scholarly journals The Bacterial signal transduction protein GlnB regulates the committed step in fatty acid biosynthesis by acting as a dissociable regulatory subunit of acetyl-CoA carboxylase

2015 ◽  
Vol 95 (6) ◽  
pp. 1025-1035 ◽  
Author(s):  
Edileusa C.M. Gerhardt ◽  
Thiago E. Rodrigues ◽  
Marcelo Müller-Santos ◽  
Fabio O. Pedrosa ◽  
Emanuel M. Souza ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Regulatory Subunit ◽  
Acetyl Coa Carboxylase ◽  
Acid Biosynthesis ◽  
Acetyl Coa ◽  
Signal Transduction Protein ◽  
Bacterial Signal Transduction

Fatty-acid biosynthesis and acetyl-coa carboxylase as a target of diclofop, fenoxaprop and other aryloxy-phenoxy-propionic acid herbicides

1988 ◽  
Vol 43 (1-2) ◽  
pp. 47-54 ◽  
Author(s):  
Klaus Kobek ◽  
Manfred Focke ◽  
K. Lichtenthaler Botanisches
Keyword(s):  
Fatty Acid ◽  
Propionic Acid ◽  
Fatty Acid Biosynthesis ◽  
De Novo ◽  
Free Acid ◽  
Acetate Incorporation ◽  
Acetyl Coa Carboxylase ◽  
Acid Biosynthesis ◽  
Acetyl Coa ◽  
Acid Herbicides

The effect of the herbicides and aryloxy-phenoxy-propionic acid derivatives diclofop, fenoxaprop, fluazifop and haloxyfop and their ethyl, methyl or butyl esters on the de novo fatty-acid biosynthesis of isolated chloroplasts was investigated with intact chloroplasts isolated from sensitive grasses (Poaceae) and tolerant dicotyledonous plants (Pisum, Spinacia). The 4 herbicides (free-acid form) block the de novo fatty-acid biosynthesis ([2-14C]acetate incorporation into the total fatty-acid fraction) of the sensitive Avena chloroplasts in a dose-dependent manner. The I50- values (a 50% inhibition of the [14C]acetate incorporation) lie in the range of 10-7 to 2 x 10-6 ᴍ. The ethyl or methyl esters (diclofop, fenoxaprop, haloxyfop) and butyl ester (fluazifop) do not affect the de novo fatty-acid biosynthesis of isolated chloroplasts or only at a very high concentration of ca. 10-4 ᴍ. In contrast, the de novo fatty-acid biosynthesis of the tolerant dicotyledonous species (pea, spinach) is not affected by the 4 aryloxy-phenoxy-propionic acid herbicides. In an enzyme preparation isolated from chloroplasts of the herbicide-sensitive barley plants the de novo fatty-acid biosynthesis from [14C]acetate and [14C]acetyl-CoA is blocked by all 4 herbicides (free acids), whereas that of [14C]malonate and [14C]malonyl-CoA is not affected. This strongly suggests that the target of all 4 herbicides (free-acid form) is the acetyl-CoA carboxylase within the chloroplasts. The applied ester derivatives, in turn, which are ineffective in the isolated chloroplast test system, have equally little or no effect on the activity of the acetyl-CoA carboxylase. It is assumed that the acetyl-CoA carboxylase of the tolerant dicot plants investigated is modified in such a way that the 4 herbicides cannot bind to and affect the target

Glucocorticoid regulation of fatty acid synthase gene expression in fetal rat lung

1993 ◽  
Vol 265 (2) ◽  
pp. L140-L147 ◽  
Author(s):  
Z. X. Xu ◽  
W. Stenzel ◽  
S. M. Sasic ◽  
D. A. Smart ◽  
S. A. Rooney
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Fatty Acid Biosynthesis ◽  
Fetal Lung ◽  
Acetyl Coa Carboxylase ◽  
Rat Lung ◽  
Acid Biosynthesis ◽  
Atp Citrate Lyase ◽  
Acetyl Coa ◽  
Citrate Lyase

There are developmental and glucocorticoid-induced increases in the rate of fatty acid biosynthesis and in the activity of fatty acid synthase in late gestation fetal lung. We have now measured mRNA levels of fatty acid synthase and of two other enzymes of fatty acid biosynthesis, ATP citrate lyase and acetyl-CoA carboxylase, in developing fetal and postnatal rat lung and in fetal lung explants cultured with and without dexamethasone. There was a developmental increase in the mRNA for fatty acid synthase with the maximum level being reached on fetal day 21 (term is fetal day 22). This profile was similar to that reported for de novo fatty acid synthesis and fatty acid synthase activity. There was a similar but less pronounced developmental increase in the mRNA for ATP citrate lyase and a corresponding increase in its activity. There was no developmental change in the mRNA for acetyl-CoA carboxylase. Dexamethasone increased the level of fatty acid synthase mRNA approximately threefold but had no effect on those for ATP citrate lyase and acetyl-CoA carboxylase. The effect of dexamethasone on fatty acid synthase mRNA was rapid, biphasic, and partly inhibited by actinomycin D and cycloheximide. We conclude that glucocorticoids increase expression of the gene for fatty acid synthase in fetal lung. The effect of the hormone appears to be due to increased transcription and post-transcriptional events and is dependent on protein synthesis.

Regulation of fatty acid biosynthesis in rats by physical training

1984 ◽  
Vol 56 (4) ◽  
pp. 1060-1064 ◽  
Author(s):  
R. Scorpio ◽  
R. L. Rigsby ◽  
D. R. Thomas ◽  
B. D. Gardner
Keyword(s):  
Fatty Acid ◽  
Physical Training ◽  
Fatty Acid Biosynthesis ◽  
Male Rats ◽  
Maximal Velocity ◽  
Acetyl Coa Carboxylase ◽  
Acid Biosynthesis ◽  
Acetyl Coa ◽  
Carboxylase Activity ◽  
Hepatic Fatty Acid

Physical training in the form of long-term nonexhaustive daily exercise was studied as a means of regulating fatty acid biosynthesis. Male rats were required to swim for periods up to 90 min/day. The exercise was carried out 6 days/wk for approximately 11 wk. Hepatic fatty acid biosynthesis and acetyl-CoA carboxylase [acetyl-CoA: CO2 ligase (EC 6.4.1.2)] activities were compared with nonexercised rats. At the end of the training period the exercised rats had a lower rate of fatty acid biosynthesis activity and a lower rate of acetyl-CoA carboxylase activity. The difference in acetyl-CoA carboxylase activity was due to a change in maximal velocity with no significant change in the Michaelis constant for acetyl-CoA. Untrained rats were subjected to a single bout of exercise. They also exhibited lower rates of fatty acid biosynthesis and acetyl-CoA carboxylase activities compared with nonexercised rats. However, the lower rates of these enzyme activities were sustained longer in the physically trained rats compared with the exercised untrained rats after the cessation of exercise. These results implicate acetyl-CoA carboxylase as a control site in the regulation of hepatic fatty acid biosynthesis by both physical training and acute exercise in rats. Possible inhibitory mechanisms are discussed.

The role of phosphorylation/dephosphorylation of acetyl-CoA carboxylase in the regulation of mammalian fatty acid biosynthesis

1986 ◽  
Vol 14 (3) ◽  
pp. 559-562 ◽  
Author(s):  
MICHAEL R. MUNDAY ◽  
TIMOTHY A. J. HAYSTEAD ◽  
ROSS HOLLAND ◽  
DAVID A. CARLING ◽  
D. GRAHAME HARDIE
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Acetyl Coa Carboxylase ◽  
Acid Biosynthesis ◽  
Acetyl Coa

Notes: Inhibition of the Acetyl-CoA Carboxylase of Barley Chloroplasts by Cycloxydim and Sethoxydim

1987 ◽  
Vol 42 (11-12) ◽  
pp. 1361-1363 ◽  
Author(s):  
Manfred Focke ◽  
Hartmut K. Lichtenthaler
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Enzyme Preparation ◽  
Fatty Acid Biosynthesis ◽  
De Novo ◽  
Acetyl Coa Carboxylase ◽  
Acid Biosynthesis ◽  
Hordeum Vulgare L ◽  
Acetyl Coa ◽  
Malonyl Coa

The effect of the three cyclohexane-1,3-dione derivatives cycloxydim, sethoxydim and clethodim on the incorpora­tion of 14C-labelled acetate, malonate. acctyl-CoA or malonyl-CoA into fatty acids was studied in an enzyme preparation isolated from barley chloroplasts (Hordeum vulgare L. var. “Alexis”). The herbicides cycloxydim, clethodim and sethoxydim block the de novo fatty acid biosynthesis from [2-14C]acetatc and [1-14C]acetyl-CoA, whereas that of [2-14C]malonatc and [2-14C)malonyl-CoA is not affected. The data indicate that the mode of action of the cyclohexane-1,3-dione derivatives in the sensitive bar­ley plant consists in the inhibition of de novo fatty acid biosynthesis by blocking the acetyl-CoA carboxylase (EC 6.4.1.2.).

Mode of Action of Herbicides Affecting Acetyl-CoA Carboxylase and Fatty Acid Biosynthesis

1990 ◽  
Vol 45 (5) ◽  
pp. 521-528 ◽  
Author(s):  
Hartmut K. Lichtenthaler
Keyword(s):  
Fatty Acid ◽  
Mode Of Action ◽  
Fatty Acid Biosynthesis ◽  
De Novo ◽  
Acetyl Coa Carboxylase ◽  
Acid Biosynthesis ◽  
Acetyl Coa ◽  
Enzyme Preparations ◽  
Acid Herbicides ◽  
Target Enzyme

The mode of action of cyclohexane-l,3-dione-type (cycloxydim, clethodim, sethoxydim, tralkoxydim) and aryloxyphenoxypropanoate-type herbicides (diclofop, fenoxaprop, haloxyfop, fluazifop) is summarized in this review. Both herbicide classes, though structurally completely different, specifically block the same target enzyme i.e. the plastid acetyl-CoA carboxylase (ACC) (EC 6.4.1.2). Most members of the Poaceae are sensitive towards both herbicide groups, whereas other monocotyledonous plants as well as the dicotyledonous plants appear to be resistant. This resistance, which can be found on the level of whole plants, in isolated chloroplasts and also on the level of ACC-enzyme preparations, is apparently due to a modification of the target enzyme ACC. Within the sensitive grass family some members (Festuca and Poa species) are partially tolerant against both graminicide groups. In the case of cyclohexanedione herbicides the tolerance seems to be due to a reduced sensitivity of the target enzyme. In the case of aryloxyphenoxypropionic acid herbicides the tolerance is apparently based on a combined action of cytoplasmic factors (metabolization?) and a slightly reduced sensitivity of the target enzyme. From differences in the sensitivity of certain grasses against the two herbicide classes it is concluded that both graminicide groups bind to the same binding domaine of the ACC enzyme but possess different subsites. The consequences of the block of de novo fatty acid biosynthesis in the plastids of sensitive plants is the lack of glycerolipid and biomembrane formation which finally causes cell death in the meristematic tissues.

Enhancement of fatty acid biosynthesis by exogenous acetyl-CoA carboxylase and pantothenate kinase in Escherichia coli

2020 ◽  
Vol 42 (12) ◽  
pp. 2595-2605 ◽  
Author(s):  
Shusaku Satoh ◽  
Miho Ozaki ◽  
Saki Matsumoto ◽  
Takumi Nabatame ◽  
Moena Kaku ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Acetyl Coa Carboxylase ◽  
Acid Biosynthesis ◽  
Acetyl Coa ◽  
Pantothenate Kinase
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