CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase: An enzyme that catalyzes the formation of PHOSPHATIDYLINOSITOL and CMP from CDP-DIACYLGLYCEROL and MYOINOSITOL.Transferases (Other Substituted Phosphate Groups): A class of enzymes that transfers substituted phosphate groups. EC 2.7.8.Phosphotransferases: A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.Cytidine Diphosphate Diglycerides: The ester of diacylglycerol with the terminal phosphate of cytidine diphosphate. It serves as an intermediate in the biosynthesis of phosphatidylethanolamine and phosphatidylserine in bacteria.CDPdiacylglycerol-Serine O-Phosphatidyltransferase: An enzyme that catalyzes the formation of phosphatidylserine and CMP from CDPdiglyceride plus serine. EC 2.7.8.8.Serine: A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.Short Rib-Polydactyly Syndrome: A syndrome inherited as an autosomal recessive trait and incompatible with life. The main features are narrow thorax, short ribs, scapular and pelvic dysplasia, and polydactyly.Planococcus Bacteria: A genus of coccoid bacteria in the family PLANOCOCCACEAE. They are widely distributed in various habitats including sea water, freshwater ponds, cyanobacterial mats, and in marine animals.Periodicals as Topic: A publication issued at stated, more or less regular, intervals.Journal Impact Factor: A quantitative measure of the frequency on average with which articles in a journal have been cited in a given period of time.Publishing: "The business or profession of the commercial production and issuance of literature" (Webster's 3d). It includes the publisher, publication processes, editing and editors. Production may be by conventional printing methods or by electronic publishing.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Ecology: The branch of science concerned with the interrelationship of organisms and their ENVIRONMENT, especially as manifested by natural cycles and rhythms, community development and structure, interactions between different kinds of organisms, geographic distributions, and population alterations. (Webster's, 3d ed)Bibliometrics: The use of statistical methods in the analysis of a body of literature to reveal the historical development of subject fields and patterns of authorship, publication, and use. Formerly called statistical bibliography. (from The ALA Glossary of Library and Information Science, 1983)Software: Sequential operating programs and data which instruct the functioning of a digital computer.Internet: A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.User-Computer Interface: The portion of an interactive computer program that issues messages to and receives commands from a user.Computer Graphics: The process of pictorial communication, between human and computers, in which the computer input and output have the form of charts, drawings, or other appropriate pictorial representation.Computational Biology: A field of biology concerned with the development of techniques for the collection and manipulation of biological data, and the use of such data to make biological discoveries or predictions. This field encompasses all computational methods and theories for solving biological problems including manipulation of models and datasets.Algorithms: A procedure consisting of a sequence of algebraic formulas and/or logical steps to calculate or determine a given task.Programming Languages: Specific languages used to prepare computer programs.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.Oligonucleotide Array Sequence Analysis: Hybridization of a nucleic acid sample to a very large set of OLIGONUCLEOTIDE PROBES, which have been attached individually in columns and rows to a solid support, to determine a BASE SEQUENCE, or to detect variations in a gene sequence, GENE EXPRESSION, or for GENE MAPPING.Oryza sativa: Annual cereal grass of the family POACEAE and its edible starchy grain, rice, which is the staple food of roughly one-half of the world's population.Seeds: The encapsulated embryos of flowering plants. They are used as is or for animal feed because of the high content of concentrated nutrients like starches, proteins, and fats. Rapeseed, cottonseed, and sunflower seed are also produced for the oils (fats) they yield.Cereals: Seeds from grasses (POACEAE) which are important in the diet.Principal Component Analysis: Mathematical procedure that transforms a number of possibly correlated variables into a smaller number of uncorrelated variables called principal components.Vicia sativa: A plant species of the genus VICIA, family FABACEAE. The seed is used for food and contains THIOCYANATES such as prunasin, cyanoalanine, cyanogen, and vicine.District of Columbia: A federal area located between Maryland and Virginia on the Potomac river; it is coextensive with Washington, D.C., which is the capital of the United States.Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.Information Storage and Retrieval: Organized activities related to the storage, location, search, and retrieval of information.SwitzerlandPhosphatidylinositols: Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to the hexahydroxy alcohol, myo-inositol. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid, myo-inositol, and 2 moles of fatty acids.Encyclopedias as Topic: 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)Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Receptor, Epidermal Growth Factor: A cell surface receptor involved in regulation of cell growth and differentiation. It is specific for EPIDERMAL GROWTH FACTOR and EGF-related peptides including TRANSFORMING GROWTH FACTOR ALPHA; AMPHIREGULIN; and HEPARIN-BINDING EGF-LIKE GROWTH FACTOR. The binding of ligand to the receptor causes activation of its intrinsic tyrosine kinase activity and rapid internalization of the receptor-ligand complex into the cell.Phosphatidylinositol 3-Kinases: Phosphotransferases that catalyzes the conversion of 1-phosphatidylinositol to 1-phosphatidylinositol 3-phosphate. Many members of this enzyme class are involved in RECEPTOR MEDIATED SIGNAL TRANSDUCTION and regulation of vesicular transport with the cell. Phosphatidylinositol 3-Kinases have been classified both according to their substrate specificity and their mode of action within the cell.DNA Mutational Analysis: Biochemical identification of mutational changes in a nucleotide sequence.Receptor, erbB-2: A cell surface protein-tyrosine kinase receptor that is overexpressed in a variety of ADENOCARCINOMAS. It has extensive homology to and heterodimerizes with the EGF RECEPTOR, the ERBB-3 RECEPTOR, and the ERBB-4 RECEPTOR. Activation of the erbB-2 receptor occurs through heterodimer formation with a ligand-bound erbB receptor family member.Exoribonucleases: A family of enzymes that catalyze the exonucleolytic cleavage of RNA. It includes EC 3.1.13.-, EC 3.1.14.-, EC 3.1.15.-, and EC 3.1.16.-. EC 3.1.-Polyribonucleotide Nucleotidyltransferase: An enzyme of the transferase class that catalyzes the reaction RNA(n+1) and orthophosphate to yield RNA(n) and a nucleoside diphosphate, or the reverse reaction. ADP, IDP, GDP, UDP, and CDP can act as donors in the latter case. (From Dorland, 27th ed) EC 2.7.7.8.PolynucleotidesPhosphorylases: A class of glucosyltransferases that catalyzes the degradation of storage polysaccharides, such as glucose polymers, by phosphorolysis in animals (GLYCOGEN PHOSPHORYLASE) and in plants (STARCH PHOSPHORYLASE).Polyadenylation: The addition of a tail of polyadenylic acid (POLY A) to the 3' end of mRNA (RNA, MESSENGER). Polyadenylation involves recognizing the processing site signal, (AAUAAA), and cleaving of the mRNA to create a 3' OH terminal end to which poly A polymerase (POLYNUCLEOTIDE ADENYLYLTRANSFERASE) adds 60-200 adenylate residues. The 3' end processing of some messenger RNAs, such as histone mRNA, is carried out by a different process that does not include the addition of poly A as described here.Polynucleotide 5'-Hydroxyl-Kinase: An enzyme that catalyzes the transfer of a phosphate group to the 5'-terminal hydroxyl groups of DNA and RNA. EC 2.7.1.78.Uridine Kinase: An enzyme that catalyzes the phosphorylation of uridine and cytidine to uridine 5'-phosphate and cytidine 5'-phosphate, respectively. ATP, dUTP, dGTP, and dATP are effective phosphate donors. EC 2.7.1.48.Uridine Phosphorylase: An enzyme that catalyzes the transfer of ribose from uridine to orthophosphate, forming uracil and ribose 1-phosphate.Guanine Deaminase: An enzyme that catalyzes the deamination of guanine to form xanthine. EC 3.5.4.3.Cytidine: A pyrimidine nucleoside that is composed of the base CYTOSINE linked to the five-carbon sugar D-RIBOSE.Azauridine: A triazine nucleoside used as an antineoplastic antimetabolite. It interferes with pyrimidine biosynthesis thereby preventing formation of cellular nucleic acids. As the triacetate, it is also effective as an antipsoriatic.RNA Polymerase II: A DNA-dependent RNA polymerase present in bacterial, plant, and animal cells. It functions in the nucleoplasmic structure and transcribes DNA into RNA. It has different requirements for cations and salt than RNA polymerase I and is strongly inhibited by alpha-amanitin. EC 2.7.7.6.Holoenzymes: Catalytically active enzymes that are formed by the combination of an apoenzyme (APOENZYMES) and its appropriate cofactors and prosthetic groups.Mediator Complex: A large protein complex which acts as a signaling adaptor protein that allows communication between the various regulatory and functional components of GENETIC TRANSCRIPTION including DNA POLYMERASE II; GENERAL TRANSCRIPTION FACTORS; and TRANSCRIPTION FACTORS that are bound to upstream ENHANCER ELEMENTS. The mediator complex was originally studied in YEAST where at least 21 subunits were identified. Many of the yeast subunits are homologs to proteins in higher organisms that are found associated with specific nuclear receptors such as THYROID HORMONE RECEPTORS and VITAMIN D RECEPTORS.Cyclin-Dependent Kinase 8: A CYCLIN C dependent kinase that is an important component of the mediator complex. The enzyme is activated by its interaction with CYCLIN C and plays a role in transcriptional regulation by phosphorylating RNA POLYMERASE II.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.

Cloning and expression of a wheat (Triticum aestivum L.) phosphatidylserine synthase cDNA. Overexpression in plants alters the composition of phospholipids. (1/102)

We describe the cloning of a wheat cDNA (TaPSS1) that encodes a phosphatidylserine synthase (PSS) and provides the first strong evidence for the existence of this enzyme in a higher eukaryotic cell. The cDNA was isolated on its ability to confer increased resistance to aluminum toxicity when expressed in yeast. The sequence of the predicted protein encoded by TaPSS1 shows homology to PSS from both yeast and bacteria but is distinct from the animal PSS enzymes that catalyze base-exchange reactions. In wheat, Southern blot analysis identified the presence of a small family of genes that cross-hybridized to TaPSS1, and Northern blots showed that aluminum induced TaPSS1 expression in root apices. Expression of TaPSS1 complemented the yeast cho1 mutant that lacks PSS activity and altered the phospholipid composition of wild type yeast, with the most marked effect being increased abundance of phosphatidylserine (PS). Arabidopsis thaliana leaves overexpressing TaPSS1 showed a marked enhancement in PSS activity, which was associated with increased biosynthesis of PS at the expense of both phosphatidylinositol and phosphatidylglycerol. Unlike mammalian cells where PS accumulation is tightly regulated even when the capacity for PS biosynthesis is increased, plant cells accumulated large amounts of PS when TaPSS1 was overexpressed. High levels of TaPSS1 expression in Arabidopsis and tobacco (Nicotiana tabacum) led to the appearance of necrotic lesions on leaves, which may have resulted from the excessive accumulation of PS. The cloning of TaPSS1 now provides evidence that the yeast pathway for PS synthesis exists in some plant tissues and provides a tool for understanding the pathways of phospholipid biosynthesis and their regulation in plants.  (+info)

Reconstituted phosphatidylserine synthase from Escherichia coli is activated by anionic phospholipids and micelle-forming amphiphiles. (2/102)

The activity of phosphatidylserine (PS) synthase (CDP-1, 2-diacyl-sn-glycerol: l-serine O-phosphatidyltransferase, EC 2.7.8. 8) from Escherichia coli was studied after reconstitution with lipid vesicles of various compositions. PS synthase exhibited practically no activity in the absence of a detergent and with the substrate CDP-diacylglycerol (CDP-DAG) present only in the lipid vesicles. Inclusion of octylglucoside (OG) in the assay mixture increased the activity 20- to 1000-fold, the degree of activation depending on the lipid composition of the vesicles. Inclusion of additional CDP-DAG in the assay mixture increased the activity 5- to 25-fold. When the fraction of phosphatidylglycerol (PG) was increased from 15 to 100 mol% in the vesicles the activity increased 10-fold using the assay mixture containing OG. The highest activities were exhibited with the anionic lipids synthesized by E. coli, namely PG, diphosphatidylglycerol (DPG), and phosphatidic acid, while phosphatidylinositol gave a lower activity. Cryotransmission electron microscopy showed that transformation of the vesicles to micelles brings about an activation of the enzyme that is proportional to the degree of micellization. Thus, the activity of PS synthase is modulated by the lipid aggregate structure and by the fraction and type of anionic phospholipid in the aggregates. The increase in the activity caused by PG and DPG is physiologically relevant; it may be part of a regulatory mechanism that keeps the balance between phosphatidylethanolamine, and the sum of PG and DPG, nearly constant in wild-type E. coli cells.  (+info)

Isolation of a Chinese hamster ovary cell mutant defective in intramitochondrial transport of phosphatidylserine. (3/102)

A CHO-K1 cell mutant with a specific decrease in cellular phosphatidylethanolamine (PE) level was isolated as a variant resistant to Ro09-0198, a PE-directed antibiotic peptide. The mutant was defective in the phosphatidylserine (PS) decarboxylation pathway for PE formation, in which PS produced in the endoplasmic reticulum is transported to mitochondria and then decarboxylated by an inner mitochondrial membrane enzyme, PS decarboxylase. Neither PS formation nor PS decarboxylase activity was reduced in the mutant, implying that the mutant is defective in some step of PS transport. The transport processes of phospholipids between the outer and inner mitochondrial membrane were analyzed by use of isolated mitochondria and two fluorescence-labeled phospholipid analogs, 1-palmitoyl-2-[N-[6(7-nitrobenz-2-oxa-1, 3-diazol-4-yl)amino]caproyl]-PS (C6-NBD-PS) and C6-NBD-phosphatidylcholine (C6-NBD-PC). On incubation with the CHO-K1 mitochondria, C6-NBD-PS was readily decarboxylated to C6-NBD-PE, suggesting that the PS analog was partitioned into the outer leaflet of mitochondria and then translocated to the inner mitochondrial membrane. The rate of decarboxylation of C6-NBD-PS in the mutant mitochondria was reduced to approximately 40% of that in the CHO-K1 mitochondria. The quantity of phospholipid analogs translocated from the outer leaflet of mitochondria into inner mitochondrial membranes was further examined by selective extraction of the analogs from the outer leaflet of mitochondria. In the mutant mitochondria, the translocation of C6-NBD-PS was significantly reduced, whereas the translocation of C6-NBD-PC was not affected. These results indicate that the mutant is defective in PS transport between the outer and inner mitochondrial membrane and provide genetic evidence for the existence of a specific mechanism for intramitochondrial transport of PS.  (+info)

One of the origins of plasma membrane phosphatidylserine in plant cells is a local synthesis by a serine exchange activity. (4/102)

In plant cells, as in animal cells, the endoplasmic reticulum (ER) is considered to be the major site of phospholipid synthesis, and it has been shown that phosphatidylserine (PS) reaches the plasma membrane via the vesicular ER-Golgi-plasma membrane pathway in leek cells. However, it has never been determined whether the plasma membrane of leek cells is able to synthesize PS. We have analyzed the distribution of PS synthesizing enzymes along the vesicular pathway. In ER, Golgi and plasma membrane fractions isolated from leek cells, we have measured the activity of the two biosynthetic pathways leading to the synthesis of PS, i.e. serine exchange and CTP cytidylyltransferase plus PS synthase. We have found a high serine exchange activity in the plasma membrane fraction, and then determined that this membrane is able to synthesize both long chain fatty acid- and very long chain fatty acid-containing PS. Therefore, the PS in the plasma membrane of leek cells has two different origins: the intracellular vesicular pathway from the ER and a local synthesis in the plasma membrane.  (+info)

Interaction of phosphatidylserine synthase from E. coli with lipid bilayers: coupled plasmon-waveguide resonance spectroscopy studies. (5/102)

The interaction of phosphatidylserine (PS) synthase from Escherichia coli with lipid membranes was studied with a recently developed variant of the surface plasmon resonance technique, referred to as coupled plasmon-waveguide resonance spectroscopy. The features of the new technique are increased sensitivity and spectral resolution, and a unique ability to directly measure the structural anisotropy of lipid and proteolipid films. Solid-supported lipid bilayers with the following compositions were used: 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC); POPC-1-palmitoyl-2-oleoyl-sn-glycero-3-phosphate (POPA) (80:20, mol/mol); POPC-POPA (60:40, mol/mol); and POPC-1-palmitoyl-2-oleoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (POPG) (75:25, mol/mol). Addition of either POPA or POPG to a POPC bilayer causes a considerable increase of both the bilayer thickness and its optical anisotropy. PS synthase exhibits a biphasic interaction with the bilayers. The first phase, occurring at low protein concentrations, involves both electrostatic and hydrophobic interactions, although it is dominated by the latter, and the enzyme causes a local decrease of the ordering of the lipid molecules. The second phase, occurring at high protein concentrations, is predominantly controlled by electrostatic interactions, and results in a cooperative binding of the enzyme to the membrane surface. Addition of the anionic lipids to a POPC bilayer causes a 5- to 15-fold decrease in the protein concentration at which the first binding phase occurs. The results reported herein lend experimental support to a previously suggested mechanism for the regulation of the polar head group composition in E. coli membranes.  (+info)

Regulation of the DPP1-encoded diacylglycerol pyrophosphate (DGPP) phosphatase by inositol and growth phase. Inhibition of DGPP phosphatase activity by CDP-diacylglyceron and activation of phosphatidylserine synthase activity by DGPP. (6/102)

The regulation of the Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate (DGPP) phosphatase by inositol supplementation and growth phase was examined. Addition of inositol to the growth medium resulted in a dose-dependent increase in the level of DGPP phosphatase activity in both exponential and stationary phase cells. Activity was greater in stationary phase cells when compared with exponential phase cells, and the inositol- and growth phase-dependent regulations of DGPP phosphatase were additive. Analyses of DGPP phosphatase mRNA and protein levels, and expression of beta-galactosidase activity driven by a P(DPP1)-lacZ reporter gene, indicated that a transcriptional mechanism was responsible for this regulation. Regulation of DGPP phosphatase by inositol and growth phase occurred in a manner that was opposite that of many phospholipid biosynthetic enzymes. Regulation of DGPP phosphatase expression by inositol supplementation, but not growth phase, was altered in opi1Delta, ino2Delta, and ino4Delta phospholipid synthesis regulatory mutants. CDP-diacylglycerol, a phospholipid pathway intermediate used for the synthesis of phosphatidylserine and phosphatidylinositol, inhibited DGPP phosphatase activity by a mixed mechanism that caused an increase in K(m) and a decrease in V(max). DGPP stimulated the activity of pure phosphatidylserine synthase by a mechanism that increased the affinity of the enzyme for its substrate CDP-diacylglycerol. Phospholipid composition analysis of a dpp1Delta mutant showed that DGPP phosphatase played a role in the regulation of phospholipid metabolism by inositol, as well as regulating the cellular levels of phosphatidylinositol.  (+info)

Cloning and characterization of the phosphatidylserine synthase gene of Agrobacterium sp. strain ATCC 31749 and effect of its inactivation on production of high-molecular-mass (1-->3)-beta-D-glucan (curdlan). (7/102)

Genes involved in the production of the extracellular (1-->3)-beta-glucan, curdlan, by Agrobacterium sp. strain ATCC 31749 were described previously (Stasinopoulos et al., Glycobiology 9:31-41, 1999). To identify additional curdlan-related genes whose protein products occur in the cell envelope, the transposon TnphoA was used as a specific genetic probe. One mutant was unable to produce high-molecular-mass curdlan when a previously uncharacterized gene, pss(AG), encoding a 30-kDa, membrane-associated phosphatidylserine synthase was disrupted. The membranes of the mutant lacked phosphatidylethanolamine (PE), whereas the phosphatidylcholine (PC) content was unchanged and that of both phosphatidylglycerol and cardiolipin was increased. In the mutant, the continued appearance of PC revealed that its production by this Agrobacterium strain is not solely dependent on PE in a pathway controlled by the Pss(AG) protein at its first step. Moreover, PC can be produced in a medium lacking choline. When the pss(AG)::TnphoA mutation was complemented by the intact pss(AG) gene, both the curdlan deficiency and the phospholipid profile were restored to wild-type, demonstrating a functional relationship between these two characteristics. The effect of the changed phospholipid profile could occur through an alteration in the overall charge distribution on the membrane or a specific requirement for PE for the folding into or maintenance of an active conformation of any or all of the structural proteins involved in curdlan production or transport.  (+info)

CDP-2,3-Di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase (archaetidylserine synthase) in the methanogenic archaeon Methanothermobacter thermautotrophicus. (8/102)

CDP-2,3-di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase (archaetidylserine synthase) activity in cell extracts of Methanothermobacter thermautotrophicus cells was characterized. The enzyme catalyzed the formation of unsaturated archaetidylserine from CDP-unsaturated archaeol and L-serine. The identity of the reaction products was confirmed by thin-layer chromatography, fast atom bombardment-mass spectrum analysis, and chemical degradation. The enzyme showed maximal activity in the presence of 10 mM Mn2+ and 1% Triton X-100. Among various synthetic substrate analogs, both enantiomers of CDP-unsaturated archaeols with ether-linked geranylgeranyl chains and CDP-saturated archaeol with ether-linked phytanyl chains were similarly active toward the archaetidylserine synthase. The activity on the ester analog of the substrate was two to three times higher than that on the corresponding ether-type substrate. The activity of D-serine with the enzyme was 30% of that observed for L-serine. A trace amount of an acid-labile, unsaturated archaetidylserine intermediate was detected in the cells by a pulse-labeling experiment. A gene (MT1027) in M. thermautotrophicus genome annotated as the gene encoding phosphatidylserine synthase was found to be homologous to Bacillus subtilis pssA but not to Escherichia coli pssA. The substrate specificity of phosphatidylserine synthase from B. subtilis was quite similar to that observed for the M. thermautotrophicus archaetidylserine synthase, while the E. coli enzyme had a strong preference for CDP-1,2-diacyl-sn-glycerol. It was concluded that M. thermautotrophicus archaetidylserine synthase belongs to subclass II phosphatidylserine synthase (B. subtilis type) on the basis of not only homology but also substrate specificity and some enzymatic properties. The possibility that a gene encoding the subclass II phosphatidylserine synthase might be transferred from a bacterium to an ancestor of methanogens is discussed.  (+info)

Accepted name: phosphatidylcholine synthase. Reaction: CDP-diacylglycerol + choline = CMP + phosphatidylcholine. Other name(s): CDP-diglyceride-choline O-phosphatidyltransferase. Systematic name: CDP-diacylglycerol:choline O-phosphatidyltransferase. Comments: Requires divalent cations, with Mn2+ being more effective than Mg2+.. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 243666-86-6. References: 1. de Rudder, K.E.E., Sohlenkamp, C. and Geiger, O. Plant-exudated choline is used for rhizobial membrane lipid biosynthesis by phosphatidylcholine synthase. J. Biol. Chem. 274 (1999) 20011-20016. [PMID: 10391951]. 2. Sohlenkamp, C., de Rudder, K.E.E., Röhrs, V., López-Lara, I.M. and Geiger, O. Cloning and characterization of the gene for phosphatidylcholine synthase. J. Biol. Chem. 275 (2000) 18919-18925. [PMID: 10858449]. ...
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Several weak hits in gapped BLAST to PSGA sequences, e.g. residues 75-210 are 36% similar to PGSA_MYCPN. All similarities begin at around residue 75 of UU364. MG114, CT797, TP0256 and CT496 are predicted phosphatidylglycerophosphate synthases with similarities to UU364 beginning around residue 17 ...
In medicine, phosphatidylserine is used to support the treatment of dementia and hyperactivity. The use of phosphatidylserine is intended to improve the
Phosphatidylserine is a phospholipid that is a component of cell membranes in your body. Its been associated with a number of benefits, from...
Phosphatidylserine supplies a supplemental source of this important phospholipid, which is a structural part of biological membranes. Available at druglessdoctor.com.
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Cant afford them both so which would be more desirable for keeping cortisol levels lower. Having great results with Phosphatidylserine 800 to 1000mgs
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CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase: An enzyme that catalyzes the formation of PHOSPHATIDYLINOSITOL and CMP from CDP-DIACYLGLYCEROL and MYOINOSITOL.
... , Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.
PS 100 (standardized phosphatidylserine) Supports mental function Phosphatidylserine is a phospholipid found in all cells, but is most concentrated in brain cells. This familiarly-called brain nutrient supports cognitive function, emotional well-being and behavioral performance by restoring cell membrane composition. It has also been shown to support memory. In a double blind placebo controlled multicenter study of 425 individuals, daily supplementation of phosphatidylserine over six months resulted in statistically significant support of behavioral and cognitive parameters. In another six-month study of 40 individuals, phosphatidylserine supplementation enhanced cerebral metabolism and outcomes of cognitive training. These findings are consistent with earlier studies. In a placebo- controlled investigation of 149 subjects, the group receiving phosphatidylserine scored higher than placebo in performance tests related to memory tasks of daily life. In a trial of 35 subjects, those receiving
MetabolismFatty acid and phospholipid metabolismBiosynthesisfatty acid/phospholipid synthesis protein PlsX (TIGR00182; HMM-score: 408.3) ...
Fingerprint Dive into the research topics of Effect of membrane phospholipid composition changes on adenylate cyclase activity in normal and rous-sarcoma-transformed chicken embryo fibroblasts. Together they form a unique fingerprint. ...
In the presence of the drug, the incorporation of cytidine, but not of inorganic phosphate, into phosphatidyl-CMP (CDP-diacylglycerol) was dependent on the cytidine concentration ...
Gene Information This gene encodes a member of the family of adenylate cyclases which are membrane-associated enzymes that catalyze the formation of the secondary messenger cyclic adenosine monophosphate (cAMP). Mouse studies show that adenylate cyclase 4 along with adenylate cyclases 2 and 3 is expressed in olfactory cilia suggesting that several different adenylate cyclases may couple to olfactory receptors and that there may be multiple receptor-mediated mechanisms for the generation of cAMP signals. Alternative splicing results in transcript variants. [provided by RefSeq Nov 2010]. ...
Low prices on Phosphatidylserine! Phosphatidylserine supports memory, focus and athletic performance*. Phosphatidylserine (PS) is a phospholipid (a fat containing phosphorus) found in every cell membrane in our bodies. It has many functions, but most important is its role in brain health. Clinical studies have shown PS to support brain glucose metabolism.
BoostCeuticals is currently manufacturing a good quality supplement which actually contains Phosphatidyl serine 100 mg daily dose. This type of dosage is popular and effective but can it be even better. Combining this Phosphatidylserine dosage with other important complimentary ingredients makes it a true Phosphatidylserine complex. It is also well documented how it works so much better with DMAE and this is included all in one supplement ...
BeWellBuzz) Phosphatidylserine belongs to a class of chemicals known as phospholipids, which are fat-soluble chemicals that are vital for cell membranes.Phosphatidylserine is a non-essential nutrient. The term non-essential nutrient refers to nutrients that our body can produce naturally. We can also procure Phosphatidylserine from food. With that said, it is important ... Continue Reading ...
BeWellBuzz) Phosphatidylserine belongs to a class of chemicals known as phospholipids, which are fat-soluble chemicals that are vital for cell membranes.Phosphatidylserine is a non-essential nutrient. The term non-essential nutrient refers to nutrients that our body can produce naturally. We can also procure Phosphatidylserine from food. With that said, it is important ... Continue Reading ...
Buy PHOSPHATIDYL SERINE Online.Phosphatidylserine consists of phosphatidylserine which is a phospholipid of vital importance for the good working order of the brain. On the other hand, Phosphatidylserine increa
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Clostridium butyricum phosphatidyltransferase: from Clostridium butyricum; catalyzes transfer of the phosphatidyl moiety of phosphatidylethanolamine, phosphatidylglycerol or phosphatidylserine to primary alcohols such as glycerol, serine and ethanolamine; catalyze transfer of both the diacyl and alkenyl acyl forms of glycerophospholipids, but the diacyl forms are used preferentially
Toxoplasma gondii is among the most prevalent protozoan parasites, which infects a wide range of organisms including one-third of the human population. Its rapid intracellular replication within a vacuole requires efficient synthesis of glycerophospholipids. Cytidine diphosphate-diacylglycerol (CDP-DAG) serves as a major precursor for phospholipid synthesis. Given the peculiarities of lipid biogenesis, understanding the mechanism and physiological importance of CDP-DAG synthesis is particularly relevant in T. gondii Here, we report the occurrence of two phylogenetically divergent CDP-DAG synthase (CDS) enzymes in the parasite. The eukaryotic-type TgCDS1 and the prokaryotic-type TgCDS2 reside in the endoplasmic reticulum (ER) and apicoplast, respectively. Conditional knockdown of TgCDS1 severely attenuated the parasite growth and resulted in a nearly complete loss of virulence in a mouse model. Moreover, mice infected with the TgCDS1 mutant became fully resistant to challenge infection with a ...
Purified Phosphatidylserine Apoptosis Kit (Green Fluorescence 405) from Creative Biomart. Phosphatidylserine Apoptosis Kit (Green Fluorescence 405) can be used for research.
... serine ethanolaminephosphotransferase EC 2.7.8.5: CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase EC 2.7.8.6 ... CDP-diacylglycerol-serine O-phosphatidyltransferase EC 2.7.8.9: phosphomannan mannosephosphotransferase EC 2.7.8.10: ... CDP-diacylglycerol-choline O-phosphatidyltransferase EC 2.7.8.25: triphosphoribosyl-dephospho-CoA synthase EC 2.7.8.26: ... L-serine-phosphatidylethanolamine phosphatidyltransferase EC 2.7.8.30: undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose ...
CDP-diacylglycerol-inositol 3-phosphatidyltransferase MeSH D08.811.913.696.900.150 --- CDP-diacylglycerol-serine O- ... Serine-type D-Ala-D-Ala carboxypeptidase MeSH D08.811.277.656.350.245.280 --- gamma-glutamyl hydrolase MeSH D08.811.277.656. ... serine-trna ligase MeSH D08.811.464.263.200.800 --- threonine-tRNA ligase MeSH D08.811.464.263.200.850 --- tryptophan-tRNA ... l-serine dehydratase MeSH D08.811.520.232.400.700 --- phenylalanine ammonia-lyase MeSH D08.811.520.232.400.850 --- threonine ...
L-serine, O-phosphatidyltransferase, and CDP-diacylglycerol:L-serine 3-O-phosphatidyltransferase. This enzyme participates in ... L-serine O-phosphatidyltransferase, phosphatidylserine synthetase, CDP-diacylglycerol-L-serine O-phosphatidyltransferase, ... a CDP-diacylglycerol-serine O-phosphatidyltransferase (EC 2.7.8.8) is an enzyme that catalyzes the chemical reaction CDP- ... CDP-diglyceride-L-serine phosphatidyltransferase, CDP-diglyceride:serine phosphatidyltransferase, cytidine 5'-diphospho-1,2- ...
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase. *CDP-diacylglycerol-serine O-phosphatidyltransferase. *CDP- ... protein serine/threonine kinase activity. • GO:0001948 protein binding. • insulin receptor substrate binding. • ATP binding. • ... positive regulation of peptidyl-serine phosphorylation. • platelet activation. • Fc-epsilon receptor signaling pathway. • ...
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase. *CDP-diacylglycerol-serine O-phosphatidyltransferase. *CDP- ...
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase. *CDP-diacylglycerol-serine O-phosphatidyltransferase. *CDP- ...
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase. *CDP-diacylglycerol-serine O-phosphatidyltransferase. *CDP- ...
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase. *CDP-diacylglycerol-serine O-phosphatidyltransferase. *CDP- ...
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase. *CDP-diacylglycerol-serine O-phosphatidyltransferase. *CDP- ... Phosphorylation occurs at two sites within the heptapeptide repeat, at Serine 5 and Serine 2. Serine 5 phosphorylation is ... It has a kinase activity that phosphorylates the C-terminal domain (CTD) of Pol II at the amino acid serine. This switches the ... The CTD consists of repetitions of an amino acid motif, YSPTSPS, of which Serines and Threonines can be phosphorylated. The ...
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase. *CDP-diacylglycerol-serine O-phosphatidyltransferase. *CDP- ... A serine/threonine protein kinase (EC 2.7.11.1) is a kinase enzyme that phosphorylates the OH group of serine or threonine ( ... Serine/threonine-specific protein kinase. From Wikipedia, the free encyclopedia. (Redirected from Non-specific serine/threonine ... While serine/threonine kinases all phosphorylate serine or threonine residues in their substrates, they select specific ...
CDIPT: CDP-diacylglycerol-inositol 3-phosphatidyltransferase. *CFDP1: Craniofacial development protein 1. *CHDS1: Coronary ... TAO2: encoding Serine/threonine-protein kinase TAO2. *TBC1D24: encoding protein TBC1 domain family, member 24 ...
Fosfatidat citidililtransferaza (EC 2.7.7.41, CDP digliceridna pirofosforilaza, CDP-diacilglicerolna sintaza, CDP-diacilgliceridna sintetaza, citidin difosfogliceridna pirofosforilaza, fosfatidat citidiltransferaza, fosfatidinsko kiselinska citidililtransferaza, CTP:1,2-diacilglicerofosfat-citidil transferaza, CTP-diacilglicerol sintetaza, DAG sintetaza, CDP-DG) je enzim sa sistematskim imenom CTP:fosfatidat citidililtransferaza.[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju. ...
Fosfatidat citidililtransferaza (EC 2.7.7.41, CDP digliceridna pirofosforilaza, CDP-diacilglicerolna sintaza, CDP-diacilgliceridna sintetaza, citidin difosfogliceridna pirofosforilaza, fosfatidat citidiltransferaza, fosfatidinsko kiselinska citidililtransferaza, CTP:1,2-diacilglicerofosfat-citidil transferaza, CTP-diacilglicerol sintetaza, DAG sintetaza, CDP-DG) je enzim sa sistematskim imenom CTP:fosfatidat citidililtransferaza.[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju. ...
In enzymology, a diacylglycerol cholinephosphotransferase (EC 2.7.8.2) is an enzyme that catalyzes the chemical reaction CDP-choline + 1,2-diacylglycerol ⇌ {\displaystyle \rightleftharpoons } CMP + a phosphatidylcholine Thus, the two substrates of this enzyme are CDP-choline and 1,2-diacylglycerol, whereas its two products are CMP and phosphatidylcholine. This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP choline:1,2-diacylglycerol cholinephosphotransferase. Other names in common use include: 1-alkyl-2-acetyl-m-glycerol:CDPcholine choline phosphotransferase, 1-alkyl-2-acetyl-sn-glycerol cholinephosphotransferase, 1-alkyl-2-acetylglycerol cholinephosphotransferase, alkylacylglycerol choline phosphotransferase, alkylacylglycerol cholinephosphotransferase, CDP-choline diglyceride phosphotransferase, cholinephosphotransferase, CPT, cytidine diphosphocholine glyceride ...
Thus, the two substrates of this enzyme are ATP and uridine, whereas its two products are ADP and UMP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:uridine 5'-phosphotransferase. Other names in common use include pyrimidine ribonucleoside kinase, uridine-cytidine kinase, uridine kinase (phosphorylating), and uridine phosphokinase. This enzyme participates in pyrimidine metabolism. ...
Ratliff, R.L., Weaver, R.H., Lardy, H.A. and Kuby, S.A. (1964). "Nucleoside triphosphate-nucleoside diphosphate transphosphorylase (nucleoside diphosphokinase). I. Isolation of the crystalline enzyme from brewers' yeast". J. Biol. Chem. 239: 301-309. PMID 14114857. ...
... (also known as CK,ChoK and choline phosphokinase) is an enzyme which catalyzes the first reaction in the choline pathway for phosphatidylcholine (PC) biosynthesis. This reaction involves the transfer of a phosphate group from adenosine triphosphate (ATP) to choline in order to form phosphocholine. ATP + choline ⇌ {\displaystyle \rightleftharpoons } ADP + O-phosphocholine Thus, the two substrates of this enzyme are ATP and choline, whereas its two products are adenosine diphosphate (ADP) and O-phosphocholine. Choline kinase requires magnesium ions (+2) as a cofactor for this reaction. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The first detailed investigation of the enzyme was conducted by McCamen in 1962, where it was shown that the brain is the richest source of the enzyme in mammalian tissue. A related enzyme, ethanolamine kinase, tends to co-purify ...
Saint Girons, I.S., Gilles, A.-M., Margarita, D., Michelson, S., Monnot, M., Fermandjian, S., Danchin, A. and Barzu, O. (1987). „Structural and catalytic characteristics of Escherichia coli adenylate kinase". J. Biol. Chem. 262: 622-629. PMID 3027060 ...
In enzymology, a 2-dehydro-3-deoxygluconokinase (EC 2.7.1.45) is an enzyme that catalyzes the chemical reaction ATP + 2-dehydro-3-deoxy-D-gluconate ⇌ {\displaystyle \rightleftharpoons } ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate Thus, the two substrates of this enzyme are ATP and 2-dehydro-3-deoxy-D-gluconate, whereas its two products are ADP and 6-phospho-2-dehydro-3-deoxy-D-gluconate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:2-dehydro-3-deoxy-D-gluconate 6-phosphotransferase. Other names in common use include 2-keto-3-deoxygluconokinase, 2-keto-3-deoxy-D-gluconic acid kinase, 2-keto-3-deoxygluconokinase (phosphorylating), 2-keto-3-deoxygluconate kinase, and ketodeoxygluconokinase. This enzyme participates in pentose phosphate pathway and pentose and glucuronate interconversions. As of late 2007, only one structure ...
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 is an enzyme that in humans is encoded by the PFKFB2 gene.[5] The protein encoded by this gene is involved in both the synthesis and degradation of fructose-2,6-bisphosphate, a regulatory molecule that controls glycolysis in eukaryotes. The encoded protein has a 6-phosphofructo-2-kinase activity that catalyzes the synthesis of fructose-2,6-bisphosphate, and a fructose-2,6-biphosphatase activity that catalyzes the degradation of fructose-2,6-bisphosphate. This protein regulates fructose-2,6-bisphosphate levels in the heart, while a related enzyme encoded by a different gene regulates fructose-2,6-bisphosphate levels in the liver and muscle. This enzyme functions as a homodimer. Two transcript variants encoding two different isoforms have been found for this gene.[5] ...
Researcher D. G. Walker of the University of Birmingham determined the presence of two specific enzymes in adult guinea pig liver, both of which catalyze the phosphorylation of glucose to glucose 6 phosphate.[dubious - discuss] The two enzymes have been identified as a specific glucokinase (ATP-D-glucose 6-phosphotransferase) and non-specific hexokinase (ATP-D-hexose 6-phosphotransferase). Hepatic cells are freely permeable to glucose, and the initial rate of phosphorylation of glucose is the rate-limiting step in glucose metabolism by the liver (ATP-D-glucose 6-phosphotransferase) and non-specific hexokinase (ATP-D-hexose 6-phosphotransferase).[6]. The role of glucose 6-phosphate in glycogen synthase: High blood glucose concentration causes an increase in intracellular levels of glucose 6 phosphate in liver, skeletal muscle and fat (adipose) tissue. (ATP-D-glucose 6-phosphotransferase) and non-specific hexokinase (ATP-D-hexose 6-phosphotransferase). In liver, synthesis of glycogen is directly ...
... s (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the (enzyme's) active site. They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like. In humans, they are responsible for coordinating various physiological functions, including digestion, immune response, blood coagulation and reproduction. The MEROPS protease classification system counts 16 superfamilies (as of 2013) each containing many families. Each superfamily uses the catalytic triad or dyad in a different protein fold and so represent convergent evolution of the catalytic mechanism. The majority belong to the S1 family of the PA clan (superfamily) of proteases. For superfamilies, P = superfamily, containing a mixture of nucleophile class families, S = purely serine ...
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is O-phosphoserine phosphohydrolase. This enzyme participates in glycine, serine and threonine metabolism. ...
de Graaf K، Hekerman P، Spelten O، وآخرون. (2004). "Characterization of cyclin L2, a novel cyclin with an arginine/serine-rich domain: phosphorylation by DYRK1A and colocalization with splicing factors". J. Biol. Chem. 279 (6): 4612-24. PMID 14623875. doi:10.1074/jbc.M310794200. ...
CDPdiacylglycerol-Serine O-PhosphatidyltransferaseIBA 01/01/2014 - "Gain-of-function mutations in the phosphatidylserine ...
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase. *CDP-diacylglycerol-serine O-phosphatidyltransferase. *CDP- ...
L-serine, O-phosphatidyltransferase, and CDP-diacylglycerol:L-serine 3-O-phosphatidyltransferase. This enzyme participates in ... L-serine O-phosphatidyltransferase, phosphatidylserine synthetase, CDP-diacylglycerol-L-serine O-phosphatidyltransferase, ... a CDP-diacylglycerol-serine O-phosphatidyltransferase (EC 2.7.8.8) is an enzyme that catalyzes the chemical reaction CDP- ... CDP-diglyceride-L-serine phosphatidyltransferase, CDP-diglyceride:serine phosphatidyltransferase, cytidine 5-diphospho-1,2- ...
CDP-diacylglycerol--serine O-phosphatidyltransferase (EC:2.7.8.8*Search proteins in UniProtKB for this EC number. ... sp,Q9ZBM2,PSS_MYCLE CDP-diacylglycerol--serine O-phosphatidyltransferase OS=Mycobacterium leprae (strain TN) OX=272631 GN=pssA ... Belongs to the CDP-alcohol phosphatidyltransferase class-I family.Curated. Keywords - Domaini. Transmembrane, Transmembrane ... 1,2-diacyl-sn-glycero-3-phospho-L-serine*Search proteins in UniProtKB for this molecule. ...
CDP-diacylglycerol-serine O-phosphatidyltransferase (pss; comp44746_c0), and two phosphatidylserine decarboxylase proenzymes ( ... one CDP-diacylglycerol-serine O-phosphatidyltransferase transcript (encoded by pss) displayed significantly decreased ... CDP-diacylglycerol-serine O-phosphatidyltransferase; psd, phosphatidylserine decarboxylase proenzyme; chl, magnesium-chelatase ... Serine/threonine-protein kinases are crucial components of diverse signaling pathways and for regulation of cell proliferation ...
Serine-phosphoethanolamine synthase Pages 35-38 * CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase ...
CDP-diacylglycerol/serine O-phosphatidyltransferase [Rh. 1. 2e-72. 86357048. 281. CDP-diacylglycerol-serine O- ... serine O-phosphatidyltransferase; InterPro: IPR004533 This enzyme, CDP-diacylglycerol--serine O-phosphatidyltransferase, is ... 0003882 CDP-diacylglycerol-serine O-phosphatidyltransferase activity, 0008654 phospholipid biosynthetic process, 0046341 CDP- ... CDP-diacylglycerol/serine O-phosphatidyltransferase [Rh. 1. 8e-72. >gi,315121771,ref,YP_004062260.1, phosphatidylserine ...
... upregulated via increased levels of phosphatidylserine decarboxylase and CDP-diacylglycerol-serine O-phosphatidyltransferase. ... and a trypsin-like serine protease suggest that individual amino acids along with proteins may be broken down for use as ...
CDP-diacylglycerol--serine O-phosphatidyltransferase. Alternative Name(s). CDP-diglycerine-serine O-phosphatidyltransferase.. ...
CDP-DIACYLGLYCEROL - SERINE O-PHOSPHATIDYLTRANSFERASE (EC 2.7.8.8) (PHOSPHATIDYLSERINE SYNTHASE).. OS006763.1_at. gb,Z95637 ...
"CDP-diacylglycerol--serine O-phosphatidyltransferase" /protein_id="WP_002963601.1" /translation=" ... "CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase" /protein_id="WP_002963840.1" /translation=" ... "DegP-like serine endoprotease" /protein_id="WP_002963760.1" /translation="MSRARISNYRKGVAAVALSAALAGAFVVTGPLGALNEARAEAVH ... "serine hydrolase family protein" /protein_id="WP_004688257.1" /translation="MKVKDADILIIPGYTNSGPDHWQTRWESKLSTARRVQQAEWSKP ...
ORYSJ CDP-diacylglycerol--serine O-phosphatidyltransferase 1 (EC 2.7.8.8) (Phosphatidylserine synthase 1) [PSS1] [LOC_ ... Serine racemase (EC 4.3.1.17) (EC 4.3.1.18) (EC 5.1.1.18) (D-serine ammonia-lyase) (D-serine dehydratase) (L-serine ammonia- ... Serine carboxypeptidase 1 chain A (Serine carboxypeptidase I chain A); Serine carboxypeptidase 1 chain B (Serine ... ORYSJ CDP-diacylglycerol--serine O-phosphatidyltransferase 3 (EC 2.7.8.8) (Phosphatidylserine synthase 3) [PSS3] [Os01g0683500/ ...
"CDP-diacylglycerol--serine FT /gene_family="HOG000270167" [ FAMILY / ALN / TREE ] FT O-phosphatidyltransferase" FT /codon_start ... "serine acetyltransferase" FT /gene_family="HOG000049437" [ FAMILY / ALN / TREE ] FT /codon_start="1" FT /locus_tag="VVM_00433" ... "serine/threonine protein kinase" FT /transl_table="11" FT /db_xref="GI:320154918" FT /db_xref="GeneID:10164778" FT /translation ... "serine--pyruvate FT /gene_family="HOG000171815" [ FAMILY / ALN / TREE ] FT aminotransferase/L-alanine:glyoxylate ...
... serine ethanolaminephosphotransferase EC 2.7.8.5: CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase EC 2.7.8.6 ... CDP-diacylglycerol-serine O-phosphatidyltransferase EC 2.7.8.9: phosphomannan mannosephosphotransferase EC 2.7.8.10: ... CDP-diacylglycerol-choline O-phosphatidyltransferase EC 2.7.8.25: triphosphoribosyl-dephospho-CoA synthase EC 2.7.8.26: ... L-serine-phosphatidylethanolamine phosphatidyltransferase EC 2.7.8.30: undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose ...
CDP-diacylglycerol-inositol 3-phosphatidyltransferase MeSH D08.811.913.696.900.150 --- CDP-diacylglycerol-serine O- ... Serine-type D-Ala-D-Ala carboxypeptidase MeSH D08.811.277.656.350.245.280 --- gamma-glutamyl hydrolase MeSH D08.811.277.656. ... serine-trna ligase MeSH D08.811.464.263.200.800 --- threonine-tRNA ligase MeSH D08.811.464.263.200.850 --- tryptophan-tRNA ... l-serine dehydratase MeSH D08.811.520.232.400.700 --- phenylalanine ammonia-lyase MeSH D08.811.520.232.400.850 --- threonine ...
CDPdiacylglycerol-serine O-phosphatidyl-transferase Current Synonym true false 8463019 Phosphatidylserine synthase Current ... Cytidine diphosphate (CDP) diacylglycerol-serine O-phosphatidyl-transferase Current Synonym true false 2913579016 Cytidine ... Cytidine diphosphate diacylglycerol-serine O-phosphatidyl-transferase (substance). Code System Preferred Concept Name. Cytidine ... diphosphate diacylglycerol-serine O-phosphatidyl-transferase Current Synonym true false 8462012 ...
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase. *CDP-diacylglycerol-serine O-phosphatidyltransferase. *CDP- ... protein serine/threonine kinase activity. • GO:0001948 protein binding. • insulin receptor substrate binding. • ATP binding. • ... positive regulation of peptidyl-serine phosphorylation. • platelet activation. • Fc-epsilon receptor signaling pathway. • ...
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase. *CDP-diacylglycerol-serine O-phosphatidyltransferase. *CDP- ...
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase. *CDP-diacylglycerol-serine O-phosphatidyltransferase. *CDP- ...
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase. *CDP-diacylglycerol-serine O-phosphatidyltransferase. *CDP- ...
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase. *CDP-diacylglycerol-serine O-phosphatidyltransferase. *CDP- ... Phosphorylation occurs at two sites within the heptapeptide repeat, at Serine 5 and Serine 2. Serine 5 phosphorylation is ... It has a kinase activity that phosphorylates the C-terminal domain (CTD) of Pol II at the amino acid serine. This switches the ... The CTD consists of repetitions of an amino acid motif, YSPTSPS, of which Serines and Threonines can be phosphorylated. The ...
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase. *CDP-diacylglycerol-serine O-phosphatidyltransferase. *CDP- ... A serine/threonine protein kinase (EC 2.7.11.1) is a kinase enzyme that phosphorylates the OH group of serine or threonine ( ... Serine/threonine-specific protein kinase. From Wikipedia, the free encyclopedia. (Redirected from Non-specific serine/threonine ... While serine/threonine kinases all phosphorylate serine or threonine residues in their substrates, they select specific ...
CDPdiacylglycerol-Serine O-Phosphatidyltransferase. *Phosphoric Monoester Hydrolases. Secondary source IDs. *GENBANK/D16444 ...
CDPdiacylglycerol-Serine O-Phosphatidyltransferase 2 Scopus citations 2013 The Lack of Maturation of Ebola Virus-Infected ...
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase. CDP-diacylglycerol--serine O-phosphatidyltransferase. ... L-Serine. H. +. Cytidine. monophosphate. PS(19:iso/18:1(9Z)). Glycerol. 3-phosphate. H. +. Cytidine. monophosphate. PG(16:1(9Z ... serine O-. phosphatidyltransferase. CDP-. diacylglycerol-. -glycerol-3-. phosphate 3-. phosphatidyltransferase. Putative. ... L-Serine. Hydrogen Ion. Cytidine. monophosphate. PS(19:iso/18:1(9Z)). Glycerol. 3-phosphate. Hydrogen Ion. Cytidine. ...
  • Serine can be catabolized back to the glycolytic intermediate, 3-phosphoglycerate, by a pathway that is essentially a reversal of serine biosynthesis. (ymdb.ca)