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|
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 PCC , phosphoenolpyruvate carboxylase, pepc gene, cyanobacteria Created Date: 1/4/ AM. (E)Cyanophosphoenolpyruvate, a new inhibitor of phosphoenolpyruvate-dependent enzymes. Biochemistry , 24 (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
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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: