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1                                              CoASH associates with two different sites on AAC as conf
2 d, NADPH reduction yields 1 protein-SH and 1 CoASH.
3 ate to coenzyme A (CoA): CH(3)COOPO(3)(2-) + CoASH <==> CH(3)COSCoA + HPO(4)(2-).
4 nal modification catalyst, using coenzyme A (CoASH) as a cosubstrate to phosphopantetheinylate Ser880
5                                  Coenzyme A (CoASH) is the major low-molecular weight thiol in Staphy
6 tyl-CoA (DPA-CoA) and three free coenzyme A (CoASH) products.
7 trobenzoic acid (DTNB) to detect coenzyme A (CoASH) release on acetylation of enzyme by the substrate
8                                  Coenzyme A (CoASH) replaces glutathione as the major low molecular w
9     In this work, the binding of coenzyme A (CoASH) to the aminoglycoside acetyltransferase (3)-IIIb
10 ansfer reaction was inhibited by coenzyme A (CoASH) with both a competitive and a noncompetitive comp
11 sis due to sequestration of free coenzyme A (CoASH).
12 an increase in CoA biosynthesis to alleviate CoASH sequestration.
13                      However, oleic acid and CoASH increased I-FABP Trp segmental mobility, while ole
14 Trp segmental mobility, while oleoyl CoA and CoASH decreased I-FABP Trp limiting anisotropy (order).
15 des with a novel 398-Da thiol, cysteine, and CoASH.
16 hopantetheinylated holo-PCP by pure Lys5 and CoASH with a Km of 1 microM and kcat of 3 min-1 for both
17 e collapses, generating the products OAS and CoASH.
18 roM and kcat of 3 min-1 for both the PCP and CoASH substrates.
19  substrate that binds to the active site and CoASH is released prior to the modified aminoglycoside.
20 m that this is the attachment site for bound CoASH.
21 yme is not subject to feedback inhibition by CoASH.
22 ulation in liver reduced non-esterified CoA (CoASH) and acetyl-CoA (C2-CoA).
23  intracellular concentration of reduced CoA (CoASH) in B. burgdorferi cells ( approximately 1 mM) and
24  intracellular concentrations of acetyl-CoA, CoASH, and pyruvate have been measured.
25 e regulation of the mitochondrial acetyl-CoA/CoASH ratio.
26 10.0-fold in the presence of the cosubstrate CoASH, while the entropy becomes 2.0-22.5-fold less favo
27             The synchrotron-reduced (Cys44 + CoASH) structure reveals ordered binding for the adenosi
28 ric assays with the DTNB method (412 nm) for CoASH production or by monitoring the use of a second su
29 s insensitive to feedback inhibition by free CoASH levels as high as 100 microm.
30 es post-translational pantetheinylation from CoASH as donor substrate.
31 unspecified cysteine abstracts a proton from CoASH forming a nucleophilic thiolate anion which attack
32            PZ-3022 therapy increased hepatic CoASH and C2-CoA and decreased C3-CoA in the PA mouse mo
33                               Interestingly, CoASH was able to reduce H(2)O(2) and be regenerated by
34          Neither oleoyl CoA, oleic acid, nor CoASH altered overall I-FABP rotational correlation time
35 p-coumaroyl-CoA, but neither p-coumarate nor CoASH, abrogated CouR's binding to its operator DNA in v
36 d) = 80 +/- 10 nm) but bound neither HIP nor CoASH.
37 oviding a clear rationale for the absence of CoASH inhibition, analysis of the Pan-binding pocket has
38 hout a significant change in the affinity of CoASH for AAC.
39 cid, donating a proton to the sulfur atom of CoASH as the tetrahedral intermediate collapses, generat
40 e of an aminoglycoside alters the binding of CoASH to AAC dramatically such that the binding occurs w
41                               The binding of CoASH to the high-affinity site occurs with a small, unf
42       Also, antibiotics eliminate binding of CoASH to the second site.
43 sine 3'-phosphate 5'-pyrophosphate moiety of CoASH, but the absence of density for the pantetheine ar
44 nitine, and palmitic acid in the presence of CoASH were without effect.
45 be widely applicable since the production of CoASH is common to all HAT enzymes, regardless of protei
46  species indirectly by measuring the rate of CoASH release.
47 es the covalent modification with release of CoASH.
48 maintains the reduced intracellular state of CoASH, has recently been reported.
49 such as fatty acids, fatty acyl CoAs, and/or CoASH differentially modulate the I-FABP and L-FABP dyna
50  of the importance of coenzyme A's (CoA's or CoASH) in many metabolic processes and the biosynthesis
51 f fatty acyl-CoAs into free fatty acids plus CoASH.
52 sacetylase catalyzes the following reaction: CoASH + CH3CO2PO3(2-) <==> CH3COSCoA + HPO4(2-) (where C
53                                All 12 CoA's (CoASH, HMG CoA, methylmalonyl CoA, succinyl CoA, methylc
54 and 78% based on coenzyme A trilithium salt (CoASH).
55                             While saturating CoASH induced a 30% quenching of Trp fluorescence in PCA
56 the first view of the reduced form (Cys42-SH/CoASH) of the Cys42-SSCoA redox center.
57           In this report we demonstrate that CoASH is the major thiol in Bacillus anthracis; a bioinf
58               We have recently reported that CoASH is the major low-molecular weight thiol in Bacillu
59                                          The CoASH generated in the HAT reactions was continuously me
60                                          The CoASH-dependent oxidation of alpha-ketoglutarate or pyru
61 gesting an even broader significance for the CoASH/CoAS-disulfide redox system in prokaryotic thiol/d
62                       Supplementation of the CoASH precursors pantothenic acid and cysteine normalize
63  direct measurement of the appearance of the CoASH product (k(cat) = 24 +/- 4 min(-1) and Km = 13 +/-
64                                        Thus, CoASH sequestration in PA leads to reduced TCA cycle act
65  for the conversion of pantothenate (Pan) to CoASH in Escherichia coli are conserved in B. anthracis.
66                                         When CoASH and ATP were present there was also a linear accum
67     T(5) was posttranslationally primed with CoASH to introduce the HS-pantetheinyl group and autoami