نتایج جستجو برای: malonyl

تعداد نتایج: 1296  

1999
GARY W. GOODWIN

Goodwin, Gary W., and Heinrich Taegtmeyer. Regulation of fatty acid oxidation of the heart by MCD and ACC during contractile stimulation. Am. J. Physiol. 277 (Endocrinol. Metab. 40): E772–E777, 1999.—We tested the hypothesis that the level of malonyl-CoA, as well as the corresponding rate of total fatty acid oxidation of the heart, is regulated by the opposing actions of acetyl-CoA carboxylase ...

Journal: :Applied and environmental microbiology 2014
Junjun Wu Oliver Yu Guocheng Du Jingwen Zhou Jian Chen

Malonyl coenzyme A (malonyl-CoA) is an important precursor for the synthesis of natural products, such as polyketides and flavonoids. The majority of this cofactor often is consumed for producing fatty acids and phospholipids, leaving only a small amount of cellular malonyl-CoA available for producing the target compound. The tuning of malonyl-CoA into heterologous pathways yields significant p...

Journal: :The Biochemical journal 1989
V A Zammit C G Corstorphine M P Kolodziej

The functional molecular sizes of the protein(s) mediating the carnitine palmitoyltransferase I (CPT I) activity and the [14C]malonyl-CoA binding in purified outer-membrane preparations from rat liver mitochondria were determined by radiation-inactivation analysis. In all preparations tested the dose-dependent decay in [14C]malonyl-CoA binding was less steep than that for CPT I activity, sugges...

Journal: :The Biochemical journal 1992
M Guzmán M J Geelen

A procedure is described for the rapid measurement of the activity of mitochondrial-outer-membrane carnitine palmitoyltransferase (CPTo) and peroxisomal carnitine palmitoyltransferase (CPTp) in digitonin-permeabilized hepatocytes. CPTo activity was determined as the tetradecylglycidate (TDGA)-sensitive malonyl-CoA-sensitive CPT activity, whereas CPTp activity was monitored as the TDGA-insensiti...

2001
D. L.

Recently, our laboratory reported the involvement of cytochrome be in the elongation of hepatic microsomal fatty acids (Keyes, S. R., Alfano, J. A., Jansson, I., and Cinti, D. L. (1979) J. Biol. Chem. 254,7778-7784). In this paper, a correlation between the rates of ba reoxidation in the presence of malonyl-CoA and malonyl-CoA incorporation measured under various conditions was demonstrated, th...

Journal: :The Journal of biological chemistry 2012
Chong Wai Liew Martina Nilsson Ming Wei Chen Huihua Sun Tobias Cornvik Zhao-Xun Liang Julien Lescar

Biosynthesis of the enediyne natural product dynemicin in Micromonospora chersina is initiated by DynE8, a highly reducing iterative type I polyketide synthase that assembles polyketide intermediates from the acetate units derived solely from malonyl-CoA. To understand the substrate specificity and the evolutionary relationship between the acyltransferase (AT) domains of DynE8, fatty acid synth...

Journal: :Biochimica et biophysica acta 1960
G K MENON J R STERN F P KUPIECKI M J COON

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2005
Seung Hun Cha Zhiyuan Hu Shigeru Chohnan M Daniel Lane

Malonyl-CoA functions as a mediator in the hypothalamic sensing of energy balance and regulates the neural physiology that governs feeding behavior and energy expenditure. The central administration of C75, a potent inhibitor of the fatty acid synthase (FAS), increases malonyl-CoA concentration in the hypothalamus and suppresses food intake while activating fatty acid oxidation in skeletal musc...

Journal: :Journal of bacteriology 2002
Michael Hügler Castor Menendez Hermann Schägger Georg Fuchs

The 3-hydroxypropionate cycle is a new autotrophic CO(2) fixation pathway in Chloroflexus aurantiacus and some archaebacteria. The initial step is acetyl-coenzyme A (CoA) carboxylation to malonyl-CoA by acetyl-CoA carboxylase, followed by NADPH-dependent reduction of malonyl-CoA to 3-hydroxypropionate. This reduction step was studied in Chloroflexus aurantiacus. A new enzyme was purified, malon...

Journal: :Circulation research 1991
D F Pauly K A Kirk J B McMillin

The sensitivity of carnitine palmitoyl coenzyme A (CoA) transferase I to inhibition of its activity by malonyl-CoA is progressively reduced in mitochondria isolated from ischemic cardiac cells as blood flow decreases to 30% or less of the preocclusion flow. The activity of carnitine palmitoyl-CoA transferase I in mitochondria isolated from nonischemic cardiac cells demonstrates incomplete inhib...

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