2 edition of Molecular characterization of phosphoenolpyruvate carboxylase in cyanobacteria. found in the catalog.
Molecular characterization of phosphoenolpyruvate carboxylase in cyanobacteria.
Irene Elizabeth Luinenburg
Written in English
|The Physical Object|
|Number of Pages||174|
58 J. Mex. Chem. Soc. , 56(1) Rodrigo Güémez-Toro et al. Allosteric Regulation of the Photosynthetic C4 Isoenzyme of Phosphoenolpyruvate Carboxylase: A Comparative Study Between Enzymes from Monocot and Dicot Plants1 Rodrigo Güémez-Toro, . At a molecular level, chronic exposition to fructose induce an upregulation of sterol regulatory element binding protein-1 (SREBP-1c) and the enzyme acetyl-coenzyme A carboxylase that can lead to increase of fat synthesis and hyperuricemia by high degradation of AMP and depletion of ATP content in the liver, all caused by the excessive synthesis of fructosephosphate, a consequence of the.
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Phosphoenolpyruvate carboxylase (PEPC, EC ) catalyzes a reaction that fixes HCO 3– on phosphoenolpyruvate (PEP) to form oxaloacetate (OAA) and inorganic phosphate in the presence of Mg 2+ (O’Leary ).Cited by: Molecular characterization of a phosphoenolpyruvate carboxylase from a thermophilic cyanobacterium, Synechococcus vulcanus with unusual allosteric properties.
Chen LM(1), Omiya T, Hata S, Izui K. Author information: (1)Laboratory of Plant Physiology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, by: Summary Phosphoenolpyruvate carboxylase (PEPC) is the second major carbon‐fixing enzyme in photoautotrophic organisms.
PEPC is required for the synthesis of amino acids of the glutamate and aspartate family by replenishing the TCA cycle. Abstract Phosphoenolpyruvate (PEP) carboxylase (EC ) was purified fold from the cyanobacterium Coccochloris peniocystis with a yield of 10%.
A single isozyme was found at all stages of purification, and activity of other beta-carboxylase enzymes was not detected. The apparent molecular weight of the native enzyme was ,Cited by: Gene, 45 () Eisevier GENE Molecular cloning of the phosphoenolpyruvate carboxylase gene of Anahaena variabilis (Recombinant DNA; cyanobacteria; photosynthesis; carbon assimilation; blue green algae) Tina R.
Harrington, Bernard R. Glick * and Nora W. Lern Department of Biology, University of Waterloo, Waterloo, Ontario, N2L 3G1 (Canada) Tel. () (Received Cited by: 9. Phosphoenolpyruvate (PEP) carboxylase (EC ) was purified fold from the cyanobacterium Coccochloris peniocystis with a yield of 10%.
A single isozyme was found at all stages of purification, and activity of other beta-carboxylase enzymes was not detected. The apparent molecular weight of the native enzyme wasAbstract. Although cyanobacteria are known to assimilate inorganic carbon by the C 3 photosynthetic pathway, they also fix large amounts of carbon in the light as C 4 acids (1).
These C 4 acids, primarily aspartate and malate, may represent as much as 20% of the total carbon fixed and have been shown to be the product of phosphoenolpyruvate (PEP) carboxylase [EC ] activity (1,2,3).Author: I.
Luinenburg, J. Coleman. Phosphoenolpyruvate carboxylase (PEPC) a cytosolic enzyme of higher plants is also found in bacteria and cyanobacteria. Genetic and biochemical investigations have indicated that there are several isoforms of PEPC belonging to C 3; C 3 /C 4 and C 4 groups but, the evolution of PEPC in cyanobacteria is not yet by: A requirement for phosphoenolpyruvate carboxylase in the cyanobacterium Synechococcus PCC As a first step in determining the role of this enzyme in cyanobacterial carbon metabolism we have attempted to generate PEPCase deficient mutants by insertional inactivation of the PEPCase gene (ppc) and recombination into the wild-type genome.
Phosphoenolpyruvate carboxylase (also known as PEP carboxylase, PEPCase, or PEPC; ECPDB ID: 3ZGE) is an enzyme in the family of carboxy-lyases found in plants and some bacteria that catalyzes the addition of bicarbonate (HCO 3 −) to phosphoenolpyruvate (PEP) to form the four-carbon compound oxaloacetate and inorganic phosphate.
PEP + HCO 3 − → oxaloacetate + PiBRENDA: BRENDA entry. Abstract Phosphoenolpyruvate (PEP) carboxylase (EC ) was purified fold from the cyanobacterium Coccochloris peniocystis with a yield of 10%.
A single isozyme. by the C 3 photosynthetic enzyme Ribulose bisphos- phate carboxylase/oxygenase (RuBisCO). At higher tem-peratures, due to increase in the ratio of O 2 to CO 2, RuBisCO loses speciﬁcity for.
The native PEPCs usually act as a homotetramer with a total molecular mass about kD and catalyze the formation of oxaloacetate (OAA) by irreversible carboxylation of phosphoenolpyruvate (PEP) in the presence of Mg 2+.
Usually, the OAA will be rapidly converted to malate by malate by: 6. phoenolpyruvate carboxylase gene GhPEPC2 is isolated from cotton (Gossypium hirsutum cv. zhongmian 35) by RACE-PCR. The cloned cDNA of GhPEPC2 is bp in length, and has an open reading frame of bp, encoding for putative amino acids with a calculated molecular mass of kD and pI of Phosphoenolpyruvate carboxykinase (PEPCK; EC.) catalyzes the reversible ATP- or GTP-dependent decarboxy- lation of oxaloacetate (OAA) to yield phosphoenolpyruvate (PEP).
is reaction uses the phosphate group from the nucleotide triphosphate and, as a result, produces CO2and the corresponding nucleoside diphosphate. Phosphoenolpyruvate carboxylase (PEPc) is a carbon dioxide fixing enzyme that in an irreversible manner and in the presence of Mg 2+, converts Author: Claudia Durall, P Sandesh Kanchugal, Maria Selmer, Peter Lindblad.
Phosphoenolpyruvate (PEP) carboxylase (EC ) was purified fold from the cyanobacterium Coccochloris peniocystis with a yield of 10%. A single isozyme was found at all stages of purification, and activity of other beta-carboxylase enzymes was not detected.
The apparent molecular weight of the native enzyme was ,Cited by: «hide 10 20 30 40 50 mnlavpafgl stnwsgngng snseeesvly qrlkmveelw ervlqsecgq 60 70 80 90 elvdlltelr lqgtheaits eiseevimgi tqriehleln dairaarafa lyfqlinive qhyeqneqqr nrweasqetn fyeqagneee mvppsrlgas teplpvgidq nelqasvgtf hwlmrelkrl nvppqhiqnl ldhldirlvi tahpteivrh tirrkqrrvd rilrkldqlq gsvtgrdwln twdaktaiaq.
Molecular Characterization and Phylogeny of Marine Cyanobacteria from Palk Bay Region of Tamil Nadu, India In silico Characterization and Homology Modeling of Cyanobacterial Phosphoenolpyruvate Carboxylase Enzymes with Computational Tools and Bioinformatics Servers.
Phosphorylation of Phosphoenolpyruvate Carboxylase Is Essential for Maximal and Sustained Dark CO 2 Fixation and Core Circadian Clock Operation in the Obligate Crassulacean Acid Metabolism Species Kalanchoë fedtschenkoiCC-BY Susanna F. Boxall, Louisa V. Dever, Jana Knerová,1 Peter D.
Gould, and James Hartwell2Cited by: In this study, we present a complex characterization of two narrow-leafed lupin gene families—glutamine synthetase (GS) and phosphoenolpyruvate carboxylase (PEPC). We combine a comparative analysis of gene structures and a synteny-based approach with phylogenetic reconstruction and reconciliation of the gene family and species history in.
The pepc gene, which encodes phosphoenolpyruvate carboxylase (PEPC), of the marine cyanobacterium Synechococcus PCCwas isolated and sequenced. PEPC is an anaplerotic enzyme, but it may also contribute to overall CO 2 fixation through β-carboxylation reactions.
A consensus sequence generated by aligning the pepc genes of Anabaena variabilis, Anacystis. Phosphoenolpyruvate carboxylase (PEPC) is an important enzyme for CO2 fixation and primary metabolism in photosynthetic organisms including cyanobacteria Cited by: 1 1 RESEARCH ARTICLE 2 3 Phosphorylation of Phosphoenolpyruvate Carboxylase is Essential for 4 Maximal and Sustained Dark CO 2 Fixation and Core Circadian Clock 5 Operation in the Obligate Crassulacean Acid Metabolism Species 6 Kalanchoë fedtschenkoi 7 8 Susanna F.
Boxall, Louisa V. Dever, Jana Kneřová1, Peter D. Gould, and James 9 Hartwell. Phosphoenolpyruvate carboxylase (PEPC, EC ) catalyzes the β-carboxylation of phosphoenolpyruvate in the presence of Mg 2+ to yield oxaloacetate and inorganic phosphate (Chollet et al., ).In vivo, the active enzyme acts as a homotetramer composed by subunits of to kD (O'Leary, ).This enzyme is widely distributed in plants, algae, and bacteria, but is absent.
Molecular characterization, enzyme properties and transcriptional regulation of phosphoenolpyruvate carboxykinase and pyruvate kinase in a ruminal bacterium, Selenomonas ruminantiumThe GenBank accession numbers for the S.
ruminantium pck and pyk sequences reported in this paper are AB and AB, by: Phosphoenolpyruvate carboxylase (PEPC) is a key enzyme in the supply of carbon skeletons for the assimilation of nitrogen by green algae.
Two PEPC isoforms with respective native molecular masses of (PEPC1) and (PEPC2) kDa have been purified from Chlamydomonas reinhardtii CW cc (Chlorophyceae).Cited by: Isolation and Sequence of the Phosphoenolpyruvate Carboxylase Gene of the Marine Cyanobacterium Synechococcus PCC Author: A.A.
Smith, M.W. Coomes and T.E. Smith Subject: Journal of Biological Sciences Keywords: Synechococcus PCCphosphoenolpyruvate carboxylase, pepc gene, cyanobacteria Created Date: 1/4/ AM. (E)Cyanophosphoenolpyruvate, a new inhibitor of phosphoenolpyruvate-dependent enzymes.
Biochemistry24 (26), DOI: /bia Yasushi Kai, Hiroyoshi Matsumura, Katsura Izui. Phosphoenolpyruvate carboxylase: three-dimensional structure and molecular Cited by: Abstract ATP-dependent phosphoenolpyruvate carboxykinase (PEPCK) is a key catabolic enzyme found in various species of bacteria, plants, and yeast.
PEPCK may play a role in carbon fixation in aquatic ecosystems consisting of photosynthetic by: 4. Phosphoenolpyruvate carboxykinase (PEPCK) is an enzyme in the lyase family used in the metabolic pathway of gluconeogenesis. It converts oxaloacetate into phosphoenolpyruvate and carbon dioxide.
It is found in two forms, cytosolic and mitochondrialInterPro: IPR Ernst K, Westhoff P. The phosphoenolpyruvate carboxylase (ppc) gene family of Flaveria trinervia (C4) and F. pringlei (C3): molecular characterization and expression analysis of the ppcB and ppcC genes.
Plant Mol. Biol. Phosphoenolpyruvate carboxylase (PEPC) catalyzes the fixation of carbon dioxide with phosphoenolpyruvate to produce oxaloacetate and inorganic phosphate. PEPC is found in most plants and bacteria. It has been reviewed by Utter and Kolenbrander (). Characteristics of PEPC from E.
coli: Molecular weight: Approximately(Smith ). Phosphoenolpyruvate carboxylase has been purified to homogeneity from maize (Zea mays L. var. Golden Cross Bantam T51) leaves. The ratio of specific activities in crude extracts and the purified enzyme suggests that the enzyme is a major soluble protein in the tissue.
The enzyme has a sedimentation coefficient (s 20, w) of S and a molecular weight, determined by sedimentation Cited by: Molecular biology, particularly molecular genetics, is among the newest and most powerful approach in modern photosynthesis research.
Development of molecular biology techniques has provided new methods to solve old problems in many biological disciplines. Molecular biology has its greatestBrand: Springer Netherlands.
PEPC [PEP (phosphoenolpyruvate) carboxylase] (EC ) is an important enzyme situated at a crucial branch point in plant carbohydrate metabolism.
It catalyses the irreversible β-carboxylation of PEP in the presence of HCO 3 − to yield OAA (oxaloacetate) and P i using Mg2 + as a cofactor.
TheFile Size: 1MB. Phosphoenolpyruvate carboxylase (PEPC) catalyzes the addition of bicarbonate to phosphoenolpyruvate (PEP) to form the four-carbon compound oxaloacetate and inorganic phosphate.
In CAM and C 4 plants, PEPC catalyzes the photosynthetic assimilation of CO2 into an organic acid. PEPC is activated by glucosephosphate and is inhibited by malate. Identification of SWEET transporters paved the way toward the molecular characterization of sugar efflux in plants.
In this study, LjSWEET3, a clade I type SWEET transporter, was identified as being the only gene preferentially expressed in nodules in a model legume, L. by: III Reaction centers; herbicide resistance.- 14 Reaction centers from three herbicide-resistant mutants of Rhodobacter sphaeroides sequence analysis and preliminary characterization 15 Molecular genetics of herbicide resistance in cyanobacteria 16 Genetic analysis of two new mutations resulting in herbicide resistance in the.
Molecular characterization of a phosphoenolpyruvate carboxylase from a thermophilic cyanobacterium, Synechococcus vulcanus with unusual allosteric properties.
Plant Cell Physiol – Chisti Y (). Characterization of Pyruvate Carboxylase from Methanobacterium thermoautotrophicum. 1. Write the balanced reaction catalyzed by pyruvate carboxylase (PYC), including structures and cofactors.
2. Write the balanced reaction catalyzed by phosphoenolpyruvate carboxylase (PPC), including structures. 3.Phosphoenolpyruvate carboxylase (PEPC) is a tightly regulated enzyme of vascular plants and green algae, situated at a crucial branch point in primary metabolism that catalyzes the irreversible β-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA) and inorganic phosphate (Pi) (O’Leary et al.
b).ENZYMOLOGY AND PHYSIOLOGY OF A NEW TYPE OF PHOSPHOENOLPYRUVATE CARBOXYLASE AND THE DEVELOPMENT OF A PYRUVATE CARBOXYLASE EXPRESSION SYSTEM Jessica Leigh Kraszewski.