylase (InterPro:IPR001985), S- ... adenosylmethionine decarboxylase, conserved site (InterPro:IPR018166), S-adenosylmethionine decarboxylase subgroup (InterPro: ...
S-adenosylmethionine decarboxylase proenzyme. O07005 YVEG. 156. 614. 40.8. 0.13. UPF0311 protein YveG. ...
PREDICTED: S-adenosylmethionine decarboxylase proenzyme. snpEff. Effect. missense_variant. Impact. MODERATE. Codon. c.763T,A. ...
Match: amd1 (adenosylmethionine decarboxylase 1 [Source:Xenbase;Acc:XB-GENE-484611]). HSP 1 Score: 50.447 bits (119), Expect = ...
S-adenosylmethionine decarboxylase proenzyme (RefSeq). 22, 241. BSU29020. gapB. glyceraldehyde-3-phosphate dehydrogenase ( ...
... an inhibitor of ornithine decarboxylase, depleted cellular polyamine levels ... The activities of the polyamine-synthesizing enzymes ornithine decarboxylase (ODC) and S-adenosyl methionine decarboxylase ( ... Treatment of mouse lymphoma S49 cells with D,L-alpha-difluoromethylornithine (DFMO), an inhibitor of ornithine decarboxylase, ... C-Jun Activation-Dependent Tumorigenic Transformation Induced Paradoxically by Overexpression or Block of S-Adenosylmethionine ...
ELISA Kit FOR Rat S-adenosylmethionine decarboxylase proenzyme (Amd1). 96 tests. 608 E0499r. See more ... ELISA Kit FOR S-adenosylmethionine decarboxylase proenzyme 1. 1kit. 746 E0499m. See more ... ELISA Kit FOR S-adenosylmethionine decarboxylase proenzyme. 1kit. 746 E0499r. See more ... ELISA Kit FOR S-adenosylmethionine decarboxylase proenzyme. 1kit. 746 E0499h. See more ...
GP21400 AMD1 Human Adenosylmethionine Decarboxylase 1 Human Recombinant * GP21549 DDT Human D-Dopachrome Tautomerase Human ... GP21568 Dopa Decarboxylase Human Dopa Decarboxylase Human Recombinant * GP21649 GAD1 Human Glutamate Decarboxylase 1 Human ... GP21650 GAD1 iso1 Human Glutamate Decarboxylase 1 Isoform-1 Human Recombinant * GP21651 GAD2 Human Glutamate Decarboxylase 2 ... GP22031 ODC1 Human Ornithine Decarboxylase 1 Human Recombinant * GP22128 PPCDC Human Phosphopantothenoylcysteine Decarboxylase ...
  • Known drug targets of putrescine include putrescine-binding periplasmic protein, ornithine decarboxylase, and S-adenosylmethionine decarboxylase proenzyme. (
  • S-adenosylmethionine decarboxylase (AdoMetDC) plays an essential regulatory role in the polyamine biosynthetic pathway by generating the n-propylamine residue required for the synthesis of spermidine and spermine from putrescein. (
  • Unlike many amino acid decarboxylases AdoMetDC uses a covalently bound pyruvate residue as a cofactor rather than the more common pyridoxal 5'-phosphate. (
  • Treatment of mouse lymphoma S49 cells with D,L-alpha-difluoromethylornithine (DFMO), an inhibitor of ornithine decarboxylase, depleted cellular polyamine levels and stopped cell growth. (
  • The activities of the polyamine-synthesizing enzymes ornithine decarboxylase (ODC) and S-adenosyl methionine decarboxylase (SAMD) are both reduced in Bt2cAMP-treated cells to about 10% of that in control populations, as shown previously. (
  • The enzyme adenosylmethionine decarboxylase (EC catalyzes the conversion of S-adenosyl methionine to S-adenosylmethioninamine. (
  • With methionine deficiency, S -adenosylmethionine accumulates, resulting in the inhibition of sphingolipid and myelin synthesis. (
  • PLP is a cofactor for glutamic acid decarboxylase, the enzyme that produces GABA, such that PLP deficiency results in insufficient GABA. (
  • In particular, upon entry into the stationary growth phase (which is often the consequence of starvation in one of the major cell metabolite supplies: carbon, nitrogen or phosphorus), we observed that polyamine biosynthesis was much affected, in parallel with the expression of S-adenosylmethionine decarboxylase [ 2 ]. (
  • Toms, A. V. , Kinsland, C. , McCloskey, D. E. , Pegg, A. E. , and Ealick, S. E. (2004) Evolutionary links as revealed by the structure of Thermotoga maritima S-adenosylmethionine decarboxylase . (
  • The precursor could also be detected by immunoblotting of extracts from prostates of rats depleted of putrescine by treatment with the ornithine decarboxylase inhibitor, α-difluoromethylornithine. (
  • 7. Over-expression of a cDNA for human ornithine decarboxylase in transgenic rice plants alters the polyamine pool in a tissue-specific manner. (
  • 13. Polyamine homeostasis in transgenic plants overexpressing ornithine decarboxylase includes ornithine limitation. (
  • alpha-Difluoromethylornithine (DFMO), an irreversible inhibitor of ornithine decarboxylase (ODC), inhibits squamous metaplasia caused by asbestos or vitamin A deficiency, whereas addition of methylglyoxal bis(guanylhydrazone) (MGBG), a structural analog of spermidine and inhibitor of S-adenosylmethionine decarboxylase, causes an enhancement of metaplasia under both circumstances. (
  • The effects of CGP 48664 and DFMO, selective inhibitors of the key enzymes of polyamine biosynthesis, namely, of S-adenosylmethionine decarboxylase (AdoMetDC) and ornithine decarboxylase (ODC), were investigated on growth, polyamine metabolism, and DNA methylation in the Caco-2 cell line. (
  • The relevant regulatory roles of the short half-life enzymes ornithine decarboxylase (ODC), S-adenosyl methione decarboxylase (SAMDC) and spermindine/spermine acetyl transferase (SSAT) in polyamine metabolism are well studied, and has been modelled here. (
  • 5. Transcriptional regulation of the rice arginine decarboxylase (Adc1) and S-adenosylmethionine decarboxylase (Samdc) genes by methyl jasmonate. (
  • In this study, maize S-adenosylmethionine decarboxylase (SAMDC) was localized to the nucleus. (
  • 8. Reduction in the endogenous arginine decarboxylase transcript levels in rice leads to depletion of the putrescine and spermidine pools with no concomitant changes in the expression of downstream genes in the polyamine biosynthetic pathway. (
  • 9. Overexpression of arginine decarboxylase in transgenic plants. (
  • Three S-adenosylmethionine decarboxylases (HvSAMDCs), two ornithine decarboxylases (HvODCs), one arginine decarboxylase (HvADC), one spermidine synthase (HvSPDS), two spermine synthases (HvSPMSs), five copper amine oxidases (HvCuAOs) and seven polyamine oxidases (HvPAOs) members of PMGs were identified and characterized in barley. (
  • Using this radioimmunoassay it was found that a number of inhibitors of other steps in the polyamine biosynthetic pathway lead to increases in the amount of S-adenosylmethionine decarboxylase protein. (
  • Die 4-Hydroxyphenylacetat-Decarboxylase (4Hpad) besitzt zusätzlich zum Protein-basierten Glycinradikal eine weitere Untereinheit mit bis zu zwei [4Fe-4S] Clustern und repräsentiert hierdurch eine neue Klasse von Fe/S-Cluster-haltigen GREs, die aromatische Verbindungen umsetzen. (
  • We identified fusion proteins of bona fide AdoMetDC/SpeD with homologous L-ornithine decarboxylases that possess two, unprecedented internal protein-derived pyruvoyl cofactors. (
  • Enzymologists categorized the protein as a decarboxylase indirectly based on its sequence. (
  • We re not sure if it s a decarboxylase,' he says, 'but it s unambiguously a methyltransferase' based on the group s solved structure of the protein bound to S-adenosylmethionine. (
  • Considering that earlier this year researchers have demonstrated that gluten and casein peptides can cross-react with specific brain proteins [GAD-65 (Glutamic Acid Decarboxylase), Cerebellar peptides, MBP (myelin basic protein), MOG (myelin oligodendrocyte glycoprotein)], more evidence is mounting that how our bodies respond to certain foods has direct influence on our immunity, neurological system, and overall wellness. (
  • S-adenosylmethionine decarboxylase (AdoMetDC) plays an essential regulatory role in the polyamine biosynthetic pathway by generating the n-propylamine residue required for the synthesis of spermidine and spermine from putrescein. (
  • The translation of the S-adenosylmethionine decarboxylase mRNA in the reticulocyte lysates was strongly inhibited by the addition of spermidine or spermine demonstrating that polyamines directly inhibit the synthesis of S-adenosylmethionine decarboxylase. (
  • 1. Expression of a heterologous S-adenosylmethionine decarboxylase cDNA in plants demonstrates that changes in S-adenosyl-L-methionine decarboxylase activity determine levels of the higher polyamines spermidine and spermine. (
  • 3. Spermine facilitates recovery from drought but does not confer drought tolerance in transgenic rice plants expressing Datura stramonium S-adenosylmethionine decarboxylase. (
  • These proteins can be divided into two main groups which show little sequence similarity either to each other, or to other pyruvoyl-dependent amino acid decarboxylases: class I enzymes found in bacteria and archaea, and class II enzymes found in eukaryotes. (
  • Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). (
  • The translation of mRNA for S-adenosylmethionine decarboxylase was studied using a polyamine-depleted reticulocyte lysate supplemented with mRNA from rat prostate and the antiserum to precipitate the proteins corresponding to S-adenosylmethionine decarboxylase. (
  • cDNA clones corresponding to S-adenosylmethionine decarboxylase were isolated using prostatic mRNA from polysomes enriched in S-adenosylmethionine decarboxylase by immunopurification. (
  • The activity of S-adenosylmethionine decarboxylase is known to be regulated negatively by these polyamines and positively by their precursor, putrescine. (
  • It catalyzes the decarboxylation of ornithine to form putrescine, which is then linked to a propylamine moiety of decarboxylated S-adenosylmethionine to form spermidine. (
  • The subsequent decrease in cysteine uptake was associated "with changes in the intracellular antioxidant glutathione and the methyl donor S-adenosylmethionine. (
  • AND MARSHALL W. NIRENBERG From the Laboratory of Biochemical Genetics, National Heart and Lung Institute, National Institutes of Health, Bethesda, Maryland 20014 SUMMARY Methods are presented for preparation of extracts from cultured cells from the nervous system and for study of choline acetyltransferase, acetylcholinesterase, glutamate decarboxylase, and catechol O-methyltransferase activities. (
  • Low activities of choline acetyltransferase, acetylcholines- terase, and glutamate decarboxylase were detected in all the cells tested. (
  • All of these activities, and particularly glutamate decarboxylase, were higher in cultured brain cells from newborn animals than in non-neuronal cell lines. (
  • Glutamate decarboxylase activity in glial cells and in brain cells was inhibited more than 95% by 1 mm amino-oxyacetic acid. (
  • and for assays of acetylcholinesterase (EC, cutechol O-methyltransferase (eC, choline acetyltransferase (EC, and glutamate decarboxylase (EC 4.1,1.15) activities. (
  • superimposing structural homologs, when one of the homologs brought its AdoMet [S-adenosylmethionine] along, fitting it right into the homologous pocket in MT0146. (
  • UDP-glucuronic acid decarboxylases of Bacteroides fragilis and their prevalence in bacteria. (
  • S-adenosylmethionine is a primary mechanism through which the cells of our body silence the expression of genes in a process known as methylation. (
  • When S-adenosylmethionine levels are low, it can interfere with methylation and this has been observed in many pathological states, including numerous cancers, e.g. 'global hypomethylation' is observed in cells whose cancer genes (oncogenes) have been turned on. (
  • This will provide evidence on the origin of the pyruvate prosthetic group of S-adenosylmethionine decarboxylase. (
  • 16. Manipulation of S-adenosylmethionine decarboxylase activity in potato tubers. (
  • The purification and characterization of active site mutants of decarboxylase are also done. (
  • The use of these probes showed that rat ventral prostate contains two S-adenosylmethionine decarboxylase mRNA species of approximately 3.4 and 2.1 kb which differ in the 3′ non-translated sequence. (
  • This study shows the optimized expression and purification protocols for the decarboxylase and the co-crystallization experiments and binding studies with 4-hydroxy-phenylacetate and 3,4-dihydroxyphenylacetate and with the inhibitor 4-hydroxy-phenylacetamide. (
  • Activities of en- zymes important in neuronal cell metabolism are useful param- eters for following cell maturation and exploring steps in differ- entiation in such cultures. (
  • S-Adenosylmethionine (SAMe) is brought to the attention of the CSWG because of the rapid increase in its use as a dietary supplement since being introduced into the US market in 1999. (
  • Fruit-specific yeast S-adenosylmethionine decarboxylase (ySAMdc) line 579HO, and a control line 556AZ were grown in leguminous hairy vetch (Vicia villosa Roth) (HV) mulch and conventional black polyethylene (BP) mulch, and their fruit analysed. (