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1 onal protein modification, the attachment of 4'-phosphopantetheine.
2 R)-4'-phospho-N-pantothenoylcysteine to form 4'-phosphopantetheine.
3 HlyC was also able to bind in vivo 4'-phosphopantetheine.
4 consensus sequence, DSLD, for attachment of 4'-phosphopantetheine.
5 ified by attachment of the prosthetic group, 4'-phosphopantetheine (4'-PP), which is transferred from
6 transferases (PPTs) catalyze the transfer of 4'-phosphopantetheine (4-PP) from coenzyme A to a conser
7 ole of ACP depends upon its covalently bound 4'-phosphopantetheine (4-PP)-conjugated acyl chain to su
9 rified active Orf* confirmed the presence of 4'-phosphopantetheine and 27-hydroxyoctacosanoic acid in
10 of the acetyl-Coenzyme A precursor S-acetyl-4'-phosphopantetheine as a possible treatment for neurod
11 odified) by AcpS, the PPTase responsible for 4'-phosphopantetheine attachment to the acyl carrier pro
14 cyl carrier protein (apoACP) via transfer of 4'-phosphopantetheine from coenzyme A (CoA) to the conse
15 the covalent posttranslational attachment of 4'-phosphopantetheine from coenzyme A (CoA), and this mo
16 purified ACP was properly modified with its 4'-phosphopantetheine functional group, (ii) it was not
17 acyl intermediates linked to its prosthetic 4'-phosphopantetheine group among four acyltransferases,
18 ing probable snapshots of ACP in action: the 4'-phosphopantetheine group of AcpP first binds an argin
19 po- and holo-forms of AcpM revealed that the 4'-phosphopantetheine group oscillates between two state
20 nally modified by covalent attachment of the 4'-phosphopantetheine group to the highly conserved seri
21 An unanticipated conformational shift of 4'-phosphopantetheine groups within the LpxD catalytic c
23 CoA in vivo and excreted significantly more 4'-phosphopantetheine into the medium compared to cells
25 are enzymes that catalyse the transfer of a 4'-phosphopantetheine moiety from CoA to a conserved ser
26 ynthase (AcpS) catalyzes the transfer of the 4'-phosphopantetheine moiety from coenzyme A (CoA) onto
27 enate (vitamin B(5)) is the precursor of the 4'-phosphopantetheine moiety of coenzyme A and acyl-carr
28 The enzyme is capable of transferring the 4'-phosphopantetheine moiety of coenzyme A to a conserve
30 nslocation of saturated acyl chains from the 4'-phosphopantetheine of the acyl carrier protein to the
31 thetases suggests nucleophilic attack by the 4'-phosphopantetheine on the alpha-phosphate of ATP.
33 y transferring an adenylyl group from ATP to 4'-phosphopantetheine (PhP) to form dephosphocoenzyme A.
34 reactive acyl intermediates with a swinging 4'-phosphopantetheine (Ppant) arm and interact with a su
35 le transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) in the presence of magnesi
36 '-monophosphate diester (L-Phe-AMP), L-Phe-S-4'-phosphopantetheine(Ppant)- and D-Phe-S-4'-Ppant-acyl
40 ies, which remained covalently linked to the 4'-phosphopantetheine residues of the two acyl carrier p
43 transfer of saturated acyl moieties from the 4'-phosphopantetheine thiol to the active site cysteine
44 sfer of an adenylyl group from Mg(2+):ATP to 4'-phosphopantetheine to form 3'-dephospho-CoA (dPCoA) a
45 o-ACP complex and the subsequent transfer of 4'-phosphopantetheine to the apo-ACP of the complex.
48 n contrast to yeast, which utilizes separate 4'-phosphopantetheine transferases to service each of th
49 pathway converting 4'-phosphopantothenate to 4'-phosphopantetheine, was confirmed in Escherichia coli
50 ein close in space to the fatty acid and the 4'-phosphopantetheine were identified using filtered/edi
51 main carries the growing chain tethered to a 4'-phosphopantetheine whereas the TE domain catalyses hy
52 ketide mimetic tethered to a stably modified 4'-phosphopantetheine, which provides important empirica
53 biosynthesis: the reversible adenylation of 4'-phosphopantetheine yielding 3'-dephospho-CoA and pyro
54 y transferring an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA).
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