Aspartate Kinase: An enzyme that catalyzes the formation of beta-aspartyl phosphate from aspartic acid and ATP. Threonine serves as an allosteric regulator of this enzyme to control the biosynthetic pathway from aspartic acid to threonine. EC 2.7.2.4.Homoserine Dehydrogenase: An enzyme that catalyzes the reduction of aspartic beta-semialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. EC 1.1.1.3.Threonine: An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.Aspartate Aminotransferases: Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC 2.6.1.1.Amino Acid Transport Systems, Acidic: Amino acid transporter systems capable of transporting acidic amino acids (AMINO ACIDS, ACIDIC).Fatigue: The state of weariness following a period of exertion, mental or physical, characterized by a decreased capacity for work and reduced efficiency to respond to stimuli.Citrullinemia: A group of diseases related to a deficiency of the enzyme ARGININOSUCCINATE SYNTHASE which causes an elevation of serum levels of CITRULLINE. In neonates, clinical manifestations include lethargy, hypotonia, and SEIZURES. Milder forms also occur. Childhood and adult forms may present with recurrent episodes of intermittent weakness, lethargy, ATAXIA, behavioral changes, and DYSARTHRIA. (From Menkes, Textbook of Child Neurology, 5th ed, p49)Aspartic Acid: One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.Antiporters: Membrane transporters that co-transport two or more dissimilar molecules in the opposite direction across a membrane. Usually the transport of one ion or molecule is against its electrochemical gradient and is "powered" by the movement of another ion or molecule with its electrochemical gradient.Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.Mitochondrial Membrane Transport Proteins: Proteins involved in the transport of specific substances across the membranes of the MITOCHONDRIA.Posterior Horn Cells: Neurons in the SPINAL CORD DORSAL HORN whose cell bodies and processes are confined entirely to the CENTRAL NERVOUS SYSTEM. They receive collateral or direct terminations of dorsal root fibers. They send their axons either directly to ANTERIOR HORN CELLS or to the WHITE MATTER ascending and descending longitudinal fibers.Receptors, N-Methyl-D-Aspartate: A class of ionotropic glutamate receptors characterized by affinity for N-methyl-D-aspartate. NMDA receptors have an allosteric binding site for glycine which must be occupied for the channel to open efficiently and a site within the channel itself to which magnesium ions bind in a voltage-dependent manner. The positive voltage dependence of channel conductance and the high permeability of the conducting channel to calcium ions (as well as to monovalent cations) are important in excitotoxicity and neuronal plasticity.Spinal Cord: A cylindrical column of tissue that lies within the vertebral canal. It is composed of WHITE MATTER and GRAY MATTER.Neuralgia: Intense or aching pain that occurs along the course or distribution of a peripheral or cranial nerve.Neurons: The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM.Peripheral Nerve Injuries: Injuries to the PERIPHERAL NERVES.Rats, Sprague-Dawley: A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.Decapitation: Traumatic or experimentally induced separation of the head from the body in an animal or human.Euthanasia, Animal: The killing of animals for reasons of mercy, to control disease transmission or maintain the health of animal populations, or for experimental purposes (ANIMAL EXPERIMENTATION).Protein Kinase C: An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters.Food Coloring Agents: Natural or synthetic dyes used as coloring agents in processed foods.N-Methylaspartate: An amino acid that, as the D-isomer, is the defining agonist for the NMDA receptor subtype of glutamate receptors (RECEPTORS, NMDA).Receptors, G-Protein-Coupled: The largest family of cell surface receptors involved in SIGNAL TRANSDUCTION. They share a common structure and signal through HETEROTRIMERIC G-PROTEINS.Arabidopsis: A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.Arabidopsis Proteins: Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments.Gene Expression Profiling: The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell.Herpestidae: The family of agile, keen-sighted mongooses of Asia and Africa that feed on RODENTS and SNAKES.Osteochondrodysplasias: Abnormal development of cartilage and bone.Gene Expression Regulation, Plant: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.Plant Leaves: Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)Indonesia: A republic stretching from the Indian Ocean east to New Guinea, comprising six main islands: Java, Sumatra, Bali, Kalimantan (the Indonesian portion of the island of Borneo), Sulawesi (formerly known as the Celebes) and Irian Jaya (the western part of New Guinea). Its capital is Djakarta. The ethnic groups living there are largely Chinese, Arab, Eurasian, Indian, and Pakistani; 85% of the peoples are of the Islamic faith.Hydroxylamines: Organic compounds that contain the (-NH2OH) radical.Hydroxylamine: A colorless inorganic compound (HONH2) used in organic synthesis and as a reducing agent, due to its ability to donate nitric oxide.Aurora Kinases: A family of highly conserved serine-threonine kinases that are involved in the regulation of MITOSIS. They are involved in many aspects of cell division, including centrosome duplication, SPINDLE APPARATUS formation, chromosome alignment, attachment to the spindle, checkpoint activation, and CYTOKINESIS.Purines: A series of heterocyclic compounds that are variously substituted in nature and are known also as purine bases. They include ADENINE and GUANINE, constituents of nucleic acids, as well as many alkaloids such as CAFFEINE and THEOPHYLLINE. Uric acid is the metabolic end product of purine metabolism.Erigeron: A plant genus of the family ASTERACEAE that is similar to CONYZA. Members contain SESQUITERPENES.Aurora Kinase A: An aurora kinase that localizes to the CENTROSOME during MITOSIS and is involved in centrosome regulation and formation of the MITOTIC SPINDLE. Aurora A overexpression in many malignant tumor types suggests that it may be directly involved in NEOPLASTIC CELL TRANSFORMATION.Resistin: A 12-kDa cysteine-rich polypeptide hormone secreted by FAT CELLS in the ADIPOSE TISSUE. It is the founding member of the resistin-like molecule (RELM) hormone family. Resistin suppresses the ability of INSULIN to stimulate cellular GLUCOSE uptake.Hormones, Ectopic: Hormones released from neoplasms or from other cells that are not the usual sources of hormones.Databases, Chemical: Databases devoted to knowledge about specific chemicals.Molecular Sequence Data: 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.Materials Testing: The testing of materials and devices, especially those used for PROSTHESES AND IMPLANTS; SUTURES; TISSUE ADHESIVES; etc., for hardness, strength, durability, safety, efficacy, and biocompatibility.Insulin Resistance: Diminished effectiveness of INSULIN in lowering blood sugar levels: requiring the use of 200 units or more of insulin per day to prevent HYPERGLYCEMIA or KETOSIS.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Calcium-Calmodulin-Dependent Protein Kinase Type 2: A multifunctional calcium-calmodulin-dependent protein kinase subtype that occurs as an oligomeric protein comprised of twelve subunits. It differs from other enzyme subtypes in that it lacks a phosphorylatable activation domain that can respond to CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE.Calcium-Calmodulin-Dependent Protein Kinases: A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. This enzyme is also sometimes dependent on CALCIUM. A wide range of proteins can act as acceptor, including VIMENTIN; SYNAPSINS; GLYCOGEN SYNTHASE; MYOSIN LIGHT CHAINS; and the MICROTUBULE-ASSOCIATED PROTEINS. (From Enzyme Nomenclature, 1992, p277)Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Protein Kinases: A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.Receptors, Glutamate: Cell-surface proteins that bind glutamate and trigger changes which influence the behavior of cells. Glutamate receptors include ionotropic receptors (AMPA, kainate, and N-methyl-D-aspartate receptors), which directly control ion channels, and metabotropic receptors which act through second messenger systems. Glutamate receptors are the most common mediators of fast excitatory synaptic transmission in the central nervous system. They have also been implicated in the mechanisms of memory and of many diseases.Receptors, Ionotropic Glutamate: A class of ligand-gated ion channel receptors that have specificity for GLUTAMATE. They are distinct from METABOTROPIC GLUTAMATE RECEPTORS which act through a G-protein-coupled mechanism.Benzylamines: Toluenes in which one hydrogen of the methyl group is substituted by an amino group. Permitted are any substituents on the benzene ring or the amino group.

Aspartate kinase-independent lysine synthesis in an extremely thermophilic bacterium, Thermus thermophilus: lysine is synthesized via alpha-aminoadipic acid not via diaminopimelic acid. (1/103)

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

The site-specific integration of genetic elements may modulate thermostable protease production, a virulence factor in Dichelobacter nodosus, the causative agent of ovine footrot. (2/103)

The gram-negative anaerobe Dichelobacter nodosus is the causative agent of footrot in sheep. The authors have previously characterized two genetic elements, the intA (vap) and intB elements, which integrate into the genome of D. nodosus. In the virulent strain A198 there are two copies of the intA element. One copy is integrated into the 3' end of the tRNA-serGCU gene, close to the aspartokinase (askA) gene, and the second copy is integrated into the 3' end of the tRNA-serGGA gene, next to the polynucleotide phosphorylase (pnpA) gene. In this study, a new genetic element was identified in the benign strain C305, the intC element, integrated into the 3' end of the tRNA-serGCU gene, next to askA. The intC element was found in most D. nodosus strains, both benign and virulent, which were examined, and was integrated into tRNA-serGCU in most strains. Between the askA and tRNA-serGCU genes, a gene (designated glpA), was identified whose predicted protein product has very high amino acid identity with RsmA from the plant pathogen Erwinia carotovora. RsmA acts as a global repressor of pathogenicity in E. carotovora, by repressing the production of extracellular enzymes. In virulent strains of D. nodosus the intA element was found to be integrated next to pnpA, and either the intA or intC element was integrated next to glpA. By contrast, all but one of the benign strains had intB at one or both of these two positions, and the one exception had neither intA, intB nor intC at one position. The loss of the intC element from the virulent strain 1311 resulted in loss of thermostable protease activity, a virulence factor in D. nodosus. A model for virulence is proposed whereby integration of the intA and intC genetic elements modulates virulence by altering the expression of glpA, pnpA, tRNA-serGCU and tRNA-serGGA.  (+info)

Organization of threonine biosynthesis genes from the obligate methylotroph Methylobacillus flagellatus. (3/103)

The genes encoding aspartate kinase (ask), homoserine dehydrogenase (hom), homoserine kinase (thrB) and threonine synthase (thrC) from the obligate methylotroph Methylobacillus flagellatus were cloned. In maxicells hom and thrC directed synthesis of 51 and 48 kDa polypeptides, respectively. The hom, thrB and thrC genes and adjacent DNA areas were sequenced. Of the threonine biosynthesis genes, only hom and thrC were tightly linked in the order hom-thrC. The gene for thymidylate synthase (thyA) followed thrC and the gene for aspartate aminotransferase (aspC) preceded hom. All four genes (aspC-hom-thrC-thyA) were transcribed in the same direction. mRNA analysis indicated that hom-thrC are apparently transcribed in one 7.5 kb transcript in M. flagellatus. Promoter analysis showed the presence of a functional promoter between aspC and hom. No functional promoter was found to be associated with the DNA stretch between hom and thrC. The thrB gene encoded an unusual type of homoserine kinase and was not linked to other threonine biosynthesis genes.  (+info)

Effects of a feedback-resistant aspartokinase III gene on L-isoleucine production in Escherichia coli K-12. (4/103)

An L-isoleucine-overproducing recombinant strain of E. coli, TVD5, was also found to overproduce L-valine. The L-isoleucine productivity of TVD5 was markedly decreased by addition of L-lysine to the medium. Introduction of a gene encoding feedback-resistant aspartokinase III increased L-isoleucine productivity and decreased L-valine by-production. The resulting strain accumulated 12 g/l L-isoleucine from 40 g/l glucose, and suppression of L-isoleucine productivity by L-lysine was relieved.  (+info)

Attractant regulation of the aspartate receptor-kinase complex: limited cooperative interactions between receptors and effects of the receptor modification state. (5/103)

The manner by which the bacterial chemotaxis system responds to a wide range of attractant concentrations remains incompletely understood. In principle, positive cooperativity between chemotaxis receptors could explain the ability of bacteria to respond to extremely low attractant concentrations. By utilizing an in vitro receptor-coupled kinase assay, the attractant-dependent response curve has been measured for the Salmonella typhimurium aspartate chemoreceptor. The attractant chosen, alpha-methyl aspartate, was originally used to quantitate high receptor sensitivity at low attractant concentrations by Segall, Block, and Berg [(1986) Proc. Natl. Acad. Sci. U.S.A. 83, 8987-8991]. The attractant response curve exhibits limited positive cooperativity, yielding a Hill coefficient of 1.7-2.4, and this Hill coefficient is relatively independent of both the receptor modification state and the mole ratio of CheA to receptor. These results disfavor models in which there are strong cooperative interactions between large numbers of receptor dimers in an extensive receptor array. Instead, the results are consistent with cooperative interactions between a small number of coupled receptor dimers. Because the in vitro receptor-coupled kinase assay utilizes higher than native receptor densities arising from overexpression, the observed positive cooperativity may overestimate that present in native receptor populations. Such positive cooperativity between dimers is fully compatible with the negative cooperativity previously observed between the two symmetric ligand binding sites within a single dimer. The attractant affinity of the aspartate receptor is found to depend on the modification state of its covalent adaptation sites. Increasing the the level of modification decreases the apparent attractant affinity at least 10-fold in the in vitro receptor-coupled kinase assay. This observation helps explain the ability of the chemotaxis pathway to respond to a broad range of attractant concentrations in vivo.  (+info)

Evidence for direct interaction between enzyme I(Ntr) and aspartokinase to regulate bacterial oligopeptide transport. (6/103)

Bradyrhizobium japonicum transports oligopeptides and the heme precursor delta-aminolevulinic acid (ALA) by a common mechanism. Two Tn5-induced mutants disrupted in the lysC and ptsP genes were identified based on the inability to use prolyl-glycyl-glycine as a proline source and were defective in [(14)C]ALA uptake activity. lysC and ptsP were shown to be proximal genes in the B. japonicum genome. However, RNase protection and in trans complementation analysis showed that lysC and ptsP are transcribed separately, and that both genes are involved in oligopeptide transport. Aspartokinase, encoded by lysC, catalyzes the phosphorylation of aspartate for synthesis of three amino acids, but the lysC strain is not an amino acid auxotroph. The ptsP gene encodes Enzyme I(Ntr) (EI(Ntr)), a paralogue of Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase (PTS) system. In vitro pull-down experiments indicated that purified recombinant aspartokinase and EI(Ntr) interact directly with each other. Expression of ptsP in trans from a multicopy plasmid complemented the lysC mutant, suggesting that aspartokinase normally affects Enzyme I(Ntr) in a manner that can be compensated for by increasing the copy number of the ptsP gene. ATP was not a phosphoryl donor to purified EI(Ntr), but it was phosphorylated by ATP in the presence of cell extracts. This phosphorylation was inhibited in the presence of aspartokinase. The findings demonstrate a role for a PTS protein in the transport of a non-sugar solute and suggest an unusual regulatory function for aspartokinase in regulating the phosphorylation state of EI(Ntr).  (+info)

Aspartate kinase 2. A candidate gene of a quantitative trait locus influencing free amino acid content in maize endosperm. (7/103)

The maize (Zea mays) Oh545o2 inbred accumulates an exceptionally high level of free amino acids, especially lysine (Lys), threonine (Thr), methionine, and iso-leucine. In a cross between Oh545o2 and Oh51Ao2, we identified several quantitative trait loci linked with this phenotype. One of these is on the long arm of chromosome 2 and is linked with loci encoding aspartate (Asp) kinase 2 and Asp kinase (AK)-homoserine dehydrogenase (HSDH) 2. To investigate whether these enzymes can contribute to the high levels of Asp family amino acids, we measured their specific activity and feedback inhibition properties, as well as activities of several other key enzymes involved in Lys metabolism. We did not find a significant difference in total activity of dihydrodipicolinate synthase, HSDH, and Lys ketoglutarate reductase between these inbreds, and the feedback inhibition properties of HSDH and dihyrodipicolinate synthase by Lys and/or Thr were similar. The most significant difference we found between Oh545o2 and Oh51Ao2 is feedback inhibition of AK by Lys but not Thr. AK activity in Oh545o2 is less sensitive to Lys inhibition than that in Oh51Ao2, with a Lys I50 twice that of Oh51Ao2. AK activity in Oh545o2 endosperm is also higher than in Oh51Ao2 at 15 d after pollination, but not 20 d after pollination. The results indicate that the Lys-sensitive Asp kinase 2, rather than the Thr-sensitive AK-HSDH2, is the best candidate gene for the quantitative trait locus affecting free amino acid content in Oh545o2.  (+info)

An integrated study of threonine-pathway enzyme kinetics in Escherichia coli. (8/103)

We have determined the kinetic parameters of the individual steps of the threonine pathway from aspartate in Escherichia coli under a single set of experimental conditions chosen to be physiologically relevant. Our aim was to summarize the kinetic behaviour of each enzyme in a single tractable equation that takes into account the effect of the products as competitive inhibitors of the substrates in the forward reaction and also, when appropriate (e.g. near-equilibrium reactions), as substrates of the reverse reactions. Co-operative feedback inhibition by threonine and lysine was also included as necessary. We derived the simplest rate equations that describe the salient features of the enzymes in the physiological range of metabolite concentrations in order to incorporate them ultimately into a complete model of the threonine pathway, able to predict quantitatively the behaviour of the pathway under natural or engineered conditions.  (+info)

In molecular biology, the amino acid kinase domain is a protein domain. It is found in protein kinases with various specificities, including the aspartate, glutamate and uridylate kinase families. In prokaryotes and plants the synthesis of the essential amino acids lysine and threonine is predominantly regulated by feed-back inhibition of aspartate kinase (AK) and dihydrodipicolinate synthase (DHPS). In Escherichia coli, thrA, metLM, and lysC encode aspartokinase isozymes that show feedback inhibition by threonine, methionine, and lysine, respectively. The lysine-sensitive isoenzyme of aspartate kinase from spinach leaves has a subunit composition of 4 large and 4 small subunits. In plants although the control of carbon fixation and nitrogen assimilation has been studied in detail, relatively little is known about the regulation of carbon and nitrogen flow into amino acids. The metabolic regulation of expression of an Arabidopsis thaliana aspartate kinase/homoserine dehydrogenase (AK/HSD) gene, ...
Protein phosphorylation is known to occur across all three kingdoms of life; however, the study of posttranslational modification in bacteria was neglected for a considerable amount of time. Early attempts to detect its presence were unsuccessful, generating the dogma that protein phosphorylation was a regulatory mechanism that emerged late in evolution to meet the needs of organisms composed of multiple and differentiated cells. The pioneering work of several groups in the 1970s identified protein kinase activity in both Escherichia coli and Salmonella typhimurium ( 1 - 3 ), which soon led to the discovery of the histidine/aspartate kinases of the two-component systems ( 4 , 5 ). The first aspect of this system involves the stimulation of a histidine kinase by a particular environmental or intracellular signal resulting in autophosphorylation on a key histidine residue. The phospho-histidine can then be used as a substrate by the cognate response regulator for its own autophosphorylation on an
Numerous significant hits using gapped BLAST to aspartokinase III from E. coli (416597), Arabidopsis thaliana (6091740, putative), Methanococcus jannaschii (2492982), among others. HD1375 is 57% similar to residues 1-449 from AK3_ECOLI ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Arsenic atom in PDB 1pqu: Crystal Structure Of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound With Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate
Protein target information for Chain A, Structure Of Aspartate Semialdehyde Dehydrogenase (Asadh) From Streptococcus Pneumoniae Complexed With 2,5-Adp (Streptococcus pneumoniae). Find diseases associated with this biological target and compounds tested against it in bioassay experiments.
Lysine biosynthesis is one of the unique metabolic capabilities of cyst forming Coccidia such as Toxoplasma gondii and Neospora caninum. Toxoplasma and Neospora genome analysis shows that they have the unique metabolic capability to synthesise lysine, an essential amino acid in humans. This capability is absent in other Apicomplexa. It has been suggested that Toxoplasma can convert aspartate into lysine via diaminopimelate pathway [1]. This pathway takes place via four different routes in different organisms (KEGG Lysine biosynthesis pathway). Of these, three variants belong to different groups of prokaryotes and the plant variant of the pathway was identified recently in Arabidopsis thaliana [2]. The first four enzymes (aspartate kinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase) and the last enzyme (diaminopimelate decarboxylase) is the same in all variants of the pathway and these five enzymes are present in T. gondii and N. caninum ...
ID AK_RICPR Reviewed; 446 AA. AC Q9ZCI7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 25-OCT-2017, entry version 95. DE RecName: Full=Aspartokinase; DE EC=2.7.2.4; DE AltName: Full=Aspartate kinase; GN Name=lysC; OrderedLocusNames=RP753; OS Rickettsia prowazekii (strain Madrid E). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=272947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=9823893; DOI=10.1038/24094; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., RA Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., RA Eriksson A.-S., Winkler H.H., Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). RN [2] RP DOMAIN RPE1. RX PubMed=11030655; DOI=10.1126/science.290.5490.347; RA Ogata H., Audic S., Barbe V., Artiguenave F., ...
The lysine, threonine, and methionine biosynthetic pathways share the three initial enzymatic steps, which are referred to as the Common Pathway (CP). In Escherichia coli three different aspartokinases (AKI, AKII, AKIII, the products of thrA, metL and lysC, respectively) can perform the first step of the CP. Moreover, two of them (AKI and AKII) are bifunctional, carrying also homoserine dehydrogenasic activity (hom product). The second step of the CP is catalyzed by a single aspartate semialdehyde dehydrogenase (ASDH, the product of asd). Thus, in the CP of E. coli while a single copy of ASDH performs the same reaction for three different metabolic routes, three different AKs perfom a unique step. Why and how such a situation did emerge and maintain? How is it correlated to the different regulatory mechanisms acting on these genes? The aim of this work was to trace the evolutionary pathway leading to the extant scenario in proteobacteria. The analysis of the structure, organization, phylogeny, and
The aspartate biosynthetic pathway, essential in plants and in most bacteria and fungi, can produce the amino acids threonine, lysine, methionine, and isoleucine. The first commitment step of this pathway is catalyzed by aspartokinase (AK). The archeal thermophilic Methanococcus jannaschii has only a single, monofunctional form of AK. X-ray crystallographic studies indicate that mjAK is a tetramer in the crystalline state, which coincides with the oligomeric structure in solution. The substrate L-aspartate binds to this recombinant enzyme in two different orientations, providing the first structural evidence supporting the relaxed regiospecificity previously observed with several alternative substrates of E. coli AK.5 Binding of the nucleotide substrate triggers significant domain movements that result in a more compact quaternary structure. The allosteric inhibitor, L-threonine, cooperatively binds to two sites in each monomer of this dimer of dimers, one site in the regulatory domain interface ...
Complete information for LYZ gene (Protein Coding), Lysozyme, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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Introduction: Aspartokinase (A1, A2, A3) Homoserine dehydrogenase (B1, B2) Threonine dehydratase (C1, C2) Allosteric regulation of selective isozymes some unregulated Sequential feedback inhibition Same product inhibits its biosynthetic path at multiple sites Inhibits first enzyme in pathway
ID Q82EQ5_STRAW Unreviewed; 430 AA. AC Q82EQ5; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 31-JAN-2018, entry version 110. DE RecName: Full=Aspartokinase {ECO:0000256,RuleBase:RU003448}; DE EC=2.7.2.4 {ECO:0000256,RuleBase:RU003448}; GN Name=lysC {ECO:0000313,EMBL:BAC72271.1}; GN ORFNames=SAVERM_4559 {ECO:0000313,EMBL:BAC72271.1}; OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / OS NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=227882 {ECO:0000313,EMBL:BAC72271.1, ECO:0000313,Proteomes:UP000000428}; RN [1] {ECO:0000313,EMBL:BAC72271.1, ECO:0000313,Proteomes:UP000000428} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / RC NRRL 8165 / MA-4680 {ECO:0000313,Proteomes:UP000000428}; RX PubMed=11572948; DOI=10.1073/pnas.211433198; RA Omura S., Ikeda H., Ishikawa J., ...
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Comprehensive supplier list for L-Threonine, L-arginyl-L-a-glutamyl-L-a-aspartyl-L-seryl-L-histidyl-L-tryptophyl-L-leucyl-L-asparaginyl-L-cysteinyl-L-arginyl-,L-Threonine, L-arginyl-L-a-glutamyl-L-leucyl-L-prolyl-L-arginyl-L-phenylalanyl-L-methionyl-L-asparaginyl-L-tyrosyl-
Le laboratoire homéopathique français Lehning est connue pour ses gouttes de complexes homéopathiques comme Climaxol, Santaherba, L72 ou L52...
Accepted name: UMP kinase. Reaction: ATP + UMP = ADP + UDP. Other name(s): uridylate kinase; UMPK; uridine monophosphate kinase; PyrH; UMP-kinase; SmbA Systematic name: ATP:UMP phosphotransferase Comments: This enzyme is strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme UMP/CMP kinase (EC 2.7.4.14) for the same purpose [2]. This enzyme is the subject of feedback regulation, being inhibited by UTP and activated by GTP [1].. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9036-23-1. References:. 1. Serina, L., Blondin, C., Krin, E., Sismeiro, O., Danchin, A., Sakamoto, H., Gilles, A.M. and B̢rzu O. Escherichia coli UMP-kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleotides and UTP. Biochemistry 34 (1995) 5066-5074. [PMID: 7711027]. 2. Marco-Marin, C., Gil-Ortiz, F. and Rubio, V. The crystal structure of ...
[129 Pages Report] Check for Discount on Global L-Threonine Sales Market Report 2020 report by QYResearch Group. This report studies sales (consumption) of L-Threonine in Global...
Looking for online definition of allosteric enzymes in the Medical Dictionary? allosteric enzymes explanation free. What is allosteric enzymes? Meaning of allosteric enzymes medical term. What does allosteric enzymes mean?
Flash Point (ASTM D93-08) Flash Point by Pensky- Martens Closed Cup Tester Flash point- tendency of the test specimen to form a flammable mixture with air under controlled laboratory conditions ~$2,000
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The alanine aminotransferase, aspartate aminotransferase and creatine kinase levels may be raised. The gamma- ...
At night, aspartate is converted to asparagine for storage. Additionally, the aspartate kinase-homoserine dehydrogenase gene is ... Homoserine dehydrogenase and aspartate kinase are both subject to significant regulation (refer to figure 3). HSD is inhibited ... The AK-HSD gene codes for aspartate kinase, an intermediate domain (coding for the linker region between the two enzymes in the ... Threonine acts as a competitive inhibitor for both HSD and aspartate kinase. In AK-HSD expressing organisms, one of the ...
"Non-arginine-aspartate (non-RD) kinases are associated with innate immune receptors that recognize conserved microbial ... NODs transduce signals in the pathway of NF-κB and MAP kinases via the serine-threonine kinase called RIP2. NODs signal via N- ... Some IRAK and RIP family kinases fall into a small functional class of kinases termed non-RD, many of which do not ... revealed that despite the small number of non-RD kinases in these genomes (9%-29%), 12 of 15 kinases known or predicted to ...
The ACT domain is named after three of the proteins that contain it: aspartate kinase, chorismate mutase and TyrA. The ...
"Evidence for direct protein kinase-C mediated modulation of N-methyl-D-aspartate receptor current". Mol. Pharmacol. 59 (5): 960 ... CAMK2B calcium/calmodulin-dependent protein kinase (CaM kinase) II beta". Walikonis RS, Oguni A, Khorosheva EM, Jeng CJ, ... Calcium/calmodulin-dependent protein kinase type II beta chain is an enzyme that in humans is encoded by the CAMK2B gene. The ... of a phosphorylation site for calcium/calmodulindependent protein kinase II in the NR2B subunit of the N-methyl-D-aspartate ...
... aspartokinase β-aspartate semialdehyde dehydrogenase homoserine dehydrogenase homoserine kinase threonine synthase. Threonine ... Threonine is synthesized from aspartate in bacteria such as E. coli. In the genetic code it is encoded by the codons ACU, ACC, ... In addition, threonine residues undergo phosphorylation through the action of a threonine kinase. In its phosphorylated form, ... "Threonine synthesis from aspartate in Escherichia coli cell-free extracts: pathway dynamics" (PDF). J Biochem. 356: 425-32. PMC ...
"Interaction of the tyrosine kinase Pyk2 with the N-methyl-D-aspartate receptor complex via the Src homology 3 domains of PSD-95 ... DLG3 is a member of the membrane-associated guanylate kinase (MAGUK) superfamily of proteins. DLG3 has been shown to interact ... 1996). "Interaction of the N-methyl-D-aspartate receptor complex with a novel synapse-associated protein, SAP102". J. Biol. ... 1999). "Interaction of NE-dlg/SAP102, a neuronal and endocrine tissue-specific membrane-associated guanylate kinase protein, ...
"Interaction of the tyrosine kinase Pyk2 with the N-methyl-D-aspartate receptor complex via the Src homology 3 domains of PSD-95 ... "Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions". Nature. 376 (6543 ... Protein tyrosine kinase 2 beta is an enzyme that in humans is encoded by the PTK2B gene. This gene encodes a cytoplasmic ... "Entrez Gene: PTK2B PTK2B protein tyrosine kinase 2 beta". Soni D, Regmi SC, Wang DM, DebRoy A, Zhao YY, Vogel SM, Malik AB, ...
"Interaction of the tyrosine kinase Pyk2 with the N-methyl-D-aspartate receptor complex via the Src homology 3 domains of PSD-95 ... Choi J, Ko J, Park E, Lee JR, Yoon J, Lim S, Kim E (April 2002). "Phosphorylation of stargazin by protein kinase A regulates ... PSD-95 is a member of the membrane-associated guanylate kinase (MAGUK) family. With PSD-93 it is recruited into the same NMDA ... The GUK domain that they have is structurally very similar to that of the guanylate kinases, however it is known to be ...
"Interaction of the tyrosine kinase Pyk2 with the N-methyl-D-aspartate receptor complex via the Src homology 3 domains of PSD-95 ... N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate receptors. NMDA channel has been shown to be involved ... "Entrez Gene: GRIN2A glutamate receptor, ionotropic, N-methyl D-aspartate 2A". Hamza TH, Chen H, Hill-Burns EM, Rhodes SL, ... Foldes RL, Adams SL, Fantaske RP, Kamboj RK (1994). "Human N-methyl-D-aspartate receptor modulatory subunit hNR2A: cloning and ...
... generally on an aspartate residue, by a transmembrane kinase. Some proteins that belong to this category are: Rhizobiaceae fixJ ...
"Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate ... Ripellino JA, Neve RL, Howe JR (1998). "Expression and heteromeric interactions of non-N-methyl-D-aspartate glutamate receptor ... Barria A, Derkach V, Soderling T (1998). "Identification of the Ca2+/calmodulin-dependent protein kinase II regulatory ...
"Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate ... "Entrez Gene: CAMK2G calcium/calmodulin-dependent protein kinase (CaM kinase) II gamma". Moyers JS, Bilan PJ, Zhu J, Kahn CR ( ... "Phosphorylation of smooth myosin light chain kinase by smooth muscle Ca2+/calmodulin-dependent multifunctional protein kinase ... Calcium/calmodulin-dependent protein kinase type II gamma chain is an enzyme that in humans is encoded by the CAMK2G gene. The ...
The formation of aspartate kinase (AK), which catalyzes the phosphorylation of aspartate and initiates its conversion into ... The synthesis of aspartate kinase (AK), which catalyzes the phosphorylation of aspartate and initiates its conversion into ... Aspartate kinase becomes downregulated by the presence of threonine or lysine. Lysine[edit]. Lysine is synthesized from ... Oxaloacetate/aspartate: lysine, asparagine, methionine, threonine, and isoleucine[edit]. The oxaloacetate/aspartate family of ...
... the relative levels of creatine kinase, aldolase, aspartate aminotransferase, alanine aminotransferase, and lactate ...
In phosphorelays, the "hybrid" histidine kinase contains an internal aspartate-containing receiver domain to which the ... to an aspartate on a final response regulator. In orthodox two-component signaling, a histidine kinase protein ... In some cases, a phosphorelay system is constructed from four separate proteins rather than a hybrid histidine kinase with an ... In bacteria, where two-component signaling is extremely common, about 25% of known histidine kinases are of the hybrid type. ...
... the phosphotransfer from the kinase to an aspartate of the response regulator, and (with bifunctional enzymes) the ... The kinase core has a unique fold, distinct from that of the Ser/Thr/Tyr kinase superfamily. HKs can be roughly divided into ... Histidine kinases usually have an N-terminal ligand-binding domain and a C-terminal kinase domain, but other domains may also ... Not all orthodox kinases are membrane bound, e.g., the nitrogen regulatory kinase NtrB (GlnL) is a soluble cytoplasmic HK. ...
Porphobilinogen deaminase Sodium Potassium Anti-nuclear antibody Creatinine Creatine kinase White blood cell Aspartate ...
... a phosphate group from ATP is first added to a histidine residue within the kinase, then transferred to an aspartate residue on ... Histidine-specific protein kinases are structurally distinct from other protein kinases and are found in prokaryotes, fungi, ... Receptor tyrosine kinases (RTKs) are transmembrane proteins with an intracellular kinase domain and an extracellular domain ... cAMP-dependent pathway: In humans, cAMP works by activating protein kinase A (PKA, cAMP-dependent protein kinase) (see picture ...
Aspartate 145 also changes position. Together these structural changes allow ATP phosphates to bind correctly. When CAK ... Lolli G, Johnson LN (April 2005). "CAK-Cyclin-dependent Activating Kinase: a key kinase in cell cycle control and a target for ... The active site of Cdk2 lies in a cleft between the two lobes of the kinase. ATP binds deep within the cleft and its phosphate ... CDK-activating kinase (CAK) activates the cyclin-CDK complex by phosphorylating threonine residue 160 in the CDK activation ...
It is found in protein kinases with various specificities, including the aspartate, glutamate and uridylate kinase families. In ... The lysine-sensitive isoenzyme of aspartate kinase from spinach leaves has a subunit composition of 4 large and 4 small ... The conversion of aspartate into either the storage amino acid asparagine or aspartate family amino acids may be subject to a ... Kochhar S, Kochhar VK, Sane PV (April 1998). "Subunit structure of lysine sensitive aspartate kinase from spinach leaves". ...
These water molecules then form hydrogen bonds to a conserved aspartate residue on the enzyme. The metal ion interaction ... This enzyme is also called NMP-kinase, or nucleoside-monophosphate kinase. A number of crystal structures have been solved for ... "Ancient Divergence of long and short isoforms of adenylate kinase molecular evolution of the nucleoside monophosphate kinase ... Following the evolution of long and short varieties of NMP-kinases, smaller changes in the amino acid sequences resulted in the ...
... of a phosphorylation site for calcium/calmodulindependent protein kinase II in the NR2B subunit of the N-methyl-D-aspartate ... Phosphorylation by cyclic AMP-dependent protein kinase, protein kinase C, and calcium/calmodulin protein kinase; identification ... "Entrez Gene: CAMK2A calcium/calmodulin-dependent protein kinase (CaM kinase) II alpha". Walikonis RS, Oguni A, Khorosheva EM, ... "Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau- ...
Two distal aspartate residues bind to the arginine network, causing the enzyme to fold and reduces its flexibility. A magnesium ... Adenylate kinase, subfamily InterPro: IPR006259 UMP-CMP kinase InterPro: IPR006266 Adenylate kinase, isozyme 1 InterPro: ... adenylate kinase performed dual enzymatic functions. ADK complements nucleoside diphosphate kinase deficiency. Adenylate kinase ... Lu Q, Inouye M (June 1996). "Adenylate kinase complements nucleoside diphosphate kinase deficiency in nucleotide metabolism". ...
"Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase ... Phosphoglycerate kinase (EC 2.7.2.3) (PGK 1) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3- ... Phosphoglycerate kinase at the US National Library of Medicine Medical Subject Headings (MeSH) Illustration at arizona.edu This ... Phosphoglycerate kinase (PGK) deficiency is an X-linked recessive trait associated with hemolytic anemia, mental disorders and ...
"Pregnenolone sulfate: a positive allosteric modulator at the N-methyl-D-aspartate receptor" (abstract). Molecular Pharmacology ... Bcr-Abl tyrosine-kinase inhibitors. *Cannabinoid receptor antagonists. *CCR5 receptor antagonists. *Neurokinin 1 receptor ...
It is found in protein kinases with various specificities, including the aspartate, glutamate and uridylate kinase families. In ... The lysine-sensitive isoenzyme of aspartate kinase from spinach leaves has a subunit composition of 4 large and 4 small ... The conversion of aspartate into either the storage amino acid asparagine or aspartate family amino acids may be subject to a ... Kochhar S, Kochhar VK, Sane PV (April 1998). "Subunit structure of lysine sensitive aspartate kinase from spinach leaves". ...
Aspartate/glutamate/uridylate kinase (IPR001048). Short name: Asp/Glu/Uridylate_kinase Domain relationships *Aspartate/ ... Subunit structure of lysine sensitive aspartate kinase from spinach leaves.. Biochem. Mol. Biol. Int. 44 795-806 1998 ... This entry contains proteins with various specificities and includes the aspartate, glutamate and uridylate kinase families. In ... The metabolic regulation of expression of an Arabidopsis thaliana aspartate kinase/homoserine dehydrogenase (AK/HSD) gene, ...
Aspartate kinase (aspartokinase, aspartic kinase) is an enzyme that catalyzes the phosphorylation of the amino acid aspartate. ... 2001). "The central enzymes of the aspartate family of amino acid biosynthesis". Acc Chem Res. 34 (5): 339-49. doi:10.1021/ ... "aspartate family". The gene for aspartokinase is present only in microorganisms and plants; it is not present in animals, which ... must obtain aspartate-family amino acids in their diet. In Escherichia coli, aspartokinase is present as three independently ...
Several protein kinases, including protein kinase C (PKC) (Chen and Huang, 1992), protein kinase A (Raman et al., 1996), Ca2+/ ... protein kinase A, Ca2+/calmodulin-dependent protein kinase II, or the Src tyrosine kinase (Pinna, 1990). The concentration of ... N-methyl-d-aspartate receptor. PCR. polymerase chain reaction. PKC. protein kinase C. PP2. 3-(4-chlorophenyl) 1-(1,1- ... Casein Kinase II Regulates N-Methyl-d-Aspartate Receptor Activity in Spinal Cords and Pain Hypersensitivity Induced by Nerve ...
1997) Cyclic AMP-dependent protein kinase and protein kinase C phosphorylate N-methyl-d-aspartate receptors at different sites. ... 1997) Characterization of protein kinase A and protein kinase C phosphorylation of the N-methyl-d-aspartate receptor NR1 ... protein kinase C. PKM. constitutively active fragment of protein kinase C. Iss. steady-state current. Ip. peak current. BAPTA. ... Regulation of N-Methyl-d-Aspartate Receptor Function by Constitutively Active Protein Kinase C. Zhi-Gang Xiong, Ramin Raouf, ...
Function Mutants in Aspartate Kinase and Homoserine Dehydrogenase Genes Points to Complexity in the Regulation of Aspartate- ... Function Mutants in Aspartate Kinase and Homoserine Dehydrogenase Genes Points to Complexity in the Regulation of Aspartate- ... Function Mutants in Aspartate Kinase and Homoserine Dehydrogenase Genes Points to Complexity in the Regulation of Aspartate- ... Function Mutants in Aspartate Kinase and Homoserine Dehydrogenase Genes Points to Complexity in the Regulation of Aspartate- ...
"Transcriptional and biochemical regulation of a novel Arabidopsis thaliana bifunctional aspartate kinase-homoserine ... Aspartate kinase regulation in maize: evidence for co-purification of threonine-sensitive aspartate kinase and homoserine ... Lysine-insensitive aspartate kinase in two threonine-overproducing mutants of maize. Dotson, S.B.; Frisch, D.A.; Somers, D.A.; ... Expression of an aspartate kinase homoserine dehydroge-nase gene is subject to specific spatial and temporal regulation in ...
Involvement of a Dysfunctional Dopamine-D1/N-Methyl-d-aspartate-NR1 and Ca2+/Calmodulin-Dependent Protein Kinase II Pathway in ... Involvement of a Dysfunctional Dopamine-D1/N-Methyl-d-aspartate-NR1 and Ca2+/Calmodulin-Dependent Protein Kinase II Pathway in ... Involvement of a Dysfunctional Dopamine-D1/N-Methyl-d-aspartate-NR1 and Ca2+/Calmodulin-Dependent Protein Kinase II Pathway in ... Involvement of a Dysfunctional Dopamine-D1/N-Methyl-d-aspartate-NR1 and Ca2+/Calmodulin-Dependent Protein Kinase II Pathway in ...
Aurora Kinases as Druggable Targets in Cancer Therapy » Free Fatty Acid Receptors Menu Not Found. Skip to content *Home ... purine biosynthesis wherein hydroxylamine is provided instead of aspartate (12). mARC-mediated. February 12, 2018. Free Fatty ... purine biosynthesis wherein hydroxylamine is provided instead of aspartate (12). mARC-mediated was acquired from Sigma-Aldrich ...
Aspartate activation of pyruvate kinase in anoxia tolerant molluscs. Publication. Publication. Comparative Biochemistry and ... Storey, K. (1986). Aspartate activation of pyruvate kinase in anoxia tolerant molluscs. Comparative Biochemistry and Physiology ... 1. 1. The effects of the amino acid, aspartate, as an allosteric modifier of pyruvate kinase (PK) were surveyed in tissue ... aspartate activation of PK provides co-ordinated control of the coupled anaerobic fermentations of aspartate → succinate and ...
... are serine/threonine proteins kinases comparable to the phosphatidylinositol 3-kinase-related kinase (PI3K) proteins family [9] ... Finally, inhibition of mitogen-activated proteins kinase kinase (MEK) synergized with docetaxel treatment in BLBC xenografts. ... Category: Cysteinyl Aspartate Protease Hypoglycemic encephalopathy (HE) is normally the effect of a insufficient glucose ... immunohistochemistry; expressions of AKT/mTOR signaling substances, extracellular-signal-regulated kinase 1/2 (ERK1/2), p-ERK1/ ...
Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate ... Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate ... Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate ... 620-638 in GluR1 was phosphorylated in vitro by CaM-kinase II but not by cAMP-dependent protein kinase or protein kinase C. The ...
T1 - Protein kinase C potentiation of N-methyl-D-aspartate receptor activity is not mediated by phosphorylation of N-methyl-D- ... Zheng, X, Zhang, L, Wang, AP, Bennett, MVL & Zukin, RS 1999, Protein kinase C potentiation of N-methyl-D-aspartate receptor ... Protein kinase C potentiation of N-methyl-D-aspartate receptor activity is not mediated by phosphorylation of N-methyl-D- ... Protein kinase C potentiation of N-methyl-D-aspartate receptor activity is not mediated by phosphorylation of N-methyl-D- ...
Levels of expression of protein kinase C gamma (PKCγ) and NMDA receptor subtype NR1 in spinal cord were detected by Western ... N-methyl-D-aspartate (NMDA) pathway in melatonin-mediated. Experiments were performed on adult, male Sprague-Dawley rats. ... investigated the effect of melatonin on morphine-induced hyperalgesia and tolerance and possible involvement of protein kinase ... Melatonin prevents morphine-induced hyperalgesia and tolerance in rats: role of protein kinase C and N-methyl-D-aspartate ...
Regulation of calcium/calmodulin-dependent protein kinase II docking to N-methyl-D-aspartate receptors by calcium/calmodulin ... Regulation of calcium/calmodulin-dependent protein kinase II docking to N-methyl-D-aspartate receptors by calcium/calmodulin ... Regulation of calcium/calmodulin-dependent protein kinase II docking to N-methyl-D-aspartate receptors by calcium/calmodulin ... Regulation of calcium/calmodulin-dependent protein kinase II docking to N-methyl-D-aspartate receptors by calcium/calmodulin ...
Nerve Growth Factor Uses Ras/ERK and Phosphatidylinositol 3-Kinase Cascades to Up-regulate the N-Methyl-D-aspartate Receptor 1 ... Nerve Growth Factor Uses Ras/ERK and Phosphatidylinositol 3-Kinase Cascades to Up-regulate the N-Methyl-D-aspartate Receptor 1 ... Nerve Growth Factor Uses Ras/ERK and Phosphatidylinositol 3-Kinase Cascades to Up-regulate the N-Methyl-D-aspartate Receptor 1 ... title = "Nerve Growth Factor Uses Ras/ERK and Phosphatidylinositol 3-Kinase Cascades to Up-regulate the N-Methyl-D-aspartate ...
Dopamine D1-Dependent Trafficking of Striatal N-Methyl-D-aspartate Glutamate Receptors Requires Fyn Protein Tyrosine Kinase but ... Strategies that prevent NMDA receptor subcellular redistribution through inhibition of Fyn kinase may prove useful in the ... or the protein tyrosine kinase Fyn. In striatal tissue from DARPP-32-depleted mice, basal tyrosine and serine phosphorylation ... reported that activation of the dopamine D1 receptor triggers a rapid redistribution of striatal N-methyl-D-aspartate (NMDA) ...
ALC, absolute lymphocyte count; ALT, alanine aminotransferase; ANC, absolute neutrophil count; AST, aspartate aminotransferase ... CK, creatinine kinase; COVID-19, coronavirus disease; CRP, C-reactive protein; GGO, ground glass opacities; IL-6, interleukin-6 ...
Aspartate/glutamate/uridylate kinase (IPR001048) Pfam signature: PF00696 N-(5phosphoribosyl) anthranilate isomerase (PRAI) ( ... GHMP kinase N-terminal domain (IPR006204) Pfam signature: PF00288 Biotin carboxylase-like, N-terminal domain (IPR005481) Pfam ... 6-phosphofructo-2-kinase (IPR013079) Pfam signature: PF01591 NIF system FeS cluster assembly, NifU, N-terminal (IPR002871) Pfam ... Casein kinase II, regulatory subunit (IPR000704) Pfam signature: PF01214 Cytochrome c oxidase, subunit Vb (IPR002124) Pfam ...
Mammalian AMP-activated protein kinase subfamily. J. Biol. Chem. 1996. 271:611-614. View this article via: PubMed CrossRef ... Serum alanine aminotransferase (ALT) and aspartate aminotransferase (AST) levels were measured enzymatically with a commercial ... AMP kinase activation ameliorates insulin resistance induced by free fatty acids in rat skeletal muscle. Am. J. Physiol. ... Activation of glucose transport by AMP-activated protein kinase via stimulation of nitric oxide synthase. Diabetes. 2000. 49: ...
Cellular Amino Acid Concentrations and Regulation of Aspartate Kinase in the Thermophilic Phototrophic Prokaryote Chloroflexus ... Aspartic Acid-Aspartate and Glutamic Acid-Glutamate Hydrogen Bonds Having Great Proton Polarizability - IR Investigations by ...
The first key reaction is catalyzed by aspartate kinase (AK, EC 2.7.2.4), which phosphorylates aspartate to produce β-aspartyl ... Aspartate kinase (AK; EC 2.7.2.4) and homoserine dehydrogenase (HSDH; EC 1.1.1.3) were extracted at 4 °C, filtered, centrifuged ... Figure 3 Specific activities of aspartate kinase - AK (A; nmoL min−1 mg−1 protein), homoserine dehydrogenase - HSDH (B; nmoL ... Table 4 Aspartate kinase (AK), homoserine dehydrogenase (HSDH), and dihydrodipicolinate synthase (DHDPS) inhibition patterns ...
aspartate kinase activity, homoserine dehydrogenase activity, homoserine biosynthetic process, lysine biosynthetic process via ... IPR001048 Asp/Glu/Uridylate_kinase. IPR005106 Asp/hSer_DH_NAD-bd. IPR001341 Asp_kinase. IPR018042 Aspartate_kinase_CS. ... IPR001048 Asp/Glu/Uridylate_kinase. IPR005106 Asp/hSer_DH_NAD-bd. IPR001341 Asp_kinase. IPR018042 Aspartate_kinase_CS. ... aspartate kinase activity Source: EcoCyc ,p>Inferred from Direct Assay,/p> ,p>Used to indicate a direct assay for the function ...
DR InterPro; IPR018042; Aspartate_kinase_CS. DR InterPro; IPR027795; GATS-like_ACT_dom. DR Pfam; PF00696; AA_kinase; 1. DR Pfam ... DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0009089; P:lysine biosynthetic process via ... DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR005260; Asp_kin_monofn. DR InterPro; IPR001341; Asp_kinase. ... 21:526-531(2003). CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L- CC aspartate. {ECO:0000256,RuleBase: ...
  • The lysine-sensitive isoenzyme of aspartate kinase from spinach leaves has a subunit composition of 4 large and 4 small subunits. (wikipedia.org)
  • In prokaryotes and plants the synthesis of the essential amino acids lysine and threonine is predominantly regulated by feed-back inhibition of aspartate kinase (AK) and dihydrodipicolinate synthase (DHPS). (wikipedia.org)
  • We have previously reported that activation of the dopamine D1 receptor triggers a rapid redistribution of striatal N-methyl-D-aspartate (NMDA) receptors between intracellular and postsynaptic subcellular compartments. (uab.edu)
  • These findings suggest a novel mechanism for the trafficking of striatal NMDA receptors by signaling pathways that are independent of DARPP-32 but require Fyn protein tyrosine kinase. (uab.edu)
  • This aberrant trafficking of AMPA receptors correlated with the dysregulation of the phosphatidylinoside-3-kinase (PI3K)/AKT signaling pathway and the downregulation of the lipid phosphatase and tensin homolog (PTEN). (frontiersin.org)
  • Receptor-like kinases (RLKs) are surface localized, transmembrane receptors comprising a large family of well-studied kinases. (frontiersin.org)
  • Equivalent mammalian receptors from the Pelle/IRAK family differ in usually employing a cytosolic tyrosine kinase domain ( Gish and Clark, 2011 ). (frontiersin.org)
  • Recent evidence suggests that it plays a key role in certain types of synaptic plasticity, in particular a form of long-term depression (LTD) that is induced by the synaptic activation of N-methyl-D-aspartate receptors (NMDARs). (frontiersin.org)
  • Information in the brain is stored primarily as changes in the weights of synaptic connections, via the processes of LTP and LTD. LTP, which is a long-lasting increase in the efficiency of synaptic transmission, is usually triggered by the synaptic activation of N-methyl-D-aspartate receptors (NMDARs), though NMDAR-independent forms of LTP also exist in the CNS ( Bliss and Collingridge, 1993 ). (frontiersin.org)
  • FGFR1-4 are cell surface membrane receptors that possess tyrosine kinase activity. (wikipedia.org)
  • A full-length representative of these four receptors consists of an extracellular region composed of three immunoglobulin-like domains which bind their proper ligands, the fibroblast growth factors (FGFs), a single hydrophobic stretch which passes through the cell's surface membrane, and a cytoplasmic tyrosine kinase domain. (wikipedia.org)
  • HKs can act as cellular receptors for signaling molecules in a way analogous to tyrosine kinase receptors (RTK). (wikipedia.org)
  • IRAKs were first identified in 1994 by Michael Martin and colleagues when they successfully co-precipitated a protein kinase with type I interleukin-1 receptors (IL-1RI) from human T cells. (wikipedia.org)
  • Even cells without over-expressed IL-1 receptors showed kinase activity when exposed to IL-1, and were able to co-precipitate a protein kinase with endogenous IL-1 receptors. (wikipedia.org)
  • DLGAP2 has been shown to interact with DLG4, the canonical synapse marker protein, which in turn binds to N-methyld-aspartate (NMDA) receptors and Shaker-type K+ channels. (wikipedia.org)
  • The lipophilic diacylglycerol remains in the membrane, acting as a cofactor for the activation of protein kinase C. These receptors are also associated with Na+ and K+ channels. (wikipedia.org)
  • For example, group I mGluRs are known to increase the activity of N-methyl-D-aspartate receptors (NMDARs), a type of ion channel-linked receptor that is central in a neurotoxic process called excitotoxicity. (wikipedia.org)
  • Another pathway of transmission of proliferative signals into the genome, with participation of growth factors and tyrosine kinases, is the monocascade STAT (signal transducer and activator of transcription) protein pathway activated by receptors of growth factors and cytokines. (wikipedia.org)
  • However, Lys metabolism in immature grains was modified, showing increases in the specific activities of aspartate kinase (AK) and dihydrodipicolinate synthase (DHDPS) after Cd exposure. (scielo.br)
  • The elicitation of different TLRs/IL-1Rs results in similar signaling cascades due to their homologous TIR motif leading to the activation of mitogen-activated protein kinases (MAPKs) and the IκB kinase (IKK) complex, which initiates a nuclear factor-κB (NF-κB) and AP-1-dependent transcriptional response of pro-inflammatory genes. (wikipedia.org)
  • In the late 1980s and early 1990s, the first protein tyrosine phosphatase (PTP1B) was purified and the discovery, as well as, cloning of JAK kinases was accomplished which led to many in the scientific community to name the 1990s as the decade of protein kinase cascades. (wikipedia.org)
  • The IKK-α and IKK-β kinase subunits are homologous in structure, composed of a kinase domain, as well as leucine zipper and helix-loop-helix dimerization domains, and a carboxy-terminal NEMO-binding domain (NBD). (wikipedia.org)
  • Following immune cell stimulation, a signal transduction cascade leads to the activation of the IKK complex, an event characterized by the binding of NEMO to the homologous kinase subunits IKK-α and IKK-β. (wikipedia.org)
  • It should also not be confused with AMP-activated protein kinase - which, although a member of the protein kinase superfamily and a Ser/Thr kinase, may have opposite effects - nor be confused with cyclin-dependent kinases (Cdks), nor be confused with the acid dissociation constant pKa. (wikipedia.org)
  • Most tyrosine kinases have an associated protein tyrosine phosphatase. (bionity.com)
  • In fact, there are now extensive lines of evidence that illustrate the importance of this lipid phosphatase activity of PTEN, in particular the ability to antagonize PI3K (phosphoinositide 3-kinase) function by dephosphorylating the 3 position in the inositol sugar ring, for its tumour suppressor function and its ability to control cell proliferation, survival and motility [ 1 ]. (biochemj.org)
  • We also detected FRET between CaNA and PKA-RII bound simultaneously to AKAP79 within 50 Å of each other, thus providing the first direct evidence of a ternary kinase-scaffold-phosphatase complex in living cells. (rupress.org)
  • Many HKs are bifunctional and possess phosphatase activity against their cognate response regulators, so that their signaling output reflects a balance between their kinase and phosphatase activities. (wikipedia.org)
  • The protein Tyr phosphatase (PTP) super-family forms the second group, and the aspartate-based protein phosphatases the third. (wikipedia.org)
  • Examples of membrane-spanning protein phosphatases containing both active (phosphatase) and inactive (pseudophosphatase) domains linked in tandem are known, conceptually similar to the kinase and pseudokinase domain polypeptide structure of the JAK pseudokinases. (wikipedia.org)
  • This type of phosphatase includes metal-dependent protein phosphatases (PPMs) and aspartate-based phosphatases. (wikipedia.org)
  • The LysM receptor-like kinase LysM RLK1 is required to activate defense and abiotic-stress responses induced by overexpression of fungal chitinases in Arabidopsis plants. (nih.gov)
  • Transcriptional control of aspartate kinase expression during darkness and sugar depletion in Arabidopsis: involvement of bZIP transcription factors. (nih.gov)