PhosphoEnol Pyruvate Carboxy Kinase (PEPCK) catalyzes the GTP dependent conversion of oxaloacetate to CO2 and phospo enol pyruvate, which is subsequently converted to glyceraldehyde-3-phosphate, which then serves as precursor for both gluconeogenesis and/or glyceroneogenesis. Using the mouse gene for the cytoplasmic form of PEPCK-Cmus linked to the skeletal muscle actin promoter, PEPCK-Cmus transgenic mice (TG) were engineered on an SJL/B6 background. The PEPCK-Cmus transgenic mice bear 4 allelic copies of PEPCK; they show a nine-fold overexpression of PEPCK in skeletal muscle associated with an increase in muscle glyceroneogenesis and a 4 fold greater concentration of triglycerides per gram muscle compared with controls. The PEPCK-Cmus TG mice have a remarkable behavioral phenotype of significantly increased and spontaneous exercise, evident from 10 days of age and continuing throughout their extended lifespan. In their home cages, the TG mice show more spontaneous activity, including rearing ...
What is the subunit composition? Larsen, T. M., L. T. Laughlin, H. M. Holden, L. Rayment, G. H. Reed. 1994. Structure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate. Biochemistry 33:6301-6309.. ...
1A5U: Structure of the bis(Mg2+)-ATP-oxalate complex of the rabbit muscle pyruvate kinase at 2.1 A resolution: ATP binding over a barrel.
The phosphoenolpyruvate (PEP)-dependent phosphotransferase system (PTS) is a major mechanism used by bacteria for uptake of carbohydrates, particularly hexoses, hexitols, and disaccharides, where the source of energy is from PEP. The PTS consists of two general components, enzyme I (EI) and histidine phosphocarrier protein (HPr), and of membrane-bound sugar specific permeases (enzymes II). Each enzyme II (EII) complex consists of one or two hydrophobic integral membrane domains (domains C and D) and two hydrophilic domains (domains A and B). EII complexes may exist as distinct proteins or as a single multidomain protein. The PTS catalyzes the uptake of carbohydrates and their conversion into their respective phosphoesters during transport. There are four successive phosphoryl transfers in the PTS. Initial autophosphorylation of EI, using PEP as a substrate, is followed by transfer of the phosphoryl group from EI to HPr. EIIA catalyzes the self-phosphoryl transfer from HPr after which the ...
The phosphoenolpyruvate (PEP)-dependent phosphotransferase system (PTS) is a major mechanism used by bacteria for uptake of carbohydrates, particularly hexoses, hexitols, and disaccharides, where the source of energy is from PEP. The PTS consists of two general components, enzyme I (EI) and histidine phosphocarrier protein (HPr), and of membrane-bound sugar specific permeases (enzymes II). Each enzyme II (EII) complex consists of one or two hydrophobic integral membrane domains (domains C and D) and two hydrophilic domains (domains A and B). EII complexes may exist as distinct proteins or as a single multidomain protein. The PTS catalyzes the uptake of carbohydrates and their conversion into their respective phosphoesters during transport. There are four successive phosphoryl transfers in the PTS. Initial autophosphorylation of EI, using PEP as a substrate, is followed by transfer of the phosphoryl group from EI to HPr. EIIA catalyzes the self-phosphoryl transfer from HPr after which the ...
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This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found o
Looking for online definition of PEP carboxylase in the Medical Dictionary? PEP carboxylase explanation free. What is PEP carboxylase? Meaning of PEP carboxylase medical term. What does PEP carboxylase mean?
Shop Probable pyruvate, phosphate dikinase regulatory protein ELISA Kit, Recombinant Protein and Probable pyruvate, phosphate dikinase regulatory protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
TABLE-US-00003 TABLE 3 PFAM Results for Amino Acid Sequences Amino Acid SEQ ID Range NO: ORF Domain Start, Stop Family PFAM Accession No. E-value 3 877 PTS_IIA 16, 111 PTS system, Lactose/Cellobiose specific IIA PF02255 8.20E-40 subunit 5 609 PTS_EIIA_1 30, 134 phosphoenolpyruvate-dependent sugar PF00358 6.00E-55 phosphotransferase system, EIIA 1 7 1479 PRD 76, 171; PRD domain PF00874 9.90E-52 181, 282 7 1479 CAT_RBD 6, 67 CAT RNA binding domain PF03123 1.10E-16 9 1574 Glyco_hydro_1 4, 471 Glycosyl hydrolase family 1 PF00232 2.90E-133 11 1707 PTS_EIIA_1 491, 595 phosphoenolpyruvate-dependent sugar PF00358 6.10E-53 phosphotransferase system, EIIA 1 11 1707 PTS_EIIC 105, 387 Phosphotransferase system, EIIC PF02378 3.10E-33 11 1707 PTS_EIIB 7, 41 phosphotransferase system, EIIB PF00367 8.50E-19 13 725 PTS_EIIA_1 528, 632 phosphoenolpyruvate-dependent sugar PF00358 4.10E-60 phosphotransferase system, EIIA 1 13 725 PTS_EIIC 122, 419 Phosphotransferase system, EIIC PF02378 3.80E-35 13 725 PTS_EIIB 21, ...
The phosphoenolpyruvate: sugar phosphotransferase system (PTS) is responsible for the uptake and concomitant phosphorylation of many sugars in several species of bacteria. The first step of the PTS involves the phosphorylation of histidine containing phosphocarrier protein (HPr) by enzyme I (E.C. 2.7.3.9), with phosphoenolpyruvate (PEP) serving as the phosphoryl donor. Enzyme I has logically been viewed as a potential target for regulation of the PTS. This thesis presents important information regarding the structure and function of enzyme I of Escherichia coli and Salmonella typhimurium. Fluorescence polarization analysis, although incomplete, showed that the interaction of HPr with enzyme I and with enzyme IIA glc are of low affinity, with a Kd of roughly 10-100 [mu]M. An enzyme I binding site on HPr was determined by a kinetic assay, using site-directed mutants of HPr as substrates for enzyme I. This site of interaction agreed very well with that found in the NMR solution structure of the ...
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The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) is a major carbohydrate transport system in bacteria. The PTS catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The general mechanism of the PTS is the following: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred to enzyme-I (EI) of PTS which in turn transfers it to a phosphoryl carrier protein (HPr). Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease which consists of at least three structurally distinct domains (IIA, IIB, and IIC) which can either be fused together in a single polypeptide chain or exist as two or three interactive chains, formerly called enzymes II (EII) and III (EIII ...
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) is a major carbohydrate transport system in bacteria. The PTS catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The general mechanism of the PTS is the following: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred to enzyme-I (EI) of PTS which in turn transfers it to a phosphoryl carrier protein (HPr). Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease which consists of at least three structurally distinct domains (IIA, IIB, and IIC) which can either be fused together in a single polypeptide chain or exist as two or three interactive chains, formerly called enzymes II (EII) and III (EIII ...
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CsiE has two central PRD domains with histidine residues predicted to be phosphorylated by the sugar phosphotransferase system (PTS) in response to the availability of carbon source. The PRD domains of BglG phosphorylated by the sugar phosphotransferase system (PTS) in response to the availability of carbon source ...
Pyruvate kinase is the enzyme that catalyzes the final step of glycolysis. It catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to adenosine diphosphate (ADP), yielding one molecule of pyruvate and one molecule of ATP. Pyruvate kinase is present in four distinct, tissue-specific isozymes in animals, each consisting of particular kinetic properties necessary to accommodate the variations in metabolic requirements of diverse tissues. There are four isozymes of pyruvate kinase in vertebrates: L (liver), R (erythrocytes), M1(muscles, hearts and brain) and M2 (only form detectable in early fetal tissue and present in most adult tissues). R and L isozymes differ from M1 and M2 in that they are both exclusively allosterically and reversibly regulated. From a kinetic standpoint, the R and L isozymes of pyruvate kinase have two key conformation states; one with a high substrate affinity and one with a low substrate affinity. The R-state, characterized by high substrate affinity, ...
TY - JOUR. T1 - Crystal structure of a phosphorylation-coupled saccharide transporter. AU - Cao, Yu. AU - Jin, Xiangshu. AU - Levin, Elena J.. AU - Huang, Hua. AU - Zong, Yinong. AU - Quick, Matthias. AU - Weng, Jun. AU - Pan, Yaping. AU - Love, James. AU - Punta, Marco. AU - Rost, Burkhard. AU - Hendrickson, Wayne A.. AU - Javitch, Jonathan A.. AU - Rajashankar, Kanagalaghatta R.. AU - Zhou, Ming. PY - 2011/5/5. Y1 - 2011/5/5. N2 - Saccharides have a central role in the nutrition of all living organisms. Whereas several saccharide uptake systems are shared between the different phylogenetic kingdoms, the phosphoenolpyruvate-dependent phosphotransferase system exists almost exclusively in bacteria. This multi-component system includes an integral membrane protein EIIC that transports saccharides and assists in their phosphorylation. Here we present the crystal structure of an EIIC from Bacillus cereus that transports diacetylchitobiose. The EIIC is a homodimer, with an expansive interface formed ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
tr:H6RQV8_BLASD] ppc; Phosphoenolpyruvate carboxylase, Carbon dioxide fixing enzyme; K01595 phosphoenolpyruvate carboxylase [EC:4.1.1.31] ...
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Os01g0110700; Similar to Phosphoenolpyruvate carboxylase (EC 4.1.1.31).; K01595 phosphoenolpyruvate carboxylase [EC:4.1.1.31] ...
Phosphoenolpyruvate (2-phosphoenolpyruvate, PEP) is the ester derived from the enol of pyruvate and phosphate. It exists as an anion. PEP is an important intermediate in biochemistry. It has the highest-energy phosphate bond found (−61.9 kJ/mol) in organisms, and is involved in glycolysis and gluconeogenesis. In plants, it is also involved in the biosynthesis of various aromatic compounds, and in carbon fixation; in bacteria, it is also used as the source of energy for the phosphotransferase system.[1][2] ...
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The structural gene (mtlA) of the Escherichia coli phosphoenolpyruvate-dependent mannitol-transport protein (EIImtl) and its upstream promoter region (Pmtl) were subcloned approximately 150 base pairs downstream of a lambda PR promoter on a multicopy mutagenesis/expression vector and used to transform a mutant (MtlA-) E. coli strain. Induction at 42 degrees C led to 50 to 100-fold overproduction of EIImtl (5-10 mg/g of cell wet weight) relative to mannitol-induced levels in a wild-type (Mtl+) strain. Most of the overproduced protein was sequestered as an inactive form in inclusion bodies and cytoplasmic membranous structures. The protein could be extracted in an active form by rupturing the cells with lysozyme and sonication or with a passage through a French pressure cell and incubating the inclusion bodies and membranous structures with detergent (Lubrol PX or deoxycholate) in the presence of Q or S Sepharose ion-exchange resin for several hours. This procedure resulted in a 20- to 25-fold ...
... Not to be confused with Phosphoenolpyruvate carboxylase, PEPC Phosphoenolpyruvate carboxykinase is an enzyme used in the
Lactobacillus curvatus has a glucose transport system homologous to the mannose family of phosphoenolpyruvate-dependent phosphotransferase systems
Mutants of Escherichia coli K-12 defective in enzyme I or Hpr, the two common components of the phosphoenolpyruvate-dependent phosphotransferase system, were isolated by a simple, direct method. The ptsI locus, the structural gene for enzyme I, and the ptsH locus, the site of mutations leading to loss of Hpr activity, are adjacent genes and could be part of a single operon. These two genes lie between the purC and supN markers in the order: strA... guaB-purC-ptsI-ptsH-supN-dsdA... his.
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Biochemistry, Metabolism:, Hereditary Factors:, Genes: Sdr-1, Strains: A(CAL-A) (A/J), AKR, BALB/C, CBA, C3H/HE, C57BL/6, C57BR/CD, DBA, RF (W), SJL. ...
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Enolases are enzymes which catalyze the conversion of 2-phosphoglycerate to phosphoenolpyruvate in the glycolytic pathway, and also the reverse…
1AQF: Ligand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution.
Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Citation: N/A Interpretive Summary: Technical Abstract: Selenomonas ruminantium is one of the more prominent and functionally diverse bacteria present in the rumen and can survive under a wide range of nutritional fluctuations. Selenomonas is not a degrader of complex polysaccharides, but is important in the utilization of soluble carbohydrates released from initial hydrolysis by other ruminal bacteria. Selenomonads have multiple carbon flow routes for carbohydrate catabolism and ATP generation, and subspecies differ in their ability to use lactate. Some soluble carbohydrates (glucose, sucrose) appear to be transported via the phosphoenolpyruvate phosphotransferase system, while arabinose and xylose are transported by proton symport. High cell yields and the presence of electron transport components in Selenomonas strains has been documented repeatedly and this may partially account for the energy partitioning observed between energy consumed for growth and maintenance functions. Most strains ...
Paulus JK, Förster K, Groth G. Direct and selective small-molecule inhibition of photosynthetic PEP carboxylase: New approach to combat C4 weeds in arable crops FEBS Letters,2014 Jun 5, 588(12):2101-6. Schlieper D, Förster K, Paulus JK, Groth G. Resolving the activation site of positive regulators in plant phosphoenolpyruvate carboxylase Molecular Plant, 2014 Feb, 7(2):437-40. Paulus JK, Niehus C, Groth G. Evolution of C4 phosphoenolpyruvate carboxylase: enhanced feedback inhibitor tolerance is determined by a single residue Molecular Plant, 2013 Nov, 6(6):1996-9. Paulus JK, Schlieper D, Groth G. Greater efficiency of photosynthetic carbon fixation due to single amino-acid substitution. Nature Communication, 2013, 4:1518 ...
Phosphoenolpyruvate (PEP) plays an essential role in plant metabolism. In catabolic direction, it delivers ATP and pyruvate by the action of pyruvate kinase, which can be fed into mitochondrial respiration. PEP and pyruvate also represent essential precursors for anabolism i.e. PEP is the precursor for the synthesis of aromatic amino acids, secondary plant products and pyruvate is important for the production of fatty acids, branched-chain amino acids or isoprenoids via the mevalonate-independent way. These pathways are exclusively localized to the plastid stroma. PEP may be imported into the plastids via a PEP/phosphate translocator (PPT) of the inner envelope membrane or it may also be generated inside the stroma by complete plastid glycolysis starting from hexose phosphates. Glycolysis as the main route for PEP production involves the enzymatic sequence of 3-phosphoglycerate to PEP conversion catalyzed by phosphoglyceromutase (PGyM) and enolase (ENO). However, biochemical studies indicate ...
The objective of the present work consisted on determining the effects of PTS and Pyk isozymes inactivation on cell physiology, metabolic flux distribution and PEP availability for aromatics biosynthesis. The inactivation of PTS in E. coli abolishes PEP-dependent glucose transport; therefore PYR production from PEP is dependent only on Pyk isozyme activities. In this study, by inactivating each Pyk isozyme in a PTS- glc+ background, strains were generated where the PEP to PYR reaction was dependent only on PykA or PykF activity. These strains were characterized by flux analysis, thus providing the first quantitative description of the metabolic consequences of the sequential elimination of activities catalyzing the PEP to PYR reaction.. The inactivation of PTS in E. coli causes a strong reduction in qGlc and μ, therefore, such mutant strains display a PTS- glc- phenotype. To improve qGlc and μ, strain VH33 has a chromosomal modification that increases its capacity for non PTS-dependent glucose ...
Saccharides have a central role in the nutrition of all living organisms. Whereas several saccharide uptake systems are shared between the different phylogenetic kingdoms, the phosphoenolpyruvate-dependent phosphotransferase system exists almost exclusively in bacteria. This multi-component system includes an integral membrane protein EIIC that transports saccharides and assists in their phosphorylation. Here we present the crystal structure of an EIIC from Bacillus cereus that transports diacetylchitobiose. The EIIC is a homodimer, with an expansive interface formed between the amino-terminal halves of the two protomers. The carboxy-terminal half of each protomer has a large binding pocket that contains a diacetylchitobiose, which is occluded from both sides of the membrane with its site of phosphorylation near the conserved His250 and Glu334 residues. The structure shows the architecture of this important class of transporters, identifies the determinants of substrate binding and ...
Different pyruvate kinase isoforms are expressed in a tissue-specific manner, with pyruvate kinase M2 (PKM2) suggested to be the predominant isoform in proliferating cells and cancer cells. Due to differential regulation of enzymatic activities, PKM2 but not PKM1 has been thought to favor cell proliferation. However, the role of PKM2 in tumorigenesis has been recently challenged. Here we report that increased glucose catabolism through glycolysis and increased pyruvate kinase activity in c-MYC-driven liver tumors are associated with increased expression of both PKM1 and PKM2 isoforms and decreased expression of the liver-specific isoform of pyruvate kinase, PKL. Depletion of PKM2 at the time of c-MYC over-expression in murine livers did not affect c-MYC induced tumorigenesis and resulted in liver tumor formation with decreased pyruvate kinase activity and decreased catabolism of glucose into alanine and the Krebs cycle. An increased PKM1/PKM2 ratio by ectopic PKM1 expression further decreased ...
How is R-type pyruvate kinase abbreviated? R-PK stands for R-type pyruvate kinase. R-PK is defined as R-type pyruvate kinase rarely.
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Requires Mg2+. ATP appears to be the only phosphate donor. No activity could be detected using GTP, UTP, phosphoenolpyruvate or diphosphate. The protein phosphorylates gl
Read "Cold Inactivation of Phosphoenolpyruvate Carboxylase and Pyruvate Orthophosphate Dikinase from the C4 Perennial Plant Atriplex halimus, Russian Journal of Plant Physiology" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
TY - JOUR. T1 - GntR-Type Transcriptional Regulator pckr Negatively Regulates the Expression of Phosphoenolpyruvate Carboxykinase in Corynebacterium glutamicum. AU - Hyeon, Jeong Eun. AU - Kang, Dae Hee. AU - Kim, Young In. AU - You, Seung Kyou. AU - Han, Sung Ok. PY - 2012/5/1. Y1 - 2012/5/1. N2 - The pck (cg3169) gene of Corynebacterium glutamicum encodes a phosphoenolpyruvate carboxykinase (PEPCK). Here, a candidate transcriptional regulator that binds to the promoter region of pck was detected using a DNA affinity purification approach. An isolated protein was identified to be PckR (Cg0196), a GntR family transcriptional regulator which consists of 253 amino acids with a mass of 27 kDa as measured by peptide mass fingerprinting. The results of electrophoretic mobility shift assays verified that PckR specifically binds to the pck promoter. The putative regulator binding region extended from position-44 to-27 (an 18-bp sequence) relative to the transcriptional start point of the pck gene. We ...
Approximately a third of the world population relies on rice every day; however, increases rice yields are not increasing to match the predicted increase in world population. Engineering the C4 photosynthetic carbon dioxide concentrating mechanism in rice may reduce inefficiencies in rice and increase yield. C4 photosynthesis uses the enzyme phosphoenolpyruvate carboxylase (PEPC) to fix atmospheric carbon dioxide in a four carbon acid which is shuttled to a separate compartment where the carbon dioxide is released and concentrated around the key enzyme of the Calvin-Benson cycle. Plants that have evolved the C4 cycle co-opted PEPC from a background role. The expression patterns and kinetic properties of PEPC are adapted to the demands of carbon fixation. The changes in gene expression have been studied previously through high-throughput sequencing techniques but the biochemical changes remain largely unexplored. Understanding how PEPC adapted is a key part of engineering C4 photosynthesis. In ...
Enolase is the eighth enzyme in the glycolytic pathway, a reaction that generates ATP from phosphoenol pyruvate in cytosolic compartments. Enolase is essential, especially for organisms devoid of the Krebs cycle that depend solely on glycolysis for energy. Interestingly, enolase appears to serve a separate function in some organisms, in that it is also exported to the cell surface via a poorly understood mechanism. In these organisms, surface enolase assists in the invasion of their host cells by binding plasminogen, an abundant plasma protease precursor. Binding is mediated by the interaction between a lysine motif of enolase with Kringle domains of plasminogen. The bound plasminogen is then cleaved by specific proteases to generate active plasmin. Plasmin is a potent serine protease that is thought to function in the degradation of the extracellular matrix surrounding the targeted host cell, thereby facilitating pathogen invasion. Recent work revealed that the malaria parasite Plasmodium ...
Sigma-Aldrich offers abstracts and full-text articles by [Katie J Dalziel, Brendan OLeary, Carolyne Brikis, Srinath K Rao, Yi-Min She, Terry Cyr, William C Plaxton].
SWISS-MODEL Repository entry for A0A070FAT1 (A0A070FAT1_ECOLX), Phosphoenolpyruvate carboxylase. Escherichia coli O128:H2 str 2011C-3317