Results 221 to 230 of about 25,845 (262)

Hydrolysis of phosphoenolpyruvate catalyzed by phosphoenolpyruvate carboxylase from Zea mays

Biochemistry, 1992
In addition to the normal carboxylation reaction, phosphoenolpyruvate carboxylase from Zea mays catalyzes a HCO3(-)-dependent hydrolysis of phosphoenolpyruvate to pyruvate and Pi. Two independent methods were used to establish this reaction. First, the formation of pyruvate was coupled to lactate dehydrogenase in assay solutions containing high ...
S L, Ausenhus, M H, O'Leary
openaire   +2 more sources

Nodule phosphoenolpyruvate carboxylase: a review

Physiologia Plantarum, 1988
Recent data concerning the fixation of CO2 and the functioning of phosphoenolpyruvate (PEP) carboxylase (EC 4.1.1.31) in legume, nodules are reviewed. The activites of N2 fixation (acctylene reduction) and PEP carboxylase are correlated Activities of PEP carboxylase are always higher in nodules than in roots.
Deroche, M.E., Carrayol, E.
openaire   +2 more sources

Phosphoenolpyruvate carboxylase from Acetobacter aceti

Archives of Microbiology, 1979
In Acetobacter aceti growing on pyruvate as the only source of carbon and energy, oxaloacetate (OAA) is produced by a phosphoenolpyruvate (PEP) carboxylase (EC 4.1.1.31). The enzyme was purified 122-fold and a molecular weight of about 380,000 was estimated by gel filtration.
J. -P. Schwitzgu�bel, L. Ettlinger
openaire   +1 more source

The unique phosphoenolpyruvate carboxylase kinase

Plant Physiology and Biochemistry, 2003
Abstract This paper deals with the contribution of P. Gadal’s group to the study of the phosphoenolpyruvate carboxylase protein kinase. It traces the important steps from the discovery up to the present time leading to characterize a new protein kinase which is specific for plants and displays original properties.
Cristina Echevarria, Jean Vidal
openaire   +1 more source

Sheep kidney phosphoenolpyruvate carboxylase purification and properties

Biochimica et Biophysica Acta (BBA) - Enzymology, 1972
Phosphoenolpyruvate carboxylase (GTP: oxaloacetate carboxy-lase (transphosphorylating), EC 4.1.1.32) has been purified and obtained in a homogeneous form from sheep kidney cortex mitochondria. The purification procedure involved extraction of the freeze-dried mitochondria, (NH4)2SO4 fractionation, Sephadex G-100 gel filtration and ion-exchange ...
R J, Barns, D B, Keech
openaire   +2 more sources

Phosphoenolpyruvate Carboxylase: An Enzymologist's View

Annual Review of Plant Physiology, 1982
INTRODUCTION . PREPARATION AND ASSAY OF PEP CARBOXYLASE .. Assay . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. .. . . . . . . . . . . . . .. .. .. . . . .. . . .. .. . . . .. . .. .. . .. . . .. . . . . . . . .. . . . . . . . . . . . . . . . . . . Assay Conditions . . . . . . . . . . . . . . . . . . .
openaire   +1 more source

Chapter 13 C4-Phosphoenolpyruvate Carboxylase

2010
Phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) is one of the enzymes indispensable for all variants of the C4 photosynthetic pathway. C4 photosynthesis evolved polyphyletically implying that the genes encoding the C4 PEPC originated several times independently from non-photosynthetic ancestral genes.
Udo Gowik, Peter Westhoff
openaire   +1 more source

Quantitative Immunochemistry of Plant Phosphoenolpyruvate Carboxylases

1986
Since its discovery (Bandurski and Greiner 1953) phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) has attracted increasing interest among plant scientists. The enzyme catalyses the reaction of CO3H− and phosphoenolpyruvate to produce oxaloacetate, immediately reduced to form malate; this latter can be oxidatively decarboxylated by NADP malic enzyme,
J. Brulfert, J. Vidal
openaire   +1 more source

Phosphoenolpyruvate carboxylase: three-dimensional structure and molecular mechanisms

Archives of Biochemistry and Biophysics, 2003
Phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31) catalyzes the irreversible carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate and Pi using Mg2+ or Mn2+ as a cofactor. PEPC plays a key role in photosynthesis by C4 and Crassulacean acid metabolism plants, in addition to its many anaplerotic functions.
Yasushi, Kai, Hiroyoshi, Matsumura, Katsura, Izui   +2 more
openaire   +2 more sources

[43] Phosphoenolpyruvate carboxylase from peanut cotyledons

1969
Publisher Summary The chapter discusses the properties and purification procedure of phosphoenolpyruvate carboxylase from peanut cotyledons. The purification procedure described is based on that of Maruyama et al. All the procedures are carried out at 4°.
M. Daniel Lane, H. Maruyama, R.L. Easterday   +2 more
openaire   +1 more source