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3 edition of Phosphoenol pyruvate carboxylase activity in chlorophyll deficient barley mutants. found in the catalog.

Phosphoenol pyruvate carboxylase activity in chlorophyll deficient barley mutants.

Stephen Robert Muench

Phosphoenol pyruvate carboxylase activity in chlorophyll deficient barley mutants.

by Stephen Robert Muench

  • 73 Want to read
  • 30 Currently reading

Published .
Written in English

    Subjects:
  • Chlorophyll,
  • Barley

  • The Physical Object
    Paginationviii, 31 l.
    Number of Pages31
    ID Numbers
    Open LibraryOL16744126M

    Doncaster HD, Leegood RC. Regulation of phosphoenolpyruvate carboxylase activity in maize leaves. Plant Physiol. (). Dong DF, Peng XX, Yan XL. Organic acid exudation induced by phosphorus deficiency and/or aluminium toxicity in two contrasting soybean genotypes. Physiol. Plant. ().   Phospho enol pyruvate carboxylase (PPC; EC ) catalyzes primary nocturnal CO2 fixation in Crassulacean acid metabolism (CAM) species. CAM PPC is regulated posttranslationally by a circadian clock-controlled protein kinase called phospho enol pyruvate carboxylase kinase (PPCK). PPCK phosphorylates PPC during the dark period, reducing its sensitivity to feedback Cited by:

    Early responses to Fe-deficiency distinguish Sorghum bicolor genotypes with contrasting alkalinity tolerance Article (PDF Available) in Environmental and Experimental Botany June with. Lillo C, Smith L H, Nimmo H G and Wilkins M B () Regulation of nitrate reductase and phosphoenol pyruvate carboxylase activities in barley leaf protoplasts. Planta, .

    Search results for Phosphoenol-pyruvate at Sigma-Aldrich. Compare Products: Select up to 4 products. *Please select more than one item to compare. 3. In glycolysis, the formation of pyruvate and ATP by pyruvate kinase is irreversible. This step is bypassed by two reactions in gluconeogenesis: (1) the formation of oxaloacetate from pyruvate and CO2 by pyruvate carboxylase and (2) the formation of phosphoenolpyruvate from oxaloacetate and GTP by phosphoenolpyruvate carboxykinase.


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Phosphoenol pyruvate carboxylase activity in chlorophyll deficient barley mutants by Stephen Robert Muench Download PDF EPUB FB2

Pyruvate carboxylase activity was present in all insect flight muscles that were investigated: in homogenates of bumble-bee flight muscle the activity was inhibited by ADP and activated by acetyl-CoA, and it was distributed mainly in the mitochondrial fraction.

This is the first demonstration of pyruvate carboxylase activity in by:   In vivo phosphoenol pyruvate carboxylase activity is controlled by CO 2 and O 2 mole fractions and represents a major flux at high photorespiration rates Cyril Abadie.

Research School of Biology, Australian National University, Canberra, ACT, Australia. Search for Cited by: 7. The patient with hepatic, renal, and cerebral pyruvate carboxylase deficiency had no detectable activity ( mU/mg protein) in his leukocytes and mU/mg protein in his by:   Phospho enol pyruvate carboxylase ([PEPC][1]) is a crucial enzyme that catalyzes an irreversible primary metabolic reaction in plants.

Previous studies have used transgenic plants expressing ectopic [PEPC][1] forms with diminished feedback inhibition to examine the role of [PEPC][1] in carbon and nitrogen metabolism.

To date, the in vivo role of [PEPC][1] in carbon and nitrogen metabolism has Cited by: Phosphoenolpyruvate carboxylase (PEP carboxylase, EC ) activity was demonstrated in a range of holo and hemiparasitic phanerogams.

Lathraea clandestina was used as Cited by: 8. carboxylation, mediated by the enzyme phosphoenol-pyruvate carboxylase (PEPC), permits a wide spec-trum of CO 2 exchange responses over the day/night cycle. Plasticity in the expression of CAM is central for optimizing carbon gain in a range of potentially Cited by: Ferrario-Mery, S., Hodges, M., Hirel, B.

and Foyer, C. Photorespiration-dependent increases in phosphoenol pyruvate carboxylase, isocitrate dehydrogenase and glutamate dehydrogenase in transformed tobacco plants deficient in ferredoxin-dependent glutamine-alpha-ketoglutarate by: Role of Pyruvate Carboxylase, Phosphoenolpyruvate Carboxykinase, and Malic Enzyme during Growth marily through the apparently constitutive enzyme pyruvate carboxylase, which is strongly activated by acetyl-CoA.

The sporulation deficiency of malic dehydrogenase mutants is typical for mutants of the citric acid cycle (4, 5, 14). During gluconeogenesis, pyruvate carboxylase is involved in the synthesis of phosphoenolpyruvate (PEP) from pyruvate.

Pyruvate is first converted by pyruvate carboxylase to oxaloacetate (OAA) in the mitochondrion requiring hydrolysis of one molecule of : BRENDA entry.

And primary carbon dioxide acceptor in C4 plant is phosphoenol pyruvic acid,it contains 3 carbon atoms. in C3 plants ribulose 1,5 bisphosphate (RUBP) is the primary CO2 acceptor. It is a 5 carbon compound. In C4 plants phospho enol pyruvate (PEP) is primary CO2 acceptor.

Pyruvate carboxylase (PC; EC ), a member of the biotin-dependent enzyme family, catalyses the ATP-dependent carboxylation of pyruvate to oxaloacetate. PC has been found in a wide variety of prokaryotes and by: Pyruvate carboxylase [EC ] is a member of the family of biotin-dependent carboxylases and is found widely among eukaryotic tissues and in many prokaryotic species.

It catalyses the ATP-dependent carboxylation of pyruvate to form oxaloacetate which may be utilised in the synthesis of glucose, fat, some amino acids or their derivatives and several neurotransmitters.

Pyruvate carboxylase oligomers arrange in tetramers and covalently attached biotins mediate the transfer of carboxyl groups between distant active sites. In this chapter, some of the recent findings on pyruvate carboxylase functioning are presented, with special focus on the structural studies of the full length by: 1.

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 + : BRENDA entry.

Bakrim N, Nhiri M, Pierre J-N, Vidal J () Metabolite control of Sorghum C 4 phosphoenol-pyruvate carboxylase catalytic activity and phosphorylation state.

Cited by: 2. C i was in PEP carboxylase activity at a C i of 30, 60 or ml l−1 CO 2, between and ml l−1 CO 2. Each data point is the mean of three measured at saturating PFD. Question: Phosphoenol Pyruvate Is A Very Energetic Molecule, In The Sense That It Can Directly Phosphorylate ADP To ATP.

This Energy Is Due To The Trapping The Molecule In The Unstable Form. ATP, Enol B. Phosphate, Enol C. Pyruvate, Coenzyme A D. ATP, Diphosphate E. Phosphate, Glycerophosphate Please Explain. Pyruvate carboxylase deficiency is an inherited disorder that causes lactic acid and other potentially toxic compounds to accumulate in the blood.

High levels of these substances can damage the body's organs and tissues, particularly in the nervous system. Researchers have identified at least three types of pyruvate carboxylase deficiency, which are distinguished by the severity of their. Distribution of pyruvate carboxylase and phosphoenol‐pyruvate carboxikinase in human liver.

Wieland. Institute of Clinical Chemistry, Schwabing City Hospital, and Diabetes Research Unit, Munich, Germany. Search for more papers by this author. by:   Abstract. Heterozygous mutants of Amaranthus edulis deficient in PEP carboxylase (PEPC) have been used to study the control of photosynthetic carbon assimilation.

A reduction in PEPC activity led to a decrease in the initial slope of the relationship between the CO 2 assimilation rate and the intercellular CO 2 concentration and to a decrease in photosynthesis at high light intensities Cited by:.

The activities of two liver gluconeogenic enzymes, pyruvate carboxylase (PC) and phosphoenolpyruvate carboxykinase (PEPCK) as well as plasma glucose were measured in manganese-sufficient and manganese-deficient rats from birth to 30 d of age. Initial (d 0) PC activity Cited by: Advances in Photosynthesis Research Proceedings of the VIth International Congress on Photosynthesis, Brussels, Belgium, August 1–6, Volume 3 Monoclonal Antibodies to Chlorophyll α-protein 1 in Barley.

Activation or Inhibition of Phosphoenol Pyruvate Carboxylase .Sigma-Aldrich offers a number of Phosphoenol-pyruvate products. View information & documentation regarding Phosphoenol-pyruvate, including CAS, MSDS & more.