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Catalyze the hydrolysis of nucleotides with the elimination of ammonia.
An enzyme that catalyzes the deamination of AMP to IMP. EC 3.5.4.6.
DNA analogs containing neutral amide backbone linkages composed of aminoethyl glycine units instead of the usual phosphodiester linkage of deoxyribose groups. Peptide nucleic acids have high biological stability and higher affinity for complementary DNA or RNA sequences than analogous DNA oligomers.
Drugs that inhibit ADENOSINE DEAMINASE activity.
Catalyze the hydrolysis of nucleosides with the elimination of ammonia.
(GTP cyclohydrolase I) or GTP 7,8-8,9-dihydrolase (pyrophosphate-forming) (GTP cyclohydrolase II). An enzyme group that hydrolyzes the imidazole ring of GTP, releasing carbon-8 as formate. Two C-N bonds are hydrolyzed and the pentase unit is isomerized. This is the first step in the synthesis of folic acid from GTP. EC 3.5.4.16 (GTP cyclohydrolase I) and EC 3.5.4.25 (GTP cyclohydrolase II).
Nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. The richest natural source is yeast. It occurs in the free form only in the retina of the eye, in whey, and in urine; its principal forms in tissues and cells are as FLAVIN MONONUCLEOTIDE and FLAVIN-ADENINE DINUCLEOTIDE.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
A natural product that has been considered as a growth factor for some insects.
Compounds based on 2-amino-4-hydroxypteridine.
A group of compounds that are derivatives of heptanedioic acid with the general formula R-C7H11O4.
NATIONAL LIBRARY OF MEDICINE service for health professionals and consumers. It links extensive information from the National Institutes of Health and other reviewed sources of information on specific diseases and conditions.
An essential amino acid. It is often added to animal feed.
A nonmetallic element with atomic symbol C, atomic number 6, and atomic weight [12.0096; 12.0116]. It may occur as several different allotropes including DIAMOND; CHARCOAL; and GRAPHITE; and as SOOT from incompletely burned fuel.
An inhibitor of nucleotide metabolism.
An inbred strain of Long-Evans rats that develops hyperglycemia, hyperinsulinemia, and mild obesity, mostly in males, that resembles non-insulin-dependent diabetes mellitus in humans. It was developed from outbred Long-Evans stock in 1983.
Exclusive legal rights or privileges applied to inventions, plants, etc.
An enzyme that catalyzes the hydrolytic deamination of deoxycytidylic acid to deoxyuridylic acid and ammonia. It plays an important role in the regulation of the pool of deoxynucleotides in higher organisms. The enzyme also acts on some 5-substituted deoxycytidylic acids. EC 3.5.4.12.
An enzyme that catalyzes the deamination of cytidine, forming uridine. EC 3.5.4.5.
A novel composition, device, or process, independently conceived de novo or derived from a pre-existing model.
An enzyme that catalyzes the hydrolysis of ADENOSINE to INOSINE with the elimination of AMMONIA.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Toxins closely associated with the living cytoplasm or cell wall of certain microorganisms, which do not readily diffuse into the culture medium, but are released upon lysis of the cells.
An enzyme that transfers methyl groups from O(6)-methylguanine, and other methylated moieties of DNA, to a cysteine residue in itself, thus repairing alkylated DNA in a single-step reaction. EC 2.1.1.63.
Family of RNA viruses that infects birds and mammals and encodes the enzyme reverse transcriptase. The family contains seven genera: DELTARETROVIRUS; LENTIVIRUS; RETROVIRUSES TYPE B, MAMMALIAN; ALPHARETROVIRUS; GAMMARETROVIRUS; RETROVIRUSES TYPE D; and SPUMAVIRUS. A key feature of retrovirus biology is the synthesis of a DNA copy of the genome which is integrated into cellular DNA. After integration it is sometimes not expressed but maintained in a latent state (PROVIRUSES).
Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).
A rare inherited immunodeficiency syndrome characterized by normal or elevated serum IMMUNOGLOBULIN M levels with absence of IMMUNOGLOBULIN G; IMMUNOGLOBULIN A; and IMMUNOGLOBULIN E. It results in a profound susceptibility to BACTERIAL INFECTIONS and an increased susceptibility to OPPORTUNISTIC INFECTIONS. Several subtypes of hyper-IgM immunodeficiency syndrome exist depending upon the location of genetic mutation.
The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.
Antibodies produced by a single clone of cells.
Immunoglobulins produced in response to VIRAL ANTIGENS.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.

MOT1 can activate basal transcription in vitro by regulating the distribution of TATA binding protein between promoter and nonpromoter sites. (1/447)

MOT1 is an ATPase which can dissociate TATA binding protein (TBP)-DNA complexes in a reaction requiring ATP hydrolysis. Consistent with this observation, MOT1 can repress basal transcription in vitro. Paradoxically, however, some genes, such as HIS4, appear to require MOT1 as an activator of transcription in vivo. To further investigate the function of MOT1 in basal transcription, we performed in vitro transcription reactions using yeast nuclear extracts depleted of MOT1. Quantitation of MOT1 revealed that it is an abundant protein, with nuclear extracts from wild-type cells containing a molar excess of MOT1 over TBP. Surprisingly, MOT1 can weakly activate basal transcription in vitro. This activation by MOT1 is detectable with amounts of MOT1 that are approximately stoichiometric to TBP. With amounts of MOT1 similar to those present in wild-type nuclear extracts, MOT1 behaves as a weak repressor of basal transcription. These results suggest that MOT1 might activate transcription via an indirect mechanism in which limiting TBP can be liberated from nonpromoter sites for use at promoters. In support of this idea, excess nonpromoter DNA sequesters TBP and represses transcription, but this effect can be reversed by addition of MOT1. These results help to reconcile previous in vitro and in vivo results and expand the repertoire of transcriptional control strategies to include factor-assisted redistribution of TBP between promoter and nonpromoter sites.  (+info)

A methenyl tetrahydromethanopterin cyclohydrolase and a methenyl tetrahydrofolate cyclohydrolase in Methylobacterium extorquens AM1. (2/447)

Recently it was found that Methylobacterium extorquens AM1 contains both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F) as carriers of C1 units. In this paper we report that the aerobic methylotroph contains a methenyl H4MPT cyclohydrolase (0.9 U x mg-1 cell extract protein) and a methenyl H4F cyclohydrolase (0.23 U x mg-1). Both enzymes, which were specific for their substrates, were purified and characterized and the encoding genes identified via the N-terminal amino acid sequence. The purified methenyl H4MPT cyclohydrolase with a specific activity of 630 U x mg-1 (Vmax = 1500 U x mg-1; Km = 30 microm) was found to be composed of two identical subunits of molecular mass 33 kDa. Its sequence was approximately 40% identical to that of methenyl H4MPT cyclohydrolases from methanogenic archaea. The methenyl H4F cyclohydrolase with a specific activity of 100 U x mg-1 (Vmax = 330 U x mg-1; Km = 80 microm) was found to be composed of two identical subunits of molecular mass 22 kDa. Its sequence was not similar to that of methenyl H4MPT cyclohydrolases or to that of other methenyl H4F cyclohydrolases. Based on the specific activities in cell extract and from the growth properties of insertion mutants it is suggested that the methenyl H4MPT cyclohydrolase might have a catabolic, and the methenyl-H4F cyclohydrolase an anabolic function in the C1-unit metabolism of M. extorquens AM1.  (+info)

Maximal stimulation of meiotic recombination by a yeast transcription factor requires the transcription activation domain and a DNA-binding domain. (3/447)

The DNA sequences located upstream of the yeast HIS4 represent a very strong meiotic recombination hotspot. Although the activity of this hotspot requires the transcription activator Rap1p, the level of HIS4 transcription is not directly related to the level of recombination. We find that the recombination-stimulating activity of Rap1p requires the transcription activation domain of the protein. We show that a hybrid protein with the Gal4p DNA-binding domain and the Rap1p activation domain can stimulate recombination in a strain in which Gal4p-binding sites are inserted upstream of HIS4. In addition, we find recombination hotspot activity associated with the Gal4p DNA-binding sites that is independent of known transcription factors. We suggest that yeast cells have two types of recombination hotspots, alpha (transcription factor dependent) and beta (transcription factor independent).  (+info)

The crystal structure of a bacterial, bifunctional 5,10 methylene-tetrahydrofolate dehydrogenase/cyclohydrolase. (4/447)

The structure of a bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/cyclohydrolase from Escherichia coli has been determined at 2.5 A resolution in the absence of bound substrates and compared to the NADP-bound structure of the homologous enzyme domains from a trifunctional human synthetase enzyme. Superposition of these structures allows the identification of a highly conserved cluster of basic residues that are appropriately positioned to serve as a binding site for the poly-gamma-glutamyl tail of the tetrahydrofolate substrate. Modeling studies and molecular dynamic simulations of bound methylene-tetrahydrofolate and NADP shows that this binding site would allow interaction of the nicotinamide and pterin rings in the dehydrogenase active site. Comparison of these enzymes also indicates differences between their active sites that might allow the development of inhibitors specific to the bacterial target.  (+info)

Chromatin opening and transactivator potentiation by RAP1 in Saccharomyces cerevisiae. (5/447)

Transcriptional activators function in vivo via binding sites that may be packaged into chromatin. Here we show that whereas the transcriptional activator GAL4 is strongly able to perturb chromatin structure via a nucleosomal binding site in yeast, GCN4 does so poorly. Correspondingly, GCN4 requires assistance from an accessory protein, RAP1, for activation of the HIS4 promoter, whereas GAL4 does not. The requirement for RAP1 for GCN4-mediated HIS4 activation is dictated by the DNA-binding domain of GCN4 and not the activation domain, suggesting that RAP1 assists GCN4 in gaining access to its binding site. Consistent with this, overexpression of GCN4 partially alleviates the requirement for RAP1, whereas HIS4 activation via a weak GAL4 binding site requires RAP1. RAP1 is extremely effective at interfering with positioning of a nucleosome containing its binding site, consistent with a role in opening chromatin at the HIS4 promoter. Furthermore, increasing the spacing between binding sites for RAP1 and GCN4 by 5 or 10 bp does not impair HIS4 activation, indicating that cooperative protein-protein interactions are not involved in transcriptional facilitation by RAP1. We conclude that an important role of RAP1 is to assist activator binding by opening chromatin.  (+info)

A set of independent selectable markers for transfection of the human malaria parasite Plasmodium falciparum. (6/447)

Genomic information is rapidly accumulating for the human malaria pathogen, Plasmodium falciparum. Our ability to perform genetic manipulations to understand Plasmodium gene function is limited. Dihydrofolate reductase is the only selectable marker presently available for transfection of P. falciparum. Additional markers are needed for complementation and for expression of mutated forms of essential genes. We tested parasite sensitivity to different drugs for which selectable markers are available. Two of these drugs that were very effective as antiplasmodial inhibitors in culture, blasticidin and geneticin (G418), were selected for further study. The genes BSD, encoding blasticidin S deaminase of Aspergillus terreus, and NEO, encoding neomycin phosphotransferase II from transposon Tn 5, were expressed under the histidine-rich protein III (HRPIII) gene promoter and tested for their ability to confer resistance to blasticidin or G418, respectively. After transfection, blasticidin and G418-resistant parasites tested positive for plasmid replication and BSD or NEO expression. Cross-resistance assays indicate that these markers are independent. The plasmid copy number and the enzymatic activity depended directly on the concentration of the drug used for selection. These markers set the stage for new methods of functional analysis of the P. falciparum genome.  (+info)

Efficient expression, purification and crystallisation of two hyperthermostable enzymes of histidine biosynthesis. (7/447)

Enzymes from hyperthermophiles can be efficiently purified after expression in mesophilic hosts and are well-suited for crystallisation attempts. Two enzymes of histidine biosynthesis from Thermotoga maritima, N'-((5'-phosphoribosyl)-formimino)-5-aminoimidazol-4-carb oxamid ribonucleotide isomerase and the cyclase moiety of imidazoleglycerol phosphate synthase, were overexpressed in Escherichia coli, both in their native and seleno-methionine-labelled forms, purified by heat precipitation of host proteins and crystallised. N'-((5'-phosphoribosyl)-formimino)-5-aminoimidazol-4-carb oxamid ribonucleotide isomerase crystallised in four different forms, all suitable for X-ray structure solution, and the cyclase moiety of imidazoleglycerol phosphate synthase yielded one crystal form that diffracted to atomic resolution. The obtained crystals will enable the determination of the first three-dimensional structures of enzymes from the histidine biosynthetic pathway.  (+info)

Distribution of tetrahydromethanopterin-dependent enzymes in methylotrophic bacteria and phylogeny of methenyl tetrahydromethanopterin cyclohydrolases. (8/447)

The methylotrophic proteobacterium Methylobacterium extorquens AM1 possesses tetrahydromethanopterin (H(4)MPT)-dependent enzymes, which are otherwise specific to methanogenic and sulfate-reducing archaea and which have been suggested to be involved in formaldehyde oxidation to CO(2) in M. extorquens AM1. The distribution of H(4)MPT-dependent enzyme activities in cell extracts of methylotrophic bacteria from 13 different genera are reported. H(4)MPT-dependent activities were detected in all of the methylotrophic and methanotrophic proteobacteria tested that assimilate formaldehyde by the serine or ribulose monophosphate pathway. H(4)MPT-dependent activities were also found in autotrophic Xanthobacter strains. However, no H(4)MPT-dependent enzyme activities could be detected in other autotrophic alpha-proteobacteria or in gram-positive methylotrophic bacteria. Genes encoding methenyl H(4)MPT cyclohydrolase (mch genes) were cloned and sequenced from several proteobacteria. Bacterial and archaeal Mch sequences have roughly 35% amino acid identity and form distinct groups in phylogenetic analysis.  (+info)

Nitrosopumilus maritimus Imidazole glycerol phosphate synthase subunit HisF (hisF) datasheet and description hight quality product and Backed by our Guarantee
Burkholderia dolosa strain LMG18942 histidinol-phosphate aminotransferase (hisC) gene, partial cds; imidazole glycerol phosphate dehydratase (hisB), multiple antibiotic resistance-related protein (marC), imidazole glycerol phosphate synthase glutamine amidotransferase subunit (hisH), phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase (hisA), imidazole glycerol phosphate synthase subunit (hisF), phosphoribosyl-AMP cyclohydrolase (hisI), and phosphoribosyl-ATP pyrophosphohydrolase (hisE) genes, complete cds; and membrane protein gene, partial ...
Burkholderia ambifaria strain LMG19467 histidinol-phosphate aminotransferase (hisC) gene, partial cds; imidazole glycerol phosphate dehydratase (hisB), multiple antibiotic resistance-related protein (marC), imidazole glycerol phosphate synthase glutamine amidotransferase subunit (hisH), phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase (hisA), imidazole glycerol phosphate synthase subunit (hisF), phosphoribosyl-AMP cyclohydrolase (hisI), and phosphoribosyl-ATP pyrophosphohydrolase (hisE) genes, complete cds; and membrane protein gene, partial ...
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The glutamine amidotransferase domain provides the ammonia necessary to the cyclase domain to produce IGP and AICAR from PRFAR.
2A0N: Crystal structure of Imidazole glycerol phosphate synthase subunit hisF (EC 4.1.3.-) (tm1036) from Thermotoga maritima at 1.64 A resolution
Nitrilases attract increasing attention due to their utility in the mild hydrolysis of nitriles. According to activity and gene screening, filamentous fungi are a rich source of nitrilases distinct in evolution from their widely examined bacterial counterparts. However, fungal nitrilases have been less explored than the bacterial ones. Nitrilases are typically heterogeneous in their quaternary structures, forming short spirals and extended filaments, these features making their structural studies difficult. A nitrilase gene was amplified by PCR from the cDNA library of Aspergillus niger K10. The PCR product was ligated into expression vectors pET-30(+) and pRSET B to construct plasmids pOK101 and pOK102, respectively. The recombinant nitrilase (Nit-ANigRec) expressed in Escherichia coli BL21-Gold(DE3)(pOK101/pTf16) was purified with an about 2-fold increase in specific activity and 35% yield. The apparent subunit size was 42.7 kDa, which is approx. 4 kDa higher than that of the enzyme isolated from the
Nitrilases (standard format) - We offer a range of biocatalysts in easy-to-use kits. Click here to find out more about this product.
Imidazole glycerol phosphate synthase subunit HisF; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit (266 aa ...
We have suggested an alignment of three cyanide degrading nitrilases to the crystallographically determined structures of Nit and DCase which was primarily created using GenTHREADER.. We have also aligned the structures of Nit and DCase using ALIGN. (see superpose.pdb). From this we have concluded that insertions and deletions in the cyanide degrading enzymes occur in externally located loops and that there are two major insertions, one major deletion and a substantial C-terminal extension.. An important difference between our enzymes, and indeed the majority of nitrilases, and the solved structures of superfamily members is the formation of spiral oligomers comprising specific numbers of subunits - but different numbers of subunits (ranging from 10-18) in different enzymes. We have postulated that the interaction that leads to the formation of the oligomer is due to an 15 amino acid insertion found in the loop between the beta strands labelled NS9 and NS10 in Nit. This, we postulate, leads to ...
Adenine Deaminase (EC 3.5.4.2) [2µM]: 786-428 by G-Biosciences at Labscoop.com - Read reviews, citations, datasheets, protocols & more.
Dear colleagues, can anyone direct me to a commercial source of imidazole glycerol or imidazole acetol? Please refrain from suggesting Sigma, Aldrich or Fluka Many thanks, Dudley Page ...
Define Methenyl. Methenyl synonyms, Methenyl pronunciation, Methenyl translation, English dictionary definition of Methenyl. n. 1. The hypothetical hydrocarbon radical CH, regarded as an essential residue of certain organic compounds. Websters Revised Unabridged Dictionary,...
This gene encodes a member of the nitrilase protein family with homology to bacterial and plant nitrilases, enzymes that cleave nitriles and organic amides to the corresponding carboxylic acids plus ammonia. Multiple transcript variants encoding different isoforms have been found for this gene ...
This clade of sequences is highly similar to the HisF protein, but generally represents the second HisF homolog in the genome where the other is an authentic HisF observed in the context of a complete histidine biosynthesis operon. The similarity between these WbuZ sequences and true HisFs is such that often the closest match by BLAST of a WbuZ is a HisF. Only by making a multiple sequence alignment is the homology relationship among the WbuZ sequences made apparent. WbuZ genes are invariably observed in the presence of a homolog of the HisH protein (designated WbuY) and a proposed N-acetyl sugar amidotransferase designated in WbuX in E. coli [1], IfnA in P. aeriginosa [2] and PseA in C. jejuni [3]. Similarly, this trio of genes is invariably found in the context of saccharide biosynthesis loci. It has been shown that the WbuYZ homologs are not essential components of the activity expressed by WbuX, leading to the proposal that these to proteins provide ammonium ions to the amidotransferase when ...
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A. Visan, M. Miroiu, C. Nita, R. Cristescu, G. Socol, N. Stefan, G. Dorcioman, N. Serban, M. Socol, I. Zgura, O.L. Rasoga, C. Breazu, L. Sima, C. R. Luculescu, A. Stanculescu, I.N. Mihailescu ...
Shop Indole-3-glycerol phosphate synthase ELISA Kit, Recombinant Protein and Indole-3-glycerol phosphate synthase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Indole-3-glycerol phosphate synthase (IGPS) catalyzes the irreversible ring closure of 1-(ocarboxyphenylamino)- 1-deoxyribulose 5- phosphate (CdRP) into indole-3-glycerol phosphate (IGP) during the fourth step in tryptophan biosynthesis. Analysis of the crystal structure of IGPS from Mycobacterium tuberculosis (MtIGPS) hinted the importance of Lys119 for binding or catalysis. Lys110 from sulfolobus sulfataricus IGPS (ssIGPS) that aligns with Lys119 from MtIGPS, was proposed to be a general acid for the proton transfer that initiates the ring closure and decarboxylation of CdRP. To study the importance of Lys119 in the chemical mechanism for MtIGPS, an amino acid change was made at this position to study any changes in catalytic function or substrate binding affinity. Kinetic assays were performed and interesting, a mutation to alanine had a dramatic effect on the activity of MtIGPS. Our studies highlight the importance of Lys119 in the MtIGPS-catalyzed chemical mechanism.
Guanine deaminase Proteins available through Novus Biologicals. Browse our Guanine deaminase Protein catalog backed by our Guarantee+.
Please cite Turkarslan et al., 2017 Mol. Sys. Biol. if you find Syntrophy Portal useful.. Acknowledgement: This material by ENIGMA- Ecosystems and Networks Integrated with Genes and Molecular Assemblies (http://enigma.lbl.gov), a Scientific Focus Area Program at Lawrence Berkeley National Laboratory is based upon work supported by the U.S. Department of Energy, Office of Science, Office of Biological & Environmental Research under contract number DE-AC02-05CH11231 ...
casSAR Dugability of Q9Y2T3 | GDA | Guanine deaminase - Also known as GUAD_HUMAN, GDA, KIAA1258. Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia. Homodimer.
Enzymes involved in tetrahydrofolate metabolism are of particular pharmaceutical interest, as their function is crucial for amino acid and DNA biosynthesis. The crystal structure of the human cytosolic methylenetetrahydrofolate dehydrogenase/cyclohydrolase (DC301) domain of a trifunctional enzyme has been determined previously with a bound NADP cofactor. While the substrate binding site was identified to be localized in a deep and rather hydrophobic cleft at the interface between two protein domains, the unambiguous assignment of catalytic residues was not possible. We succeeded in determining the crystal structures of three ternary DC301/NADP/inhibitor complexes. Investigation of these structures followed by site-directed mutagenesis studies allowed identification of the amino acids involved in catalysis by both enzyme activities. The inhibitors bind close to Lys56 and Tyr52, residues of a strictly conserved motif for active sites in dehydrogenases. While Lys56 is in a good position for ...
Nit Protein; One Of Two Proteins In S. Cerevisiae With Similarity To The Nit Domain Of NitFhit From Fly And Worm And To The Mouse And Human Nit Protein Which Interacts With The Fhit Tumor Suppressor; Nitrilase Superfamily Member
Dichotomous Effects of Isometric Secondary Amines Containing an Aromatic Nitrile and a Nitro Group on Human Aortic Smooth Muscle Cells: Syntheses, Nitrosation and Cell Culture Studies ...
Dichotomous Effects of Isometric Secondary Amines Containing an Aromatic Nitrile and a Nitro Group on Human Aortic Smooth Muscle Cells: Syntheses, Nitrosation and Cell Culture Studies ...
trpC - Indole-3-glycerol phosphate synthase; Involved in tryptophan biosynthesis; amino acid biosynthesis; converts 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate to C(1)-(3-indolyl)-glycerol 3-phosphate and carbon dioxide and water; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TrpC family [a.k.a. JL37_03690, KGE00121.1, indole-3-glycerol-phosphate synthase, Indole-3-glycerol-phosphate synthase] ...
SWISS-MODEL Repository entry for Q92N33 (ADEC1_RHIME), Adenine deaminase 1. Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobiummeliloti)
A cardiopatia congênita (CC) é a malformação congênita mais comum, embora ainda seja relativamente rara. O rastreamento de cardiopatia congênita inclui ultrassonografia no segundo trimestre da gestação e exame clínico pós-parto; no entanto, as taxas de detecção são baixas. O reconhecimento prec...
Berezov, T T., Activity of omega-amidase in human and animal malignant neoplasms. (russ.) (1966). Subject Strain Bibliography 1966. 266 ...
La cardiopatía congénita (CC) es el defecto congénito más frecuente, aunque sigue siendo relativamente raro. El cribado para detectar la cardiopatía congénita incluye la ecografía en el segundo trimestre del embarazo y la exploración clínica posnatal; no obstante, las tasas de detección son redu...
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Plasmid lentiCas9-Blast from Dr. Feng Zhangs lab contains the inserts Cas9 and Blasticidin resistance and is published in Nat Methods. 2014 Aug;11(8):783-4. doi: 10.1038/nmeth.3047. This plasmid is available through Addgene.
NIR og NIT instrumenter er i dag blitt uunværlige analyseverktøy for kornmottak og fôrprodusenter som krever raske svar på viktige kvalitetsparametre som f.eks. fett, protein, vanninnhold, stivelse og aske, samt hektolitervekt for korn ...
Order Recombinant Prochlorococcus marinus subsp pastoris Indole-3-glycerol phosphate synthase trpC 01015965649 at Gentaur Prochlorococcus marinus subsp. pastoris Indole-3-glycerol phosphate synthase (trpC)
In eukaryotes, folate-dependent one-carbon (1-C) metabolism is composed of two parallel pathways compartmentalized to either the cytoplasm or mitochondria. In each, 1-C units, carried on tetrahydrofolate (THF), are interconverted by four catalytic activities. Serine hydroxymethyltransferase transfers the 3-carbon of serine to THF forming 5,10-methylene-THF which is oxidized in 3 successive steps to formate via the intermediates, 5,10-methenyl-THF and 10-formyl-THF. Because of the redox potential in each compartment, 1-C flux is thought by most authors to be from formate to serine in the cytosol and in the opposite direction in mitochondria. Transport of serine, glycine and formate across the mitochondrial membranes creates a 1-C cycle. All eukaryotes characterized to date contain a cytoplasmic trifunctional C1-THF synthase possessing 5,10-methylene-THF dehydrogenase, 5,10-methenyl-THF cyclohydrolase and 10-formyl-THF synthetase activities which interconvert the catalytic intermediates between ...
ID TRPC_SYNR3 Reviewed; 294 AA. AC A5GRL0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 11-DEC-2019, entry version 64. DE RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000255,HAMAP-Rule:MF_00134}; DE Short=IGPS {ECO:0000255,HAMAP-Rule:MF_00134}; DE EC=4.1.1.48 {ECO:0000255,HAMAP-Rule:MF_00134}; GN Name=trpC {ECO:0000255,HAMAP-Rule:MF_00134}; GN OrderedLocusNames=SynRCC307_0616; OS Synechococcus sp. (strain RCC307). OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus; OC unclassified Synechococcus. OX NCBI_TaxID=316278; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCC307; RG Genoscope; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) CC = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O; CC Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16526, ...
Understanding how the flexibility inherent in protein structures is related to their amazing catalytic power is a timely question that has applications in drug development and protein design. My review in 2008 in Nature Chemical Biology discusses this concept extensively. I and my students are working on understanding this important problem in two model systems: Dihydrofolate reductase from Geobacillus stearothermophilus (DHFR) and Indole-3-glycerol phosphate synthase from Sulfolobus solfataricus (IGPS). Working on one of these projects, a student will be trained in mutagenesis, protein expression and purification, attachment of probes to proteins, enzyme kinetics, ligand binding measurements and computational modeling of enzyme kinetics ...
Live attenuated vaccines are superior to the killed or subunit vaccines. We designed a Salmonella Typhimurium strain by deleting folD gene (encoding methylenetetrahydrofolate dehydrogenase-cyclohydrolase) in the presence of a heterologous fhs gene (encoding formyltetrahydrofolate synthetase) and tested its vaccine potential under stringent conditions of lethal and sub-lethal challenges with virule ...
To sustain their proliferation, cancer cells become dependent on one-carbon metabolism to support purine and thymidylate synthesis. Indeed, one of the most highly upregulated enzymes during neoplastic transformation is MTHFD2, a mitochondrial methylenetetrahydrofolate dehydrogenase and cyclohydrolase involved in one-carbon metabolism. Because MTHFD2 is expressed normally only during embryonic development, it offers a disease-selective therapeutic target for eradicating cancer cells while sparing healthy cells. Here we report the synthesis and preclinical characterization of the first inhibitor of human MTHFD2. We also disclose the first crystal structure of MTHFD2 in complex with a substrate-based inhibitor and the enzyme cofactors NAD+ and inorganic phosphate. Our work provides a rationale for continued development of a structural framework for the generation of potent and selective MTHFD2 inhibitors for cancer treatment. Cancer Res; 77(4); 937-48. ©2017 AACR. ...
Aryl nitriles are important structural motifs found in pharmaceuticals, agrochemicals, and natural products.1 Furthermore, aromatic nitriles are versatile synthetic precursors and useful intermediates because they can be easily transformed into a diverse class of functionalities, such as amides, esters, primary amines, aldehydes, and carboxylic acids.2 Consequently, the development of efficient methods for the synthesis of aryl nitriles has drawn much attention from the organic synthetic community.3 The Sandmeyer and Rosenmund-von Braun reactions are two typical methods for the preparation of aromatic nitriles.4 The transition metal-catalyzed cyanations of aryl halides, aryl boronic acids and arenes with various cyanating agents have emerged as an alternative route to aryl nitriles.5 However, these protocols suffer from drawbacks, such as the use of an expensive transition-metal catalyst or stoichiometric amounts of mostly toxic metal cyanides and harsh reaction conditions.6 Recently, the search ...
The methylenetetrahydrofolate dehydrogenase (MTHFD1) gene, as one of the key genes involved in the folate pathway, has been reported to play a critical role in
SEQUESTRATION OF FORMALDEHYDE TO STABILIZE NITRILASE SPECIFIC ACTIVITY WHEN CONVERTING GLYCOLONITRILE TO GLYCOLIC ACID - diagram, schematic, and image 57 ...
SEQUESTRATION OF FORMALDEHYDE TO STABILIZE NITRILASE SPECIFIC ACTIVITY WHEN CONVERTING GLYCOLONITRILE TO GLYCOLIC ACID - diagram, schematic, and image 82 ...
carbamate = H2N-CO-O-. Other name(s): cyanate lyase; cyanate hydrolase; cyanase; cyanate aminohydrolase; cyanate C-N-lyase; cyanate hydratase Systematic name: carbamate hydro-lyase. Comments: This enzyme, which is found in bacteria and plants, is used to decompose cyanate, which can be used as the sole source of nitrogen [6,7]. Reaction (1) can be considered as the reverse of carbamate = cyanate + H2O, where this is assisted by reaction with bicarbonate and carbon dioxide (see mechanism above) [2], and hence is classified in sub-subclass 4.2.1. Bicarbonate functions as a recycling substrate [2].. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 37289-24-0. References:. 1. Anderson, P.M. Purification and properties of the inducible enzyme cyanase. Biochemistry 19 (1980) 2882-2888. [PMID: 6994799]. 2. Johnson, W.V. and Anderson, P.M. Bicarbonate is a recycling substrate for cyanase. J. Biol. Chem. 262 (1987) 9021-9025. [PMID: 3110153]. 3. Taussig, A. The ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
It was sometime around 1999 or 2000 and i had just finished being interviewed by George Stoney for a film he was working on about Paulo Freire. Nita Freire was in town and she stopped by Georges apartment. It was a briefcase or a shoebox, i cant recall, that Nita put on the table. Out poured dozens of photos of Paulos life. The table was inches deep in images from across decades. Nita handled them gently as we sorted through them, making choices about what might work best in the film. She showed George and i and photo when she was a girl in school and a so-very-young Paulo was a new teacher. She told us so lovingly of their life together. As i sorted through the treasures i found a few copies of a bookmark shaped profile topped with a photo of a very young Paulo. In the photo he is very thin and his eyes have an intensity that made me wonder if he had some sense of the future that lay before him. And then there were his ears... Nita let me keep one of the bookmarks ...
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Individuals are considered vulnerable if they are over 65 years of age or if they are already suffering from one of the conditions mentioned hereafter. Those conditions are: • Diabetes • Cardiovascular diseases • Chronic diseases of the respiratory tract • Cancer • An immune deficiency due to a condition or therapy. ...
Well we were finally able to spend a weekend at the lake. It feels like forever since we were able to get out there, but has probably only been a month, really. Our sweet little cabin, where stress is unknown and peaceful relaxation a given. The 11am nap. Of course, nobody is awake to take my … ...
Desordem hereditária caracterizada por espessamento das unhas das mãos e dos pés. Várias variantes clínicas têm sido descritas. Pacientes apresentam ao nascimento ou durante o primeiro ano de vida, hipertrofia e descoloração marrom-amarelada das unhas, em alguns casos associadas com hiperqueratose hiponíquia e do leito ungueal. Hiperqueratose e hiperidrose das palmas das mãos e plantas dos pés, bolhas acrais, queratose folicular e leucoqueratose oral podem também ocorrer. Herança autossômica dominante é a regra, embora casos transmitidos em formas autossômica recessiva foram relatados.. ...
Aminohydrolases. *Guanine deaminase. *Adenosine deaminase. *AMP deaminase. *Inosine monophosphate synthase. *DCMP deaminase ...
Aminohydrolases. *Guanine deaminase. *Adenosine deaminase. *AMP deaminase. *Inosine monophosphate synthase. *DCMP deaminase ...
Aminohydrolases. *Guanine deaminase. *Adenosine deaminase. *AMP deaminase. *Inosine monophosphate synthase. *DCMP deaminase ...
... enzymes (nitrile aminohydrolase; EC 3.5.5.1) catalyse the hydrolysis of nitriles to carboxylic acids and ammonia, ...
The systematic name of this enzyme class is ADP aminohydrolase. Other names in common use include adenosine diphosphate ...
The systematic name of this enzyme class is dCTP aminohydrolase. Other names in common use include deoxycytidine triphosphate ...
The systematic name of this enzyme class is ATP aminohydrolase. This enzyme is also called adenosine triphosphate deaminase. ...
The systematic name of this enzyme class is thiocyanate aminohydrolase. As of late 2007, 4 structures have been solved for this ...
The systematic name of this enzyme class is sepiapterin aminohydrolase. Tsusué M (April 1971). "Studies on sepiapterin ...
The systematic name of this enzyme class is adenine aminohydrolase. Other names in common use include adenase, adenine aminase ...
The systematic name of this enzyme class is arylacetonitrile aminohydrolase. This enzyme participates in cyanoamino acid ...
The systematic name of this enzyme class is cytosine aminohydrolase. This enzyme is also called isocytosine deaminase. This ...
The systematic name of this enzyme class is guanosine aminohydrolase. This enzyme is also called guanosine aminase. Isihida Y, ...
The systematic name of this enzyme class is ricinine aminohydrolase. This enzyme participates in nitrogen metabolism. ROBINSON ...
The systematic name of this enzyme class is 4-aminoimidazole aminohydrolase. This enzyme is also called 4-aminoimidazole ...
The systematic name of this enzyme class is blasticidin-S aminohydrolase. As of late 2007, two structures have been solved for ...
The N-terminal domain is a cysteine, histidine-dependent aminohydrolase amidase. Structurally the synthetase and amidase ...
The systematic name of this enzyme class is 2-aminomuconate aminohydrolase. This enzyme participates in tryptophan metabolism. ...
The systematic name of this enzyme class is dCTP aminohydrolase (dUMP-forming). This enzyme participates in pyrimidine ...
The systematic name of this enzyme class is cytidine/2'-deoxycytidine aminohydrolase. This enzyme participates in pyrimidine ...
The systematic name of this enzyme class is 2-amino-4-hydroxypteridine aminohydrolase. This enzyme is also called acrasinase. ...
The systematic name of this enzyme class is 3-cyano-L-alanine aminohydrolase. This enzyme is also called beta-cyanoalanine ...
The systematic name of this enzyme class is S-adenosyl-L-homocysteine aminohydrolase. This enzyme is also called ...
The systematic name of this enzyme class is 1-aminocyclopropane-1-carboxylate aminohydrolase (isomerizing). This enzyme is also ...
The systematic name of this enzyme class is 3,5-dibromo-4-hydroxybenzonitrile aminohydrolase. This enzyme participates in 1,4- ...
The systematic name of this enzyme class is 1-pyrroline-4-hydroxy-2-carboxylate aminohydrolase (decyclizing). This enzyme is ...
... (EC 3.5.4.32, 8-OGD) is an enzyme with systematic name 8-oxoguanine aminohydrolase. This enzyme ...
... (EC 3.5.1.2, glutaminase I, L-glutaminase, glutamine aminohydrolase) is an amidohydrolase enzyme that generates ...
The systematic name of this enzyme class is 2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol isomerizing). Other ...
... pyrimidine 2-aminohydrolase. This enzyme participates in riboflavin metabolism. As of late 2007, 6 structures have been solved ...
An aminohydrolase is a hydrolase enzyme which acts upon an amino group. Aminohydrolases are classified under EC number EC 3.5.4 ... Aminohydrolases at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal v t e. ...
Aminopyrimidine aminohydrolase (EC 3.5.99.2, thiaminase, thiaminase II, tenA (gene)) is an enzyme with systematic name 4-amino- ... Aminopyrimidine+aminohydrolase at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal. ... 5-aminomethyl-2-methylpyrimidine aminohydrolase. This enzyme catalyses the following chemical reaction (1) 4-amino-5- ...
Adenine aminohydrolase: occurrence and possible significance in trypanosomid flagellates. G W Kidder and L L Nolan ... Adenine aminohydrolase: occurrence and possible significance in trypanosomid flagellates Message Subject (Your Name) has sent ...
Aminopyrimidine aminohydrolaseBy similarity. Manual assertion inferred from sequence similarity toi ... sp,Q4L7X6,TENA_STAHJ Aminopyrimidine aminohydrolase OS=Staphylococcus haemolyticus (strain JCSC1435) OX=279808 GN=tenA PE=3 SV= ...
Putative aminohydrolase SsnAAdd BLAST. 442. Proteomic databases. PaxDb, a database of protein abundance averages across all ... IPR017700. Aminohydrolase_SsnA. IPR011059. Metal-dep_hydrolase_composite. IPR032466. Metal_Hydrolase. Pfam protein domain ... IPR017700. Aminohydrolase_SsnA. IPR011059. Metal-dep_hydrolase_composite. IPR032466. Metal_Hydrolase. Pfam protein domain ... sp,Q46812,SSNA_ECOLI Putative aminohydrolase SsnA OS=Escherichia coli (strain K12) OX=83333 GN=ssnA PE=1 SV=2 ...
Domain architectures illustrate each occurrence of the N-terminal nucleophile aminohydrolases (Ntn hydrolases) superfamily. ... Domain combinations containing the N-terminal nucleophile aminohydrolases (Ntn hydrolases) superfamily in Mycobacterium ... Home > Genomes > Mycobacterium tuberculosis KZN 1435 > N-terminal nucleophile aminohydrolases (Ntn hydrolases) > Domain ... 7 domain combinations include a N-terminal nucleophile aminohydrolases (Ntn hydrolases) domain in Mycobacterium tuberculosis ...
Aminohydrolase - An aminohydrolase is a hydrolase enzyme which acts upon an amino group.Aminohydrolases are classified under EC ... aminohydrolase - ami·no·hy·dro·lase (ə me″no hiґdro lās) systematic name for some enzymes of the hydrolase class that catalyze ...
Aminohydrolases. *Guanine deaminase. *Adenosine deaminase. *AMP deaminase. *Inosine monophosphate synthase. *DCMP deaminase ...
Aminohydrolases. *Guanine deaminase. *Adenosine deaminase. *AMP deaminase. *Inosine monophosphate synthase. *DCMP deaminase ...
adenosine aminohydrolase. Additional Information & Resources. Tests Listed in the Genetic Testing Registry. *Tests of ADA ...
AMP aminohydrolase. adenosine monophosphate deaminase (isoform E). erythrocyte AMP deaminase. erythrocyte type AMP deaminase. ...
Cytidine Aminohydrolase. Deoxycytidine Kinase. Nucleoside Transport Proteins. hENT1 protein, human. Additional relevant MeSH ...
Ratio of glutamine aminotransferase & glutamine aminohydrolase in plasma of patients with Ratio of glutamine aminotransferase ... glutamine aminohydrolase in plasma of patients with malignant & other blood disorders. ...
Ureidoglycine Aminohydrolase From Arabidopsis Thaliana in Complex With Its Substrate, (S)-Ureidoglycine ... The binding sites of Manganese atom in the structure of Crystal Structure of (S)-Ureidoglycine Aminohydrolase From Arabidopsis ... Manganese in the structure of Crystal Structure of (S)-Ureidoglycine Aminohydrolase From Arabidopsis Thaliana in Complex With ...
Adenosine aminohydrolase; find Sigma-Aldrich-A5043 MSDS, related peer-reviewed papers, technical documents, similar products & ...
Hydrolases such as: Mucopeptide N-acetylmuramylhydrolase (3.2.1.17; lysozyme); Trypsin (3.4.4.4); L-Asparagine aminohydrolase ( ...
Hydrolyzed by dihydropyrimidine aminohydrolase and dihydroorotase. Excretion. Urine (42%) Half-Life Elimination. 2.1 to 2.5 ...
Wisdom et al., "Cytidine Aminohydrolase from Sheep Liver," Proc. Biochem. Soc., 471st Meeting , CIBA Laboratories, Ltd., ...
Recombinant Human GDA protein is an Escherichia coli Full length protein 1 to 454 aa range, | 90% purity and validated in SDS-PAGE.
Adenosine aminohydrolase. *Adenosine deaminase. see all. * Function. Catalyzes the hydrolytic deamination of adenosine and 2- ...
Also called aminohydrolase. deaminase. An ENZYME that brings about the breakdown of amino compounds.. deaminase. an enzyme ...
aliphatic nitrile aminohydrolase. Reaction(IUBMB). R-CN + 2 H2O = R-COOH + NH3 [RN:R00540]. ...
Complete information for AMPD3 gene (Protein Coding), Adenosine Monophosphate Deaminase 3, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Aminohydrolases. *Guanine deaminase. *Adenosine deaminase. *AMP deaminase. *Inosine monophosphate synthase. *DCMP deaminase ...
Aminohydrolases Grant support * F30 CA200432/CA/NCI NIH HHS/United States * T32 AI083196/AI/NIAID NIH HHS/United States ...
Aminohydrolases. *Guanine deaminase. *Adenosine deaminase. *AMP deaminase. *Inosine monophosphate synthase. *DCMP deaminase ...
Long-term consequences of perinatal fatty acid amino hydrolase inhibition.. Wu CS, Morgan D, Jew CP, Haskins C, Andrews MJ, ...
... adenosine aminohydrolase, ADA, EC 3.5.4.4.) is widely distributed in human tissues. In some tissues ADA exists exclusively as ... Adenosine deaminase (adenosine aminohydrolase, ADA, EC 3.5.4.4.) is widely distributed in human tissues. In some tissues ADA ...
Adenosine aminohydrolase (ADA_HUMAN). *Mutant adenosine deaminase (Q16073_HUMAN). Graphical View of Domain Structure for ...
Rabbit Polyclonal Anti-AICDA Antibody. Validated: WB, ICC/IF, IHC, IHC-P. Tested Reactivity: Human, Mouse, Primate. 100% Guaranteed.
  • An aminohydrolase is a hydrolase enzyme which acts upon an amino group. (wikipedia.org)
  • Aminopyrimidine aminohydrolase (EC 3.5.99.2, thiaminase, thiaminase II, tenA (gene)) is an enzyme with systematic name 4-amino-5-aminomethyl-2-methylpyrimidine aminohydrolase. (wikipedia.org)
  • We identified and partially characterized a novel enzyme, N 6 -methyl-AMP (N 6 -mAMP) aminohydrolase, which clears the methyl marker from N 6 -mAMP. (uni-hannover.de)
  • L-arginine aminohydrolase] is an enzyme that hydrolyzes Larginine to L-ornithine and urea in the urea cycle. (biovendor.com)
  • One important regulator of this molecule is the ADMA-metabolizing enzyme dimethyl-arginine dimethyl-aminohydrolase (DDAH). (cdc.gov)
  • Downstream of glxK is YlbA, encoding S-uridoglycine aminohydrolase, the second enzyme involved in allantoin degradation ( Moraes and Reithmeier 2012 ). (tcdb.org)
  • Structural and functional insights into (S)-ureidoglycine aminohydrolase, key enzyme of purine catabolism in Arabidopsis thaliana. (semanticscholar.org)
  • Glutaminase ( EC 3.5.1.2, glutaminase I , L-glutaminase , glutamine aminohydrolase ) is an amidohydrolase enzyme that generates glutamate from glutamine . (worldheritage.org)
  • Adenosine deaminase (adenosine aminohydrolase, ADA, EC 3.5.4.4. (springer.com)
  • Cytidine deaminase (EC 3.5.4.5) (cytidine aminohydrolase) catalyses the hydrolysis of cytidine into uridine and ammonia while deoxycytidylate deaminase (EC 3.5.4.12) (dCMP deaminase) hydrolyses dCMP into dUMP. (embl.de)
  • aminohydrolase - ami·no·hy·dro·lase (ə me″no hiґdro lās) systematic name for some enzymes of the hydrolase class that catalyze the hydrolysis of an amino group from a cyclic amidine [EC 3.5.4] or a nitrile [EC 3.5.5]. (academic.ru)
  • Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S-ureidoglycolate and NH3 (PubMed:20038185). (rcsb.org)
  • Ratio of glutamine aminotransferase & glutamine aminohydrolase in plasma of patients with malignant & other blood disorders. (bvsalud.org)