Results 191 to 200 of about 146,351 (241)

Disruption of starch biosynthesis and triacylglycerol degradation impairs growth but improves photosynthesis in Arabidopsis

open access: yesNew Phytologist, Volume 251, Issue 6, Page 3472-3488, September 2026.
Proposed model for altered carbon partitioning in wild‐type (a) and tgd1 sdp1 adg1‐1 Arabidopsis triple mutant (b). Summary Enhancing lipid accumulation by redirecting carbon from starch to triacylglycerol (TAG) in vegetative tissues is a promising strategy for developing high‐energy‐density crops for bioenergy production. However, our understanding of
Jilian Fan   +5 more
wiley   +1 more source
Some of the next articles are maybe not open access.

Related searches:

Regulation and structure of the heteromeric acetyl-CoA carboxylase

Biochimica Et Biophysica Acta - Molecular and Cell Biology of Lipids, 2016
The enzyme acetyl-CoA carboxylase (ACCase) catalyzes the committed step of the de novo fatty acid biosynthesis (FAS) pathway by converting acetyl-CoA to malonyl-CoA. Two forms of ACCase exist in nature, a homomeric and heteromic form. The heteromeric form of this enzyme requires four different subunits for activity: biotin carboxylase; biotin carboxyl ...
Jay Thelen
exaly   +3 more sources

Regulation of Spinach Chloroplast Acetyl-CoA Carboxylase

Archives of Biochemistry and Biophysics, 1998
We have investigated several factors which influence acetyl-CoA carboxylase (ACCase) activity in lysed spinach chloroplasts. (1) When assayed after rapid lysis of light-incubated chloroplasts, ACCase activity was 2-fold higher than activity from dark-incubated chloroplasts.
J B Ohlrogge
exaly   +3 more sources

Regulation of acetyl-CoA carboxylase

Biochemical Society Transactions, 2006
Acetyl-CoA carboxylase (ACC) catalyses the formation of malonyl-CoA, an essential substrate for fatty acid synthesis in lipogenic tissues and a key regulatory molecule in muscle, brain and other tissues. ACC contributes importantly to the overall control of energy metabolism and has provided an important model to explore mechanisms of enzyme control ...
R W, Brownsey   +4 more
openaire   +2 more sources

Wheat acetyl-CoA carboxylase

Plant Molecular Biology, 1993
The acetyl-CoA carboxylase present in both wheat germ and total wheat leaf protein contains ca. 220 kDa subunits. It is the major biotin-dependent carboxylase present in wheat chloroplasts. Active acetyl-CoA carboxylase purified from wheat germ is a homodimer with an apparent molecular mass of ca. 500 kDa.
P, Gornicki, R, Haselkorn
openaire   +2 more sources

Effect of insulin on association of acetyl CoA carboxylase phosphatase and acetyl CoA carboxylase

Biochemical and Biophysical Research Communications, 1985
Insulin promotes an association between acetyl CoA carboxylase and acetyl CoA carboxylase phosphatase. The association between rat epididymal fat tissue carboxylase and the phosphatase occurs in both a tissue culture system and in vivo and is accompanied by an increase in acetyl CoA carboxylase activity.
G R, Krakower, K H, Kim
openaire   +2 more sources

Acetyl CoA carboxylase

Archives of Biochemistry and Biophysics, 1971
Abstract A biotin carboxyl carrier protein (BCCP) from Escherichia coli has been purified and crystallized. The purified protein was found to be homogeneous by polyacrylamide gel electrophoresis and sedimentation in a synthetic boundary cell. BCCP has a sedimentation coefficient of 1.04 S, a diffusion coefficient ( D 20,w ) of 10.4 × 10 −7 cm 2 ...
A.M. Nervi   +2 more
openaire   +1 more source

Multi-subunit acetyl-CoA carboxylases

Progress in Lipid Research, 2002
Acetyl-CoA carboxylase (ACC) catalyses the first committed step of fatty acid synthesis, the carboxylation of acetyl-CoA to malonyl-CoA. Two physically distinct types of enzymes are found in nature. Bacterial and most plant chloroplasts contain a multi-subunit ACC (MS-ACC) enzyme that is readily dissociated into its component proteins.
John E, Cronan, Grover L, Waldrop
openaire   +2 more sources

Inhibitors of Mammalian Acetyl-CoA Carboxylase

Recent Patents on Cardiovascular Drug Discovery, 2007
Inhibition of acetyl-CoA carboxylase (ACC), with its resultant inhibition of fatty acid synthesis and stimulation of fatty acid oxidation, has the potential to favorably affect, in a concerted manner, a multitude of the cardiometabolic risk factors associated with diabetes, obesity, and the metabolic syndrome.
Jeffrey W, Corbett, James H, Harwood
openaire   +2 more sources

Home - About - Disclaimer - Privacy