An enzyme that catalyzes the formation of PHOSPHATIDYLINOSITOL and CMP from CDP-DIACYLGLYCEROL and MYOINOSITOL.
A class of enzymes that transfers substituted phosphate groups. EC 2.7.8.
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.
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.
An enzyme that catalyzes the formation of phosphatidylserine and CMP from CDPdiglyceride plus serine. EC 2.7.8.8.
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.

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)

CDP-diacylglycerol-inositol 3-phosphatidyltransferase is an enzyme that plays a role in the synthesis of phosphatidylinositol (PI) lipids, which are important components of cell membranes and also serve as secondary messengers in intracellular signaling pathways.

The enzyme catalyzes the transfer of a phosphate group from CDP-diacylglycerol to the 3-hydroxyl position of inositol, resulting in the formation of phosphatidylinositol 3-phosphate (PI3P). PI3P is a key signaling molecule that regulates various cellular processes, including membrane trafficking, autophagy, and inflammation.

CDP-diacylglycerol-inositol 3-phosphatidyltransferase is also known as phosphatidylinositol 3-kinase (PI3K) or type II PI3K, and it is distinct from the class I PI3Ks that are involved in growth factor signaling and oncogenesis. Mutations in CDP-diacylglycerol-inositol 3-phosphatidyltransferase have been implicated in various diseases, including cancer, neurodevelopmental disorders, and autoimmune diseases.

Phosphotransferases are a group of enzymes that catalyze the transfer of a phosphate group from a donor molecule to an acceptor molecule. This reaction is essential for various cellular processes, including energy metabolism, signal transduction, and biosynthesis.

The systematic name for this group of enzymes is phosphotransferase, which is derived from the general reaction they catalyze: D-donor + A-acceptor = D-donor minus phosphate + A-phosphate. The donor molecule can be a variety of compounds, such as ATP or a phosphorylated protein, while the acceptor molecule is typically a compound that becomes phosphorylated during the reaction.

Phosphotransferases are classified into several subgroups based on the type of donor and acceptor molecules they act upon. For example, kinases are a subgroup of phosphotransferases that transfer a phosphate group from ATP to a protein or other organic compound. Phosphatases, another subgroup, remove phosphate groups from molecules by transferring them to water.

Overall, phosphotransferases play a critical role in regulating many cellular functions and are important targets for drug development in various diseases, including cancer and neurological disorders.

Cytidine diphosphate-diacylglycerol (CDP-DAG) is a bioactive lipid molecule that plays a crucial role in the synthesis of other lipids and is also involved in cell signaling pathways. It is formed from the reaction between cytidine diphosphocholine (CDP-choline) and phosphatidic acid, catalyzed by the enzyme CDP-choline:1,2-diacylglycerol cholinephosphotransferase.

CDP-DAG is a critical intermediate in the biosynthesis of several important lipids, including phosphatidylglycerol (PG), cardiolipin (CL), and platelet-activating factor (PAF). These lipids are essential components of cell membranes and have various functions in cell signaling, energy metabolism, and other physiological processes.

CDP-DAG also acts as a second messenger in intracellular signaling pathways, particularly those involved in the regulation of gene expression, cell proliferation, differentiation, and survival. It activates several protein kinases, including protein kinase C (PKC) isoforms, which phosphorylate and regulate various target proteins, leading to changes in their activity and function.

Abnormalities in CDP-DAG metabolism have been implicated in several diseases, including cancer, cardiovascular disease, and neurological disorders. Therefore, understanding the regulation and function of CDP-DAG and its downstream signaling pathways is an active area of research with potential therapeutic implications.

CDP-diacylglycerol-serine O-phosphatidyltransferase is an enzyme that plays a role in the synthesis of phosphatidylserine, a type of phospholipid found in cell membranes. The systematic name for this enzyme is CDP-diacylglycerol:L-serine O-phosphatidyltransferase. It catalyzes the following chemical reaction:

CDP-diacylglycerol + L-serine = CMP + O-phosphatidylserine

This enzyme is involved in the Kennedy pathway, which is the main pathway for the biosynthesis of glycerophospholipids in eukaryotic cells. CDP-diacylglycerol-serine O-phosphatidyltransferase is located in the endoplasmic reticulum and is essential for the synthesis of phosphatidylserine, which is an important structural component of cell membranes and also serves as a precursor for the biosynthesis of other phospholipids. Defects in this enzyme have been associated with neurological disorders.

Serine is an amino acid, which is a building block of proteins. More specifically, it is a non-essential amino acid, meaning that the body can produce it from other compounds, and it does not need to be obtained through diet. Serine plays important roles in the body, such as contributing to the formation of the protective covering of nerve fibers (myelin sheath), helping to synthesize another amino acid called tryptophan, and taking part in the metabolism of fatty acids. It is also involved in the production of muscle tissues, the immune system, and the forming of cell structures. Serine can be found in various foods such as soy, eggs, cheese, meat, peanuts, lentils, and many others.

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 and CDP-diacylglycerol-serine O-phosphatidyltransferase. ...
... serine ethanolaminephosphotransferase EC 2.7.8.5: CDP-diacylglycerol-glycerol-3-phosphate 1-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: Now EC 2.4.2.52, triphosphoribosyl-dephospho-CoA synthase EC ... L-serine-phosphatidylethanolamine phosphatidyltransferase EC 2.7.8.30: Now EC 2.4.2.53, undecaprenyl-phosphate 4-deoxy-4- ...
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 ligase ... protein-serine-threonine kinases MeSH D08.811.913.696.620.682.700.062 - activin receptors MeSH D08.811.913.696.620.682.700.062. ...
CDP-diacylglycerol-inositol 3-phosphatidyltransferase CFDP1: Craniofacial development protein 1 CHDS1: Coronary heart disease, ... encoding Serine/threonine-protein kinase TAO2 TBC1D24: encoding protein TBC1 domain family, member 24 TEDC2: encoding protein ...
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- ...
Phosphatidyl serine is a nutrient used in some supplement products. ... Cdp-diacylglycerol-serine o-phosphatidyltransferase activity. Specific Function. Catalyzes a base-exchange reaction in which ... Phosphatidyl serine. DrugBank Accession Number. DB00144. Background. Phosphatidyl serine (PS) is a phospholipid nutrient found ... Phosphatidyl serine (12 mg/1) + 1,2-docosahexanoyl-sn-glycero-3-phosphoserine calcium (6.4 mg/1) + 1,2-icosapentoyl-sn-glycero- ...
CDP-diacylglycerol--serine O-phosphatidyltransferase 145, 308. DVU3005. aminotransferase 22, 145. DVU3157. hypothetical protein ...
CDP-diacylglycerol/serine O-phosphatidyltransferase YP_002551570 normal 1 n/a Acidovorax ebreus TPSY Bacteria -. ...
regulation of CDP-diacylglycerol-serine O-phosphatidyltransferase activity GO:1904217 * negative regulation of DNA-directed DNA ...
CDP Diacylglycerol-Serine use CDPdiacylglycerol-Serine O-Phosphatidyltransferase O-Phosphatidyltransferase, CDPdiacylglycerol- ... O-Acetyltransferase, Serine use Serine O-Acetyltransferase O-Acyltransferase 1, Diacylglycerol use Diacylglycerol O- ... O-Acetyltransferase, L-Serine use Serine O-Acetyltransferase ... Serine use CDPdiacylglycerol-Serine O-Phosphatidyltransferase o ...
CDP Diacylglycerol-Serine use CDPdiacylglycerol-Serine O-Phosphatidyltransferase O-Phosphatidyltransferase, CDPdiacylglycerol- ... O-Acetyltransferase, Serine use Serine O-Acetyltransferase O-Acyltransferase 1, Diacylglycerol use Diacylglycerol O- ... O-Acetyltransferase, L-Serine use Serine O-Acetyltransferase ... Serine use CDPdiacylglycerol-Serine O-Phosphatidyltransferase o ...
CDP Diacylglycerol-Serine use CDPdiacylglycerol-Serine O-Phosphatidyltransferase O-Phosphatidyltransferase, CDPdiacylglycerol- ... O-Acetyltransferase, Serine use Serine O-Acetyltransferase O-Acyltransferase 1, Diacylglycerol use Diacylglycerol O- ... O-Acetyltransferase, L-Serine use Serine O-Acetyltransferase ... Serine use CDPdiacylglycerol-Serine O-Phosphatidyltransferase o ...
CDP Diacylglycerol-Serine use CDPdiacylglycerol-Serine O-Phosphatidyltransferase O-Phosphatidyltransferase, CDPdiacylglycerol- ... O-Acetyltransferase, Serine use Serine O-Acetyltransferase O-Acyltransferase 1, Diacylglycerol use Diacylglycerol O- ... O-Acetyltransferase, L-Serine use Serine O-Acetyltransferase ... Serine use CDPdiacylglycerol-Serine O-Phosphatidyltransferase o ...
CDP Diacylglycerol-Serine use CDPdiacylglycerol-Serine O-Phosphatidyltransferase O-Phosphatidyltransferase, CDPdiacylglycerol- ... O-Acetyltransferase, Serine use Serine O-Acetyltransferase O-Acyltransferase 1, Diacylglycerol use Diacylglycerol O- ... O-Acetyltransferase, L-Serine use Serine O-Acetyltransferase ... Serine use CDPdiacylglycerol-Serine O-Phosphatidyltransferase o ...
CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity GO:0003881 * glucose-1-phosphate thymidylyltransferase activity ... UDP-N-acetylglucosamine:serine-protein N-acetylglucosamine-1-phosphotransferase activity GO:0018421 ...
5. CDP-diacylglycerol--inositol 3-phosphatidyltransferase. General function:. Involved in phosphotransferase activity, for ... 1. Serine/threonine-protein kinase VPS15. General function:. vacuole inheritance. Specific function:. Serine/threonine-protein ... Serine/threonine-protein kinase VPS15. General function:. vacuole inheritance. Specific function:. Serine/threonine-protein ... CDP-diacylglycerol + myo-inositol = CMP + phosphatidyl-1D-myo-inositol. Gene Name:. PIS1. Uniprot ID:. P06197 Molecular weight: ...
HUMAN CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial OS=Homo sapiens GN=PGS1 PE=2 SV=1 ... HUMAN Serine/threonine-protein phosphatase PP1-alpha catalytic subunit OS=Homo sapiens GN=PPP1CA PE=1 SV=1 ... HUMAN CDP-diacylglycerol--inositol 3-phosphatidyltransferase OS=Homo sapiens GN=CDIPT PE=1 SV=1 ... HUMAN Serine/threonine-protein phosphatase 6 regulatory subunit 3 OS=Homo sapiens GN=PPP6R3 PE=1 SV=2 ...
CDP-diacylglycerol--glycerol-3-phosphate3-phosphatidyltransferase. NP_389574.2. BBF10K_000900. ymdA. ribonuclease Y. NP_ ... serine--tRNA ligase. NP_387894.1. BBF10K_000754. dnaX. DNA polymerase III subunit gamma/tau. NP_387900.2. BBF10K_000755. ...
CDP-diacylglycerol---glycerol-3-phosphate 3-phosphatidyltransferase [EC:2.7.8.5]. K00998 CDP-diacylglycerol---serine O- ... CDP-diacylglycerol---serine O-phosphatidyltransferase [EC:2.7.8.8]. K17464 D-glucosaminate PTS system EIIA component [EC:2.7. ... L-serine kinase (ADP) [EC:2.7.1.226]. K23371 L-serine kinase (ATP) / ParB family transcriptional regulator, heme-responsive ...
CDP-diacylglycerol---glycerol-3-phosphate 3-phosphatidyltransferase [EC:2.7.8.5]. K00998 CDP-diacylglycerol---serine O- ... CDP-diacylglycerol---serine O-phosphatidyltransferase [EC:2.7.8.8]. K17464 D-glucosaminate PTS system EIIA component [EC:2.7. ... L-serine kinase (ADP) [EC:2.7.1.226]. K23371 L-serine kinase (ATP) / ParB family transcriptional regulator, heme-responsive ...
... positive regulation of CDP-diacylglycerol-serine O-phosphatidyltransferase activity; and positive regulation of serine C- ...
CDP Diacylglycerol-Serine O-Phosphatidyltransferase CDP Diglyceride Serine O-Phosphatidyltransferase CDP-DG Synthase ... CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase [D08.811.913.696.900.074] * CDPdiacylglycerol-Serine O- ... CDP Diacylglycerol-Serine O-Phosphatidyltransferase Term UI T031671. Date12/04/1996. LexicalTag NON. ThesaurusID NLM (1998). ... CDPdiacylglycerol-Serine O-Phosphatidyltransferase Preferred Term Term UI T031672. Date01/01/1999. LexicalTag ACX. ThesaurusID ...
CDP Diacylglycerol-Serine O-Phosphatidyltransferase CDP Diglyceride Serine O-Phosphatidyltransferase CDP-DG Synthase ... CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase [D08.811.913.696.900.074] * CDPdiacylglycerol-Serine O- ... CDP Diacylglycerol-Serine O-Phosphatidyltransferase Term UI T031671. Date12/04/1996. LexicalTag NON. ThesaurusID NLM (1998). ... CDPdiacylglycerol-Serine O-Phosphatidyltransferase Preferred Term Term UI T031672. Date01/01/1999. LexicalTag ACX. ThesaurusID ...
... positive regulation of CDP-diacylglycerol-serine O-phosphatidyltransferase activity, and positive regulation of C- ...
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- ...
negative regulation of CDP-diacylglycerol-serine O-phosphatidyltransferase activity GO:1904218 * 2-hydroxy-6-oxo-6-phenylhexa-2 ...
CDP-diacylglycerol--serine O-phosphatidyltransferase (NCBI ptt file). 31, 250. BC3579. BC3579. hypothetical Membrane Spanning ...
CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase N0000168246 CDPdiacylglycerol-Serine O-Phosphatidyltransferase ... N0000168147 Serine O-Acetyltransferase N0000180271 Serine Proteases N0000167788 Serine-tRNA Ligase N0000167580 Serine-Type D- ... N0000182091 Septins N0000169427 Sericins N0000006259 Serine N0000168133 Serine C-Palmitoyltransferase N0000007945 Serine ... T-Cell N0000175181 Receptor-Interacting Protein Serine-Threonine Kinase 2 N0000175180 Receptor-Interacting Protein Serine- ...
Metabolism Fatty acid and phospholipid metabolism Biosynthesis CDP-diacylglycerol-serine O-phosphatidyltransferase (TIGR00473; ... CDP-diacylglycerol--glycerol-3-phosphate 1-phosphatidyltransferase CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP + 3(3-sn- ... CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Fatty Acids, Lipids, and Isoprenoids ... no clan defined CDP-OH_P_transf; CDP-alcohol phosphatidyltransferase (PF01066; HMM-score: 60.1) ...
","CDP-diacylglycerol--serine O-phosphatidyltransferase 1","protein_coding" "lcl,VRMN01000004.1_cds_KAA8494654.1_3184"," ... Probable serine/threonine protein kinase IRE3 OS=Arabidopsis thaliana","protein_coding" "Cre16.g671100","30777420"," ... ","Serine protease ABC transporter B family tagA","protein_coding" "lcl,LHPG02000014.1_cds_PRW39112.1_2583","PRW39112"," ... ","Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B","protein_coding" "lcl,VRMN01000001.1_cds_ ...
D8.811.277.40.330.300.400.700.60 CDPdiacylglycerol-Serine O-Phosphatidyltransferase D8.586.913.696.900.150 D8.811.913.696. ... D8.811.277.656.300.760 Serine Proteinase Inhibitors D8.373.745.800 D27.505.519.389.745.800 D27.505.373.745.800 Serine-tRNA ... D24.611.834.877.903 L-Serine Dehydratase D8.586.520.241.300.750 D8.811.520.241.300.750 Laboratory Chemicals D26.600 D27.720.470 ... D8.811.682.135.848 Protein-Serine-Threonine Kinases D8.586.913.696.620.682.700 D8.811.913.696.620.682.700 Protein-Tyrosine ...
CDPdiacylglycerol-Serine O-Phosphatidyltransferase [D08.811.913.696.900.150] CDPdiacylglycerol-Serine O-Phosphatidyltransferase ... CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase [D08.811.913.696.900.074] CDP-Diacylglycerol-Inositol 3- ...
probable CDP-diacylglycerol--serine O-phosphatidyltransferase. QuickGO ontology. BLASTP. 1560908. 1561327. 420. halocyanin-like ...
CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase CDPdiacylglycerol-Serine O-Phosphatidyltransferase CDX2 Transcription ...
Chain: B: cdp-diacylglycerol--inositol 3-phosphatidyltransferase; c6nivA_. 1.45 protein fibril Chain: A: phenol-soluble modulin ... Chain: A: serine--trna ligase; c6gr8B_. 1.75 transferase Chain: B: inner centromere protein; ...
The purification procedure included Triton X-100 solubilization of the microsomal membranes, CDPdiacylglycerol-Sepharose ( ... but not by serine-protease inhibitors or by small peptide inhibitors. Its activity can be restored after chelation by excess ... phosphatidyltransferase, EC 2.7.8.11) was purified 1,000-fold from the microsomal fraction of Saccharomyces cerevisiae. ... and at serine residue in vivo. PMID- 6300026 TI - The application of nucleic acid chemistry to studies on the functional ...
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase. 64.37. 0.6930. 59. slr0012 Ribulose bisphosphate ... Serine/threonine kinase. 144.78. 0.7094. 134. slr1072 GDP-D-mannose dehydratase. 144.95. 0.6950. ...
  • In enzymology, a CDP-diacylglycerol-serine O-phosphatidyltransferase (EC 2.7.8.8) is an enzyme that catalyzes the chemical reaction CDP-diacylglycerol + L-serine ⇌ {\displaystyle \rightleftharpoons } CMP + (3-sn-phosphatidyl)-L-serine Thus, the two substrates of this enzyme are CDP-diacylglycerol and L-serine, whereas its two products are CMP and (3-sn-phosphatidyl)-L-serine. (wikipedia.org)
  • In enzymology , the term serine/threonine protein kinase describes a class of enzymes in the family of transferases , that transfer phosphates to the oxygen atom of a serine or threonine side chain in proteins . (cloudfront.net)
  • This enzyme participates in glycine, serine and threonine metabolism and glycerophospholipid metabolism. (wikipedia.org)
  • is a kinase enzyme , in particular a protein kinase , that phosphorylates the OH group of the amino-acid residues serine or threonine , which have similar side chains. (cloudfront.net)
  • At least 350 of the 500+ human protein kinases are serine/threonine kinases (STK). (cloudfront.net)
  • Serine/threonine kinases play a role in the regulation of cell proliferation, programmed cell death ( apoptosis ), cell differentiation, and embryonic development. (cloudfront.net)
  • While serine/threonine kinases all phosphorylate serine or threonine residues in their substrates, they select specific residues to phosphorylate on the basis of residues that flank the phosphoacceptor site, which together comprise the consensus sequence . (cloudfront.net)
  • Types include those acting directly as membrane-bound receptors ( Receptor protein serine/threonine kinase ) and intracellular kinases participating in Signal transduction . (cloudfront.net)
  • In apoptosis, phosphatidyl serine is transferred to the outer leaflet of the plasma membrane. (drugbank.com)
  • Phosphatidyl serine (PS) is a phospholipid nutrient found in fish, green leafy vegetables, soybeans and rice, and is essential for the normal functioning of neuronal cell membranes and activates Protein kinase C (PKC) which has been shown to be involved in memory function. (drugbank.com)
  • Phosphatidyl serine is a nutrient used in some supplement products. (drugbank.com)
  • The systematic name of this enzyme class is CDP-diacylglycerol:L-serine 3-sn-phosphatidyltransferase. (wikipedia.org)
  • An enzyme that catalyzes the formation of phosphatidylserine and CMP from CDPdiglyceride plus serine. (nih.gov)
  • This enzyme participates in glycine, serine and threonine metabolism and glycerophospholipid metabolism. (wikipedia.org)
  • In enzymology, a CDP-diacylglycerol-serine O-phosphatidyltransferase (EC 2.7.8.8) is an enzyme that catalyzes the chemical reaction CDP-diacylglycerol + L-serine ⇌ {\displaystyle \rightleftharpoons } CMP + (3-sn-phosphatidyl)-L-serine Thus, the two substrates of this enzyme are CDP-diacylglycerol and L-serine, whereas its two products are CMP and (3-sn-phosphatidyl)-L-serine. (wikipedia.org)
  • The systematic name of this enzyme class is CDP-diacylglycerol:L-serine 3-sn-phosphatidyltransferase. (wikipedia.org)
  • Serine-threonine/tyrosine-protein kinase, catalytic domain [Interproscan]. (ntu.edu.sg)