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1 the enzyme is a broad substrate specificity acyl-CoA synthetase.
2 was to use triacsin C to inhibit long-chain acyl-CoA synthetase.
3 d by an inhibitor (triacsin C) of long chain acyl-CoA synthetase.
4 imilarity to the Escherichia coli long chain acyl-CoA synthetase.
5 it encodes LACS2, a member of the long-chain acyl-CoA synthetases.
6 wo highly conserved motifs characteristic of acyl-CoA synthetases.
7 ptide synthetases, luciferase, and aryl- and acyl-CoA synthetases.
8 the defective gene had sequence homology to acyl-CoA synthetases.
9 Firefly luciferase is homologous to fatty acyl-CoA synthetases.
10 and murine homologs comprise a new family of acyl-CoA synthetases.
11 ultigene family of very long chain (C20-C26) acyl-CoA synthetases.
12 for RpPat, all of which are also AMP-forming acyl-CoA synthetases.
13 SrtN) regulate the activities of AMP-forming acyl-CoA synthetases.
14 ing Peri A and HSL but stably overexpressing acyl-CoA synthetase 1 (ACS1) and fatty acid transport pr
15 hearts with a temporally induced knockout of acyl-CoA synthetase 1 (Acsl1(T-/-)) are virtually unable
18 ates with increased expression of long-chain acyl-CoA synthetase 1 (ACSL1), an enzyme that catalyzes
20 ipotoxicity overexpressing ACSL1 (long-chain acyl-CoA synthetase 1) in cardiomyocytes, we show that m
23 that requires activation by very long-chain acyl-CoA synthetase-1 (ACSVL1) to modulate both targets,
24 sters GLUT4 in fat cells contains long chain acyl-CoA synthetase-1 and its product fatty acyl-CoA, sh
25 ectrometry of a p75 protein band, long chain acyl-CoA synthetase-1, specifically present in immunoads
26 y increased the beta-cell mRNA expression of acyl CoA synthetase-2 and peroxisomal acyl CoA oxidase i
28 transfected with control siRNA, knockdown of acyl-CoA synthetase 3 (ACSL3) significantly decreased re
29 A comparative analysis demonstrates that the acyl-CoA synthetase 3 is recruited early to the assembly
30 rial HMG-CoA synthase and increases in fatty acyl-CoA synthetase (3-8-fold) and carnitine palmitoyl-C
34 th basal and Wy-14,643-induced expression of acyl-CoA synthetase, a well characterized PPARalpha targ
35 s were generated in two domains conserved in acyl-CoA synthetases: a 6- amino acid substitution into
39 uggested that FATP1 exhibits very long chain acyl-CoA synthetase (ACS) activity and that such activit
43 omes and FA synthesis in the cytosol, namely acyl-CoA synthetase (acs-1 and acs-2), acyl-CoA oxidase
44 stence of inhibitor-sensitive and -resistant acyl-CoA synthetases (ACS, EC ) that are linked to speci
47 contained not only CPT1a but also long chain acyl-CoA synthetase (ACSL) and the voltage-dependent ani
60 he first crystal structure of a medium-chain acyl-CoA synthetase ACSM2A, in a series of substrate/pro
62 ly of proteins that includes very long-chain acyl-CoA synthetases (ACSVL) consists of six members.
63 (ACSL) and very long chain acyl-coenzyme A (acyl-CoA) synthetases [(ACSVL)/fatty acid transport prot
65 -chain fatty acids, and have very long-chain acyl CoA synthetase activities that were 40% wild-type.
67 ls at 24 h after infection had 2-fold higher acyl-CoA synthetase activities and 30% higher rates of f
68 al, exhibiting both fatty acid transport and acyl-CoA synthetase activities that work in concert to m
69 tty acid transport and very long-chain fatty acyl-CoA synthetase activities were distinguishable.
70 tty acid accumulation, very long-chain fatty acyl-CoA synthetase activities, and the fatty acid profi
71 on of mmFATP5 did not substantially increase acyl-CoA synthetases activities using the substrates tes
72 ximal levels of fatty-acid import and has an acyl CoA synthetase activity specific for very-long-chai
75 the cytoplasm of transfected cells displayed acyl-CoA synthetase activity for long chain fatty acid s
78 n either wild-type or nearly wild-type fatty acyl-CoA synthetase activity profiles; 2) those that had
79 lls revealed that most of the hsBG-dependent acyl-CoA synthetase activity was soluble and not membran
80 s, COS-1 cells expressing hsBG had increased acyl-CoA synthetase activity with either long-chain fatt
82 odulation of endoplasmic reticulum-localized acyl-CoA synthetase activity, although mutant forms of a
84 howed that VLCS activity, but not long-chain acyl-CoA synthetase activity, was reduced to about 40% o
85 tional in fatty acid import, only FATP2a had acyl-CoA synthetase activity, with an apparent preferenc
89 converted to 5HD-CoA by mitochondrial fatty acyl CoA synthetase and acted as a weak substrate or inh
91 esis of TAGs and CEs by targeting long-chain acyl-CoA synthetase and acyl-CoA:cholesterol acyltransfe
92 n this paper, we present evidence that FATP1/acyl-CoA synthetase and DGAT2/diacylglycerol acyltransfe
94 fic activities of the key enzymes long chain acyl-CoA synthetase and diacylglycerol acyltransferase,
95 equent genetic analysis identified ACS-4, an acyl-CoA synthetase and its FA-CoA product, as key germl
96 reactions are known reactions, catalyzed by acyl-CoA synthetase and peptidylglycine alpha-amidating
97 lts indicate that FATP1 is a very long chain acyl-CoA synthetase and suggest that a potential mechani
98 AAE15 has sequence similarity to long-chain acyl-CoA synthetases and a predicted N-terminal plastidi
99 ed fatty acids are esterified to acyl-CoA by acyl-CoA synthetases and transferred to lysophospholipid
101 whether adipocyte lipogenic proteins (CD36, acyl-CoA synthetases, and diacylglycerol acyltransferase
103 vation in these cells, indicating that other acyl-CoA synthetases are necessary for very long-chain f
104 results show that many different AMP-forming acyl-CoA synthetases are regulated by N-lysine acetylati
106 n a conformation similar to those adopted by acyl-CoA synthetases as they convert acyl adenylates int
107 t did not acetylate the wild-type long-chain acyl-CoA synthetase B (RpLcsB; formerly Rpa2714) enzyme
110 as palustris (RpPat) inactivates AMP-forming acyl-CoA synthetases by acetylating the epsilon-amino gr
112 rence confirmed that endogenous ACSVL3 is an acyl-CoA synthetase capable of activating both long-chai
113 Short- and medium-chain acyl coenzyme A (acyl-CoA) synthetases catalyze the formation of acyl-CoA
118 that PMNs and their plasma membranes use an acyl:CoA synthetase-dependent route to esterify 5-HETE a
120 on of an FATP4 variant with mutations in the acyl-CoA synthetase domain did not provide any degree of
121 lude that expression of FATP4 with an intact acyl-CoA synthetase domain in suprabasal keratinocytes i
122 CP) synthase AasC but inhibitors of the host acyl-CoA synthetase enymes ACSL also impaired growth of
123 eudomonas palustris, at least 10 AMP-forming acyl-CoA synthetase enzymes are acetylated by the Pat ho
124 nt lysine residue in a number of FadD (fatty acyl CoA synthetase) enzymes is acetylated by KATmt in a
125 olar morphology through the long-chain fatty acyl-CoA synthetase Faa1, independently of the RNA methy
128 These data support the hypothesis that fatty acyl-CoA synthetase (Faa1p or Faa4p) functions as a comp
130 xa2p complex functionally interacts with the acyl-CoA synthetases Faa2p and/or Fat1p on the inner sur
131 In Saccharomyces cerevisiae Fat1p and fatty acyl-CoA synthetase (FACS) are hypothesized to couple im
133 oA hydrolase (HIBCH, p = 8.42 x 10(-89)) and acyl-CoA synthetase family member 3 (ACSF3, p = 3.48 x 1
134 mutations in a gene encoding a member of the acyl-CoA synthetase family, a diverse group of evolution
136 fatty acid transport protein/very long chain acyl-CoA synthetase (FATP/Acsvl) family are emerging as
138 in fatty acids are converted to acyl-CoAs by acyl-CoA synthetase (fatty acid CoA ligase: AMP forming,
140 Saccharomyces cerevisiae contains four known acyl-CoA synthetases (fatty acid activation proteins, Fa
141 ly of AMP-forming enzymes that also includes acyl-CoA synthetases, firefly luciferase, and nonribosom
142 WLHTGDIGXWXPXGXLKIIDRKK, common to all fatty acyl-CoA synthetases for which sequence information is a
144 quence information from putative WS/DGAT and acyl-CoA synthetase genes identified in this strain was
145 identified gonadotropin-regulated long chain acyl-CoA synthetase (GR-LACS) was cloned and characteriz
148 Fatty acid transport protein 1 (FATP1) is an acyl-CoA synthetase highly expressed in skeletal muscle
152 hen bred to transgenic mice that overexpress acyl-CoA synthetase in the heart, a strain that exhibits
156 ymatic mechanism of FadK is similar to other acyl-CoA synthetases in that it forms an acyl-AMP interm
157 ns a histidine residue where all other known acyl-CoA synthetases, including mouse and rat ACSBG2, co
158 ily of both prokaryotic and eukaryotic fatty acyl-CoA synthetases, indicating a common ancestry.
160 Moreover, mLD formation was blocked by the acyl-CoA synthetase inhibitor triacsin C, implicating th
162 pression was completely blocked by the fatty acyl-CoA synthetase inhibitor, triacsin C, evidence of i
163 nation of a branched chain fatty acid and an acyl-CoA synthetase is required for critical cellular pr
164 acids to their CoA derivatives, catalyzed by acyl-CoA synthetases, is involved in AMPK activation by
172 utin pathway genes, which encodes long-chain acyl-CoA synthetase LACS2, is likely to be directly targ
173 e palmitoyltransferase-I (CPT-I), long-chain acyl-CoA synthetase (LCAS), and voltage-dependent anion
174 tment increased the activities of long chain acyl-CoA synthetases (LCASs), including oleoyl-CoA synth
175 dy revealed a central role of the long-chain acyl-CoA synthetase LCS2 in the production of triacylgly
178 ion into TAG, with long lasting increases in acyl-CoA synthetase long 1 (ACSL1) and diacylglycerol ac
179 rnitine O-palmitoyltransferase 1 (Cpt1a) and acyl-CoA synthetase long chain family member 1 (Acsl1),
180 plex consisting of TIP30, endophilin B1, and acyl-CoA synthetase long chain family member 4 (ACSL4) t
181 (Ppargc1a), uncoupling protein 1 (Ucp1) and acyl-CoA synthetase long-chain family member 1 (Acsl1),
182 s inserted within an intron of the autosomal acyl-CoA synthetase long-chain family member 3 (Acsl3) g
183 ferentiation, and that overexpression of rat acyl-CoA synthetase long-chain family member 6 (Acsl6, f
184 ependent steroid dehydrogenase-like protein, acyl-CoA synthetase, long chain family member (ACSL) 1,
186 osphate acyltransferase mRNA fell by 57% and acyl-CoA synthetase mRNA by 67% (brain isoform) and 38%
187 reported that hBG1, the human homolog of the acyl-CoA synthetase mutated in the Drosophila mutant "bu
188 allowed us to delineate a new superfamily of acyl-CoA synthetases (nucleoside diphosphate-forming) an
189 ACSL1 (acyl-CoA synthetase 1), the major acyl-CoA synthetase of adipocytes, has been proposed to
190 was significantly more similar to that of an acyl-CoA synthetase of the distantly related bacterium,
191 echanism and crystal structure evidence, the acyl-CoA synthetases, one of three subgroups of a superf
193 factor-TU, methylglutaryl coenzyme A (CoA), acyl CoA synthetase, oxoacyl CoA thiolase, and ubiquitin
195 atty acid-CoA ligase (also called fatty acid acyl-CoA synthetase) plays an essential role in lipid bi
196 enzyme A (acyl-CoA) dehydrogenase (pltE), an acyl-CoA synthetase (pltF), a thioesterase (pltG), and t
200 hibition of either acetyl-CoA carboxylase or acyl-CoA synthetase reduced mineralization of CVCs, wher
201 owledge, these mutant proteins are the first acyl-CoA synthetases reported that are defective in aden
202 conserved motifs from all known families of acyl-CoA synthetases revealed that hsBG along with the D
203 cluding multiple AMP-forming CoA ligases and acyl-CoA synthetases seem to be present as ways to form
204 al cholesterol ester hydrolase 1 (NCEH1) and acyl-CoA synthetase short-chain family member 2 (ACSS2).
205 pose that this sequence represents the fatty acyl-CoA synthetase signature motif (FACS signature moti
206 e ATP/AMP binding domain and the 25-aa fatty acyl-CoA synthetase signature motif, but displays low ov
207 een site-directed mutations within the fatty acyl-CoA synthetase structural gene (fadD) corresponding
209 D cells by using triacsin C, an inhibitor of acyl-CoA synthetase that blocks the reincorporation of h
211 acid transport protein 4 (FATP4) is a fatty acyl-CoA synthetase that preferentially activates very l
212 As such, LACS1 defines a functionally novel acyl-CoA synthetase that preferentially modifies both VL
213 5 and triacsin C, an inhibitor of long chain acyl-CoA synthetase that reduces LC-CoA levels, did not
215 rresponding sequences from other AMP-forming acyl-CoA synthetases that were known RpPat substrates.
216 eversed by triacsin C, an inhibitor of fatty acyl-CoA synthetase, the enzyme that generates LC-CoA.
218 The adenylate-forming enzymes, including acyl-CoA synthetases, the adenylation domains of non-rib
219 studies have focused on the structure of the acyl-CoA synthetases, their post-translational modificat
220 R8/LACS1, one of nine Arabidopsis long-chain acyl-CoA synthetases thought to activate acyl chains.
221 on of Triacsin-C, an inhibitor of long-chain acyl-CoA synthetase, to AdCMV-GlpK-treated INS-1 cells d
222 e palmitoyl-CoA transferase, very long chain acyl-CoA synthetase, very long chain acyl-CoA dehydrogen
223 n crossed with animals expressing long-chain acyl-CoA synthetase via the MHC promoter (MHC-ACS), whic
225 , which each have very long-chain fatty acid acyl-CoA synthetase (VLCFA-ACS) activity, as negative re
226 d with decreased peroxisomal very long-chain acyl-CoA synthetase (VLCS) activity and decreased peroxi
229 odystrophy, are activated by very long-chain acyl-CoA synthetase (VLCS) normally found in peroxisomes
230 unction of peroxisomal very long chain fatty acyl-CoA synthetase (VLCS) that leads to severe and prog
234 y (C16:0), characteristic of very long chain acyl-CoA synthetases, whereas both mutant M1 and M2 were
236 membrane-bound fatty acid transporters or as acyl-CoA synthetases, which activate long-chain fatty ac
237 ture motif) common to long- and medium-chain acyl-CoA synthetases, which appears to contribute to the
238 ed, expressed, and characterized as a 65-kDa acyl-CoA synthetase with extremely high specificity for
239 wn crystal structures of the T. thermophilus acyl-CoA synthetase with remarkably high levels of conse
240 dings indicate that inhibition of long-chain acyl-CoA synthetases with triacsin C, a fatty acid analo
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