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1 ogen biosynthesis and peroxisomal 3-ketoacyl thiolase.
2 shed by deleting the first 16 amino acids of thiolase.
3 and reduction of p46Shc expression activates thiolase.
4 ent of the peroxisomal matrix, e-oxoacyl-CoA thiolase.
5 ted whether Peb1p interacts with the PTS2 of thiolase.
6 ifunctional enzyme, and 3-oxoacyl-coenzyme A thiolase.
7 -CoA hydratase and long-chain 3-ketoacyl-CoA thiolase.
8 ith the mango, cucumber, and rat peroxisomal thiolases.
9 thylglutaryl-CoA synthases, and biosynthetic thiolases.
10 with amino acid sequence homology to type II thiolases.
11 2 acx2-1 double mutants and the ketoacyl-CoA thiolase-2 (kat2) mutant exhibit a sucrose-independent g
12 l coenzyme A (acetyl-CoA) acetyltransferase (thiolase), 3-hydroxybutyryl-CoA dehydrogenase, and acyl-
13 te could be partially restored by expressing thiolase (a PTS2-containing enzyme) fused to the PTS1.
14 studies showed colocalization of HsPMP20 and thiolase, a bona fide peroxisomal protein.
15                              Acetoacetyl CoA thiolase (AACT, EC 2.3.1.9) catalyzes the condensation o
16  is the lipid oxidation enzyme 3-ketoacylCoA thiolase ACAA2, to which p46Shc binds directly and with
17 g the cysteine, considered to be part of the thiolase active site, the kiwifruit protein shows approx
18                                     AcAc-CoA thiolase activities also paralleled HMG-CoA reductase an
19  cytosolic acetoacetyl coenzyme A (AcAc-CoA) thiolase activities.
20 hromatography was shown to have both ACT and thiolase activities.
21 y to regulatory stimuli than acetoacetyl-CoA thiolase activity but usually less than HMG-CoA reductas
22 es its expression and eliminates most of the thiolase activity in seedlings.
23 nificantly lower (k(cat) 3 min(-1)) than the thiolase activity of FadA (k(cat) 2170 min(-1)).
24 uggest p46Shc to be a negative mitochondrial thiolase activity regulator, and reduction of p46Shc exp
25 gher lipid oxidation capacity, and increased thiolase activity.
26 ocated downstream from yfcY, a gene encoding thiolase activity.
27  greater than 99% decrease in k(cat) for the thiolase activity.
28  indicating that the mutant lacks long-chain thiolase activity.
29 f a protein that directly binds and controls thiolase activity.
30                                       Mature thiolase alone, lacking the PTS2 signal, was not importe
31 sely affected the activity of 3-ketoacyl-CoA thiolase although not enough to become rate-limiting.
32  structural homology to aldolases, acts as a thiolase, an activity previously undescribed for this fa
33 e mevalonate pathway, acetoacetyl-coenzyme A thiolase and 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-
34              Similarly, induction of hepatic thiolase and bifunctional enzyme also required expressio
35 e product catalyzed both the acetoacetyl-CoA thiolase and HMG-CoA reductase reactions.
36   The catalytic properties of 3-ketoacyl-CoA thiolase and l-3-hydroxyacyl-CoA dehydrogenase of the mu
37    Under conditions at which acetoacetyl-CoA thiolase and long-chain thiolase were completely inactiv
38 ith ACP has not previously been observed for thiolases and in the case of the S. collinus FadA is sig
39 roxisomes or for the import of 3-oxoacyl-CoA thiolase (and at least two other peroxisomal matrix prot
40 cyl-CoA oxidase, L-bifunctional protein, and thiolase, and (b) a second noninducible pathway catalyzi
41                Moreover, the stabilized ICL, thiolase, and an ICL-GFP reporter remained peroxisome as
42 tor-activated receptor alpha (PPARalpha) and thiolase, and an up-regulation of PPARgamma, a positive
43 hase, acyl-CoA dehydrogenase, 3-ketoacyl-CoA thiolase, and many proteins involved in chaperone activi
44  At this stage, the basal mRNA levels of HD, thiolase, and other peroxisome proliferator-induced targ
45 me A (CoA), acyl CoA synthetase, oxoacyl CoA thiolase, and ubiquitin also were underexpressed in NASH
46 drial aldehyde dehydrogenase, 3-ketoacyl-CoA thiolases, and adenosine triphosphate synthase.
47 e and reduced accumulation of 3-ketoacyl-CoA thiolase, another PTS2-containing protein; both defects
48 e 2 peroxisomal targeting sequence (PTS2) of thiolase are defective, whereas the biogenesis of protei
49 n chains and a coenzyme moiety-unusual for a thiolase-are unknown.
50 lso related to the E. coli and mitochondrial thiolases, as well as to the acetoacetyl-CoA thiolases o
51                                       In the thiolase assay kinetic analyses revealed similar K(m) va
52 oxisomal Arabidopsis thaliana 3-ketoacyl-CoA thiolase (AtKAT), an enzyme of fatty acid beta-oxidation
53            Our results expand the utility of thiolase-based pathways and provide biosynthetic access
54  PTS2 protein imports increased the level of thiolase bound and imported into the organelles.
55                       Although the basics of thiolase chemistry are precedented, the mechanism by whi
56 nase deficiency, medium-chain 3-ketoacyl-CoA thiolase deficiency, 3-hydroxy-3-methylglutaryl-CoA synt
57           In competition experiments, mature thiolase did not affect the import of a PTS1 protein, bu
58               The import of the PTS2 protein thiolase differed from PTS1 protein import in several wa
59                                              Thiolase differs from these other peroxisomal proteins i
60 onate is virtually nil because acetoacyl-CoA thiolase does not favor the formation of beta-ketopentan
61 mature protein competes with the full-length thiolase during assembly of an import complex at the sur
62 t was missing the peroxisomal 3-ketoacyl-CoA thiolase encoded by the PEROXISOME DEFECTIVE1 (PED1/At2g
63  in ciliated neurons and by a 3-ketoacyl-coA thiolase (encoded by kat-1) that acts in fat storage tis
64   The catalytic properties of 3-ketoacyl-CoA thiolase, enoyl-CoA hydratase, and delta 3-cis-delta 2-t
65  In this regard, synthetic pathways based on thiolase enzymes to catalyze the initial carbon-carbon b
66  the previously characterized CoA-ligase and thiolase enzymes, provides evidence that the whole pathw
67  Features distinguish it from members of the thiolase family, suggesting that it carries out a relate
68 , like other KAS-II enzymes, mtKasB adopts a thiolase fold but contains unique structural features in
69 om Enterococcus is a member of the family of thiolase fold enzymes and, while similar to the recently
70 leaves, as does PED1 (encoding a 3-keto-acyl-thiolase for beta-oxidation).
71 n fluorescent protein chimera of peroxisomal thiolase, formation of peroxisomes, and peroxisome funct
72  oleate-induced PTS2-dependent import of the thiolase Fox3p into peroxisomes is conducted by the solu
73  SNO-CoA reductase, protects acetoacetyl-CoA thiolase from inhibitory S-nitrosylation and thereby aff
74 ivity is consistent with a beta-ketoacyl-CoA thiolase function in cholesterol beta-oxidation that is
75 ndogenous clostridial promoters: that of the thiolase gene (thlP) and that for the clostridial transc
76 -acetyl CoA, and KAT2 appears to be the only thiolase gene expressed at significant levels during ger
77 t loss-of-function mutations of the ketoacyl thiolase gene kat-1 result in an increased accumulation
78    An inhibitor of long-chain 3-ketoacyl-CoA thiolase has been developed as a tool for probing the co
79 se/3-hydroxyacyl-CoA dehydrogenase (HD), and thiolase, has been examined in mice by disrupting ACOX g
80 y using HMG-CoA synthase and acetoacetyl-CoA thiolase/HMG-CoA reductase from E. faecalis.
81           Kinetic studies of acetoacetyl-CoA thiolase implicated a ping-pong mechanism.
82                                              Thiolase import was slower than typical PTS1 protein imp
83 irming that the PTS2 signal is necessary for thiolase import.
84 sing p46Shc stimulates enzymatic activity of thiolase in vitro Thus, we suggest p46Shc to be a negati
85  Pex7p is functional, resulting in import of thiolase into peroxisomes and improved growth of the yea
86 at is selectively defective in the import of thiolase into peroxisomes but has a normal ability to pa
87               The activity of 3-ketoacyl-CoA thiolase involved in mitochondrial beta-oxidation of fat
88        Peb1p is found in peroxisomes whether thiolase is expressed or not.
89 t the peroxisomal packaging of PTS2 targeted thiolase is lacking.
90                                              Thiolase is the last enzyme of the mitochondrial fatty a
91                       The subunit, a typical thiolase, is a combination of two similar alpha/beta dom
92 mosome 2 (KAT2), which encodes a peroxisomal thiolase, is activated in early seedling growth.
93                               3-ketoacyl-CoA thiolase (KAT) (EC: 2.3.1.16) catalyses a key step in fa
94   Reduced fertilization was also observed in thiolase (kat2-1) and peroxisomal acyl-Coenzyme A synthe
95       Of the two major 3-ketoacyl coenzyme A thiolases, KAT2 plays the primary role in BA synthesis.
96 cation and biochemical characterization of a thiolase-ketoreductase pair involved in production of br
97        The fusion protein was expressed in a thiolase knockout strain.
98 id residues were fused in front of truncated thiolase lacking the NH2-terminal 16-amino acid PTS2.
99 lectively inhibits long-chain 3-ketoacyl CoA thiolase (LC 3-KAT), thereby reducing fatty acid oxidati
100 thiolases, as well as to the acetoacetyl-CoA thiolases of prokaryotes.
101                                          The thiolase-p46Shc connection shown here in vitro and in or
102                                   Finally, a thiolase-Peb1p complex was isolated by immunoprecipitati
103 ies of the mutant strains indicated that the thiolase reaction is the limiting step in PHB biosynthes
104  were completely inactivated, 3-ketoacyl-CoA thiolase retained some activity.
105 lity of residues within the motif, rat liver thiolase (rthio) and various chimeric chloramphenicol ac
106 carrier protein synthases are members of the thiolase superfamily and are key regulators of bacterial
107 Degradative thiolases, which are part of the thiolase superfamily and naturally function in the beta-
108 that is critical for this process is OleA, a thiolase superfamily enzyme that condenses two fatty acy
109                                    OleA is a thiolase superfamily enzyme that has been shown to catal
110                                           In thiolase superfamily enzymes, catalysis is achieved via
111 udies of the HMG-CoA synthase members of the thiolase superfamily have shown that the catalytic loop
112              OleA is the first characterized thiolase superfamily member that has two long-chain alky
113 rmation can be catalysed by enzymes from the thiolase superfamily, including beta-ketoacyl-acyl-carri
114 etabeta fold, which is characteristic of the thiolase superfamily.
115  substrates of this particular member of the thiolase superfamily.
116 sidue five, a change that is known to reduce thiolase targeting in vivo.
117 ha-branched products even when paired with a thiolase that highly prefers unbranched linear products.
118 erved a strong interaction between Peb1p and thiolase that was abolished by deleting the first 16 ami
119 rease the amount of radiolabeled full-length thiolase that was imported.
120 546) gene, annotated as a lipid-metabolizing thiolase, the expression of which is upregulated by chol
121 ed genes including peroxisomal 3-oxoacyl-CoA thiolase (THIO), peroxisomal enoyl-CoA hydratase/3-hydro
122 ofluorescence, localization of 3-oxoacyl-CoA thiolase to peroxisomes was unchanged whether Pal1 was p
123                                              Thiolases typically utilize a ping-pong mechanism center
124 ld lower and the Km for the substrate of the thiolase was 6-fold higher.
125 de consisting of the first 16 amino acids of thiolase was sufficient for the affinity binding of Peb1
126                                              Thiolase was thought previously only to be regulated by
127 hich acetoacetyl-CoA thiolase and long-chain thiolase were completely inactivated, 3-ketoacyl-CoA thi
128                                      ICL and thiolase were mislocalized to the cytosol but only ICL w
129      ICL, MLS, and the beta-oxidation enzyme thiolase were stabilized in the pex4-1 pex22-1 double mu
130          Of all beta-oxidation enzymes, only thiolases were inactivated by the inhibitor.
131 on enzymes (CYP4A3, bifunctional enzyme, and thiolase) were observed in the livers of HNF1alpha-null
132 dehydrogenase, and long-chain 3-ketoacyl-CoA thiolase, were determined with substrates having acyl ch
133 ty acyl-CoA oxidase, bifunctional enzyme, or thiolase, which accompanies peroxisome proliferation in
134                                  Degradative thiolases, which are part of the thiolase superfamily an
135 related to the peroxisomal beta-ketoacyl-CoA thiolases, which catalyze the CoA-dependent degradative

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