Results 11 to 20 of about 118,012 (240)

Binuclear Complexes Containing a Methylnickel Moiety: Relevance to Organonickel Intermediates in Acetyl Coenzyme A Synthase Catalysis

open access: yes, 2016
Binuclear Complexes Containing a Methylnickel Moiety: Relevance to Organonickel Intermediates in Acetyl Coenzyme A Synthase ...
Krishnan Rangan (2389432)   +4 more
core   +4 more sources

The dynamic organization of fungal acetyl-CoA carboxylase [PDF]

open access: yes, 2016
Acetyl-CoA carboxylases (ACCs) catalyse the committed step in fatty-acid biosynthesis: the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. They are important regulatory hubs for metabolic control and relevant drug targets for the treatment of ...
Hagmann, Anna   +4 more
core   +1 more source

Acetyl-coenzyme A [PDF]

open access: yesAutophagy, 2014
As the major lysosomal degradation pathway, autophagy represents the guardian of cellular homeostasis, removing damaged and potentially harmful material and replenishing energy reserves in conditions of starvation. Given its vast physiological importance, autophagy is crucially involved in the process of aging and associated pathologies.
Schroeder, S.   +15 more
openaire   +3 more sources

Acetyl Coenzyme A Carboxylase

open access: yesJournal of Biological Chemistry, 1974
Publisher Summary This chapter discusses the molecular properties of acetyl-CoA carboxylases from animal, bacterial, and plant cells. It also focuses on the regulation of catalytic activity. The mode of regulation of acetyl-CoA carboxylase reflects its physiological role in animal and bacterial cells.
Ras B. Guchhait   +2 more
openaire   +2 more sources

Characterization of Maize Acetyl-Coenzyme A Carboxylase [PDF]

open access: yesPlant Physiology, 1993
Maize (Zea mays L.) leaf acetyl-CoA carboxylase (ACCase) was purified about 500-fold by ammonium sulfate fractionation and gel filtration and blue Sepharose affinity and anion-exchange chromatography. Most ACCase activity (85%) recovered from the anion-exchange column was found in a highly purified fraction (specific activity 5.5 [mu]mol acid-stable ...
M. A., Egli   +4 more
openaire   +2 more sources

Regulation of Acetyl-Coenzyme A Carboxylase and Acetyl-Coenzyme A Synthetase in Spinach Chloroplasts

open access: yesZeitschrift für Naturforschung C, 1984
In analogy to chloroplast fatty acid synthesis from acetate the key enzymes of acetate fixation, acetyl-CoA synthetase and acetyl-CoA carboxylase, in rapidly Triton X-100 lysed spinach chloroplasts show an activation by light and deactivation in the dark. The stim ulation of acetyl-CoA carboxylase by dithiothreitol in darkened chloroplasts points to an
Andreas Sauer, Klaus-Peter Heise
openaire   +1 more source

The Compartmentation of Acetyl-Coenzyme A Carboxylase in Plants [PDF]

open access: yesPlant Physiology, 1995
Although the biochemical pathways for fatty acid synthesis are more or less similar in plants and animals (Harwood, 1988), there is a major cell biological difference between these two groups of eukaryotes. In plants, the major site of fatty acid synthesis is the plastid, an organelle absent from the animal cell.
Y., Sasaki, T., Konishi, Y., Nagano
openaire   +2 more sources

Activation of immobilized acetyl-Coenzyme A carboxylase [PDF]

open access: yesBiochemical Journal, 1978
Partially purified acetyl-CoA carboxylase was covalently bound to a Sepharose 4B matrix. Although aggregation was thus prevented, the enzymic activity was stimulated by citrate and isocitrate.
A D, Landman, J, Lampert
openaire   +2 more sources

The Role of Acetyl-Coenzyme A Synthetase in Arabidopsis [PDF]

open access: yesPlant Physiology, 2008
The acs1 knockout mutant that has a disruption in the plastidic acetyl-coenzyme A (CoA) synthetase (ACS; At5g36880) gene was used to explore the role of this protein and plastidic acetate metabolism in Arabidopsis (Arabidopsis thaliana). Disruption of the ACS gene decreased ACS activity by 90% and largely blocked the incorporation of exogenous (14)C ...
Lin, Ming, Oliver, David
openaire   +3 more sources

Machine Learning Accelerates Crystallization for Structure Determination

open access: yesAngewandte Chemie, EarlyView.
Single‐crystal X‐ray diffraction (SCXRD) is often constrained by the difficulty of obtaining suitable crystals. Here, a machine learning‐accelerated co‐crystal discovery workflow is established for a crystalline mate strategy that achieves over 95% prediction accuracy and experimentally delivers 114 co‐crystals from 120 candidates.
Cui‐Zhou Luan   +10 more
wiley   +2 more sources

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