Adenosylmethionine Decarboxylase: 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 4.1.1.50.Mitoguazone: Antineoplastic agent effective against myelogenous leukemia in experimental animals. Also acts as an inhibitor of animal S-adenosylmethionine decarboxylase.Carboxy-Lyases: 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.PolyaminesPutrescine: A toxic diamine formed by putrefaction from the decarboxylation of arginine and ornithine.S-Adenosylmethionine: 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)Ornithine Decarboxylase: 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.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.Diamines: Organic chemicals which have two amino groups in an aliphatic chain.S-Adenosylhomocysteine: 5'-S-(3-Amino-3-carboxypropyl)-5'-thioadenosine. Formed from S-adenosylmethionine after transmethylation reactions.Glutamate Decarboxylase: 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 4.1.1.15.Dopa Decarboxylase: 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.Histidine Decarboxylase: 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 4.1.1.22.Methionine: A sulfur-containing essential L-amino acid that is important in many body functions.Methylation: 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)Uroporphyrinogen Decarboxylase: 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 Decarboxylase: 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 4.1.1.23.Tyrosine Decarboxylase: 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 4.1.1.25.Eflornithine: An inhibitor of ORNITHINE DECARBOXYLASE, the rate limiting enzyme of the polyamine biosynthetic pathway.Aromatic-L-Amino-Acid Decarboxylases: An enzyme group with broad specificity. The enzymes decarboxylate a range of aromatic amino acids including dihydroxyphenylalanine (DOPA DECARBOXYLASE); TRYPTOPHAN; and HYDROXYTRYPTOPHAN.
(1/292) 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.

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)

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

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)

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

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)

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

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)

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

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)

(6/292) 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.

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)

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

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)

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

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
... is an enzyme that 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 ...
*  S-Adenosylmethioninamine
Adenosylmethionine decarboxylase Spermidine synthase Spermine synthase Thermospermine synthase (ACAULIS5) Takahashi, Taku; ... S-Adenosylmethioninamine (decarboxylated S-adenosyl methionine) is a substrate that is involved in the biosynthesis of ...
*  S-Adenosyl methionine
Here, SAM-e is decarboxylated by adenosylmethionine decarboxylase (EC 4.1.1.50) to form S-adenosylmethioninamine. This compound ... S-Adenosyl methionine is a common cosubstrate involved in methyl group transfers, transsulfuration, and aminopropylation. ... Chiang P, Gordon R, Tal J, Zeng G, Doctor B, Pardhasaradhi K, McCann P (1996). "S-Adenosylmethionine and methylation". FASEB J ... Najm WI, Reinsch S, Hoehler F, Tobis JS, Harvey PW (February 2004). "S-Adenosyl methionine (SAMe) versus celecoxib for the ...
*  AZIN2
"Adenovirus-mediated expression of both antisense ornithine decarboxylase and S-adenosylmethionine decarboxylase inhibits lung ... Antizyme inhibitor 2 (AzI2) also known as arginine decarboxylase (ADC) is an enzyme that in humans is encoded by the AZIN2 gene ... "Entrez Gene: ADC arginine decarboxylase". Human AZI2 genome location and AZI2 gene details page in the UCSC Genome Browser. ... Zhu MY, Iyo A, Piletz JE, Regunathan S (2004). "Expression of human arginine decarboxylase, the biosynthetic enzyme for ...
*  Ornithine decarboxylase
"Comparison of androgen regulation of ornithine decarboxylase and S-adenosylmethionine decarboxylase gene expression in rodent ... Ornithine decarboxylase at herkules.oulu.fi Ornithine decarboxylase at the US National Library of Medicine Medical Subject ... The enzyme ornithine decarboxylase (ODC) catalyzes the decarboxylation of ornithine (a product of the urea cycle) to form ... Therefore, ornithine decarboxylase is an essential enzyme for cell growth, producing the polyamines necessary to stabilize ...
*  List of MeSH codes (D08)
... adenosylmethionine decarboxylase MeSH D08.811.520.224.125.100 --- aromatic-L-amino-acid decarboxylase MeSH D08.811.520.224. ... 125.100.500 --- dopa decarboxylase MeSH D08.811.520.224.125.250 --- glutamate decarboxylase MeSH D08.811.520.224.125.300 --- ... 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 --- ...
*  Spermidine synthase
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 related ... site, which is thought to repel the carboxyl moiety of S-adenosyl methionine. ...
*  Protein primary structure
... especially decarboxylases such as S-adenosylmethionine decarboxylase (SAMDC) that exploit the electron-withdrawing power of the ...
*  List of EC numbers (EC 4)
... adenosylmethionine decarboxylase EC 4.1.1.51: 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase EC 4.1.1.52: 6- ... EC 4.1.1.1: pyruvate decarboxylase EC 4.1.1.2: oxalate decarboxylase EC 4.1.1.3: oxaloacetate decarboxylase EC 4.1.1.4: ... aspartate 1-decarboxylase EC 4.1.1.12: aspartate 4-decarboxylase EC 4.1.1.13: deleted EC 4.1.1.14: valine decarboxylase EC 4.1. ... aconitate decarboxylase EC 4.1.1.7: benzoylformate decarboxylase EC 4.1.1.8: oxalyl-CoA decarboxylase EC 4.1.1.9: malonyl-CoA ...
*  Putrescine
In one pathway, arginine is converted into agmatine, with a reaction catalyzed by the enzyme arginine decarboxylase (ADC); then ... 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 ... arginine is converted into ornithine and then ornithine is converted into putrescine by ornithine decarboxylase (ODC). The ...
*  Melatonin
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. ...
*  Catechol-O-methyl transferase
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- ...
*  N,N-Dimethyltryptamine
"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-adenosyl-methionine (SAM), via nucleophilic attack, to tryptamine. ...
*  Reelin
Guidotti A, Ruzicka W, Grayson DR, Veldic M, Pinna G, Davis JM, Costa E (Jan 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 ...
*  SpeF leader
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 ...
*  Amino acid synthesis
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 major donor of activated methyl groups is S-adenosylmethionine, which is synthesized by the transfer of an adenosyl group ... The repressor protein MetJ, in cooperation with the corepressor protein S-adenosyl-methionine, mediates the repression of ...
*  Amino acid
Ornithine and S-adenosylmethionine are precursors of polyamines. Aspartate, glycine, and glutamine are precursors of ... and eflornithine drug that inhibits ornithine decarboxylase and used in the treatment of sleeping sickness. Since 2001, 40 non- ... is formed through the transsulfuration pathway or by the demethylation of methionine via the intermediate metabolite S-adenosyl methionine ...
*  Phosphatidylethanolamine
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. It can ...
*  List of enzymes
Aromatic-L-amino-acid decarboxylase (EC 4.1.1.28) RubisCO (EC 4.1.1.39) Category:EC 4.1.2 Fructose-bisphosphate aldolase (EC ... EC 3.3 Adenosylmethionine hydrolase S-adenosyl-L-homocysteine hydrolase Alkenylglycerophosphocholine hydrolase ... EC 4.1.1 Ornithine decarboxylase (EC 4.1.1.17) Uridine monophosphate synthetase (EC 4.1.1.23) ...
*  Radical SAM
... but still use three Cys residues as ligands to a 4Fe4S cluster and produce a radical from S-adenosylmethionine. These include ... cytosylglucuronic acid decarboxylase - blasticidin S biosynthesis BtrN - butirosin biosynthesis pathway oxidoreductase ( ...
*  Fatty acid synthesis
BCKA decarboxylase and relative activities of α-keto acid substrates The BCKA decarboxylase enzyme is composed of two subunits ... S-adenosyl-methionine donates a methyl group to the double bond of oleic acid. This methylation reaction forms the intermediate ... All of these factors may affect chain length, and HSFs have been demonstrated to alter the specificity of BCKA decarboxylase ... Decarboxylation of the primer precursors occurs through the branched-chain α-keto acid decarboxylase (BCKA) enzyme. Elongation ...
*  Cystathionine beta-lyase
"Modeling of the spatial structure of eukaryotic ornithine decarboxylases". Protein Science. 4 (7): 1291-1304. doi:10.1002/pro. ... is an essential amino acid for bacteria that is required for protein synthesis and the synthesis of S-adenosylmethionine; thus ...
*  Neurotransmitter
These conversions require vitamin B6, vitamin C, and S-adenosylmethionine. A few studies suggest potential antidepressant ... and the biosynthetic enzyme aromatic amino acid decarboxylase (AADC). Malenka RC, Nestler EJ, Hyman SE (2009). "Chapter 6: ...
*  Cofactor (biochemistry)
ISBN 0-86542-793-3. Chiang P, Gordon R, Tal J, Zeng G, Doctor B, Pardhasaradhi K, McCann P (1996). "S-Adenosylmethionine and ... Another example is thiamine pyrophosphate (TPP), which is tightly bound in transketolase or pyruvate decarboxylase, while it is ...
*  List of EC numbers (EC 2)
... malonate decarboxylase holo-(acyl-carrier protein) synthase EC 2.7.7.67: CDP-archaeol synthase EC 2.7.7.68: 2-phospho-L-lactate ... adenosylmethionine cyclotransferase EC 2.5.1.5: galactose-6-sulfurylase EC 2.5.1.6: methionine adenosyltransferase EC 2.5.1.7: ... adenosylmethionine-8-amino-7-oxononanoate transaminase EC 2.6.1.63: kynurenine-glyoxylate transaminase EC 2.6.1.64: glutamine- ...
Selective regulation of S-adenosylmethionine decarboxylase activity by the spermine analogue 6-spermyne | Biochemical Journal  Selective regulation of S-adenosylmethionine decarboxylase activity by the spermine analogue 6-spermyne | Biochemical Journal
Selective regulation of S-adenosylmethionine decarboxylase activity by the spermine analogue 6-spermyne. C W Porter, J McManis ... Selective regulation of S-adenosylmethionine decarboxylase activity by the spermine analogue 6-spermyne ... Selective regulation of S-adenosylmethionine decarboxylase activity by the spermine analogue 6-spermyne ... Selective regulation of S-adenosylmethionine decarboxylase activity by the spermine analogue 6-spermyne ...
more infohttp://www.biochemj.org/content/254/2/337
Adenosylmethionine decarboxylase - Wikipedia  Adenosylmethionine decarboxylase - Wikipedia
Adenosylmethionine decarboxylase is an enzyme that 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 ...
more infohttps://en.wikipedia.org/wiki/Adenosylmethionine_decarboxylase
Impact of S-Adenosylmethionine Decarboxylase 1 on Pulmonary Vascular RemodelingCLINICAL PERSPECTIVE | Circulation  Impact of S-Adenosylmethionine Decarboxylase 1 on Pulmonary Vascular RemodelingCLINICAL PERSPECTIVE | Circulation
Impact of S-Adenosylmethionine Decarboxylase 1 on Pulmonary Vascular RemodelingCLINICAL PERSPECTIVE. Friederike Christine ... Microarray analysis from these mice revealed s-adenosylmethionine decarboxylase 1 (AMD-1) as one of the most downregulated ... Impact of S-Adenosylmethionine Decarboxylase 1 on Pulmonary Vascular RemodelingCLINICAL PERSPECTIVE ... Impact of S-Adenosylmethionine Decarboxylase 1 on Pulmonary Vascular RemodelingCLINICAL PERSPECTIVE ...
more infohttp://circ.ahajournals.org/content/129/14/1510.short?rss=1
RCSB PDB 









- 1MSV: The S68A S-adenosylmethionine decarboxylase proenzyme processing mutant. Macromolecule Annotations...  RCSB PDB - 1MSV: The S68A S-adenosylmethionine decarboxylase proenzyme processing mutant. Macromolecule Annotations...
Decarboxylase Proenzyme Processing as Revealed by the Structure of the S68A Mutant. ... S-adenosylmethionine decarboxylase S-adenosylmethionine decarboxylase S-adenosylmethionine decarboxylase S-adenosylmethionine ... S-adenosylmethionine decarboxylase S-adenosylmethionine decarboxylase S-adenosylmethionine decarboxylase S-adenosylmethionine ... S-adenosylmethionine decarboxylase S-adenosylmethionine decarboxylase B. 1msvB00. Alpha Beta 4-Layer Sandwich S- ...
more infohttp://www.rcsb.org/pdb/explore/derivedData.do?structureId=1MSV
In vitro and in vivo anti-tumor action of the S-adenosylmethionine decarboxylase (SAMDC) inhibitor SAM486A in human breast...  In vitro and in vivo anti-tumor action of the S-adenosylmethionine decarboxylase (SAMDC) inhibitor SAM486A in human breast...
In vitro and in vivo anti-tumor action of the S-adenosylmethionine decarboxylase (SAMDC) inhibitor SAM486A in human breast ... In vitro and in vivo anti-tumor action of the S-adenosylmethionine decarboxylase (SAMDC) inhibitor SAM486A in human breast ... In vitro and in vivo anti-tumor action of the S-adenosylmethionine decarboxylase (SAMDC) inhibitor SAM486A in human breast ... In vitro and in vivo anti-tumor action of the S-adenosylmethionine decarboxylase (SAMDC) inhibitor SAM486A in human breast ...
more infohttp://cancerres.aacrjournals.org/content/64/7_Supplement/1201.1
RNAi silencing of three homologues of S-adenosylmethionine decarboxylase gene in tapetal tissue of tomato results in male...  RNAi silencing of three homologues of S-adenosylmethionine decarboxylase gene in tapetal tissue of tomato results in male...
Solanumlycopersicum Male sterility Polyamines S-Adenosylmethionine decarboxylase RNAi Pollen development Electronic ... Song J, Nada K, Tachibana S (2001) The early increase of S-adenosylmethionine decarboxylase activity is essential for the ... RNAi silencing of three homologues of S-adenosylmethionine decarboxylase gene in tapetal tissue of tomato results in male ... In the present study, S-adenosylmethionine decarboxylase (SAMDC), a key gene involved in polyamine biosynthesis, has been ...
more infohttps://rd.springer.com/article/10.1007/s11103-013-0051-2
The functional intronless S-adenosylmethionine decarboxylase gene of the mouse (Amd-2) is linked to the ornithine decarboxylase...  The functional intronless S-adenosylmethionine decarboxylase gene of the mouse (Amd-2) is linked to the ornithine decarboxylase...
... is linked to the ornithine decarboxylase gene (Odc) on Chromosome 12 and is present in distantly related species of the genus ... "The functional intronless S-adenosylmethionine decarboxylase gene of the mouse (Amd-2) ... The functional intronless S-adenosylmethionine decarboxylase gene of the mouse (Amd-2) is linked to the ornithine decarboxylase ... The functional intronless S-adenosylmethionine decarboxylase gene of the mouse (Amd-2) is linked to the ornithine decarboxylase ...
more infohttps://www.deepdyve.com/lp/springer_journal/the-functional-intronless-s-adenosylmethionine-decarboxylase-gene-of-MHl9x0vtMC
Delineation of functional roles of parasite-specific inserts in the malarial S-adenosylmethionine decarboxylase / ornithine...  Delineation of functional roles of parasite-specific inserts in the malarial S-adenosylmethionine decarboxylase / ornithine...
Delineation of functional roles of parasite-specific inserts in the malarial S-adenosylmethionine decarboxylase / ornithine ... Delineation of functional roles of parasite-specific inserts in the malarial S-adenosylmethionine decarboxylase / ornithine ... Ornithine decarboxylase (ODC) and Sadenosylmethionine decarboxylase (AdoMetDC) are the rate-limiting enzymes in polyamine ... activity analysis thereof showed that these inserts are essential for the catalytic activities of both the decarboxylase ...
more infohttps://repository.up.ac.za/handle/2263/26979
A phage display study of interacting peptide binding partners of malarial S-Adenosylmethionine decarboxylase/Ornithine...  A phage display study of interacting peptide binding partners of malarial S-Adenosylmethionine decarboxylase/Ornithine...
... namely ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC). The AdoMetDC/ODC domains are assembled ... A phage display study of interacting peptide binding partners of malarial S-Adenosylmethionine decarboxylase/Ornithine ... A phage display study of interacting peptide binding partners of malarial S-Adenosylmethionine decarboxylase/Ornithine ... Inhibition of both decarboxylase activities is curative of murine malaria and indicates the viability of such strategies in ...
more infohttps://repository.up.ac.za/handle/2263/24105
The pivotal roles of the plant S-adenosylmethionine decarboxylase 5′ untranslated leader sequence in regulation of gene...  The pivotal roles of the plant S-adenosylmethionine decarboxylase 5′ untranslated leader sequence in regulation of gene...
S-Adenosylmethionine decarboxylase (SAMDC; EC 4.1.1.50) is a key rate-limiting enzyme located in the polyamine biosynthesis ... Hu, W.-W., Gong, H., Eng, C.P. (2005). The pivotal roles of the plant S-adenosylmethionine decarboxylase 5′ untranslated leader ... The pivotal roles of the plant S-adenosylmethionine decarboxylase 5′ untranslated leader sequence in regulation of gene ...
more infohttp://scholarbank.nus.edu.sg/handle/10635/101986
Polyamine Cell Signaling | SpringerLink  Polyamine Cell Signaling | SpringerLink
Regulation of S-Adenosylmethionine Decarboxylase Colin Hanfrey. Pages 449-464 * Genetic Engineering of Polyamine Catabolism in ...
more infohttps://link.springer.com/book/10.1007%2F978-1-59745-145-1
Search: All Pfam signatures | InterPro | EMBL-EBI  Search: All Pfam signatures | InterPro | EMBL-EBI
S-adenosylmethionine decarboxylase (IPR001985) Pfam signature: PF01536 Herpesvirus glycoprotein D/GG/GX domain (IPR002896) Pfam ... Orn/DAP/Arg decarboxylase 2, C-terminal (IPR022643) Pfam signature: PF00278 Proteinase inhibitor I13, potato inhibitor I ( ... S-adenosylmethionine synthetase, N-terminal (IPR022628) Pfam signature: PF00438 Bromodomain (IPR001487) Pfam signature: PF00439 ... Orotidine 5'-phosphate decarboxylase domain (IPR001754) Pfam signature: PF00215 Histone-like DNA-binding protein (IPR000119) ...
more infohttp://www.ebi.ac.uk/interpro/member-database/Pfam
Recent Advances in Polyamine Metabolism and Abiotic Stress Tolerance  Recent Advances in Polyamine Metabolism and Abiotic Stress Tolerance
... dcSAM is synthesized by action of S-adenosylmethionine decarboxylase (AdoMetDC; EC 4.1.4.50) on S-adenosyl-methionine which in ... S-adenosylmethionine decarboxylase (EC 4.1.4.50); AIH: agmatine iminohydrolase (EC 3.5.3.12); CPA: N-carbamoylputrescine ... Figure 1: Polyamine biosynthetic pathway with special reference to plants. ADC: arginine decarboxylase (EC 4.1.1.9); AdoMetDC: ... I. Hummel, G. Gouesbet, A. El Amrani, A. Aïnouche, and I. Couée, "Characterization of the two arginine decarboxylase (polyamine ...
more infohttps://www.hindawi.com/journals/bmri/2014/239621/
Plus it  Plus it
... ornithine decarboxylase; PAO, polyamine oxidase; SAMDC, S-adenosylmethionine decarboxylase; SSAT, spermidine/spermine N1 ... Manni A., Wechter R., Gilmour S., Verderame M. F., Mauger D., Demers L. M. Ornithine decarboxylase over-expression stimulates ...
more infohttp://cancerres.aacrjournals.org/content/63/13/3619
Anti-AMD1 antibody (ab65820) | Abcam  Anti-AMD1 antibody (ab65820) | Abcam
S adenosylmethionine decarboxylase 1 antibody. *S adenosylmethionine decarboxylase proenzyme antibody. *S-adenosylmethionine ...
more infohttps://www.abcam.com/amd1-antibody-ab65820.html
KEGG PATHWAY: hsa00270  KEGG PATHWAY: hsa00270
AMD1; adenosylmethionine decarboxylase 1 [KO:K01611] [EC:4.1.1.50]. 6723 SRM; spermidine synthase [KO:K00797] [EC:2.5.1.16]. ... In bacteria and plants, methionine is synthesized from aspartate [MD:M00017]. S-Adenosylmethionine (SAM), synthesized from ...
more infohttps://www.genome.jp/dbget-bin/www_bget?hsa00270
KEGG BRITE: Enzymes - Xanthobacter autotrophicus  KEGG BRITE: Enzymes - Xanthobacter autotrophicus
4.1.1.50 adenosylmethionine decarboxylase 4.1.1.51 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase ...
more infohttp://www.genome.jp/kegg-bin/get_htext?xau01000+Xaut_1917
Deoxyadenosines
      - Deoxyadenosine
     Summary Report | CureHunter  Deoxyadenosines - Deoxyadenosine Summary Report | CureHunter
Adenosylmethionine Decarboxylase 5. Adenosine 6. Adenosine Deaminase 7. DNA (Deoxyribonucleic Acid) 8. Deoxyguanosine ...
more infohttp://www.curehunter.com/public/keywordSummaryD003839-Deoxyadenosines-Deoxyadenosine.do
GO Gene List  GO Gene List
S-adenosylmethionine decarboxylase 1. NM_009665. Gene Info. Amd2. S-adenosylmethionine decarboxylase 2. NM_007444. Gene Info. ... Mevalonate (diphospho) decarboxylase. NM_138656. Gene Info. Neil1. Nei endonuclease VIII-like 1 (E. coli). NM_028347. Gene Info ... Cysteine sulfinic acid decarboxylase. NM_144942. Gene Info. Cth. Cystathionase (cystathionine gamma-lyase). NM_145953. Gene ... UDP-glucuronate decarboxylase 1. NM_026430. Gene Info. Xrcc6. X-ray repair complementing defective repair in Chinese hamster ...
more infohttps://cgap.nci.nih.gov/Genes/GoGeneQuery?PAGE=1&ORG=Mm&GOID=0016829
  • 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. (wikipedia.org)