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1 t hydrolyzes fatty acyl-CoA to yield acyl 4'-phosphopantetheine.
2 nsensus sequence, DSLD, for attachment of 4'-phosphopantetheine.
3 l protein modification, the attachment of 4'-phosphopantetheine.
4 4'-phospho-N-pantothenoylcysteine to form 4'-phosphopantetheine.
5 HlyC was also able to bind in vivo 4'-phosphopantetheine.
6 ed by attachment of the prosthetic group, 4'-phosphopantetheine (4'-PP), which is transferred from Co
7 nsferases (PPTs) catalyze the transfer of 4'-phosphopantetheine (4-PP) from coenzyme A to a conserved
8 of ACP depends upon its covalently bound 4'-phosphopantetheine (4-PP)-conjugated acyl chain to suppo
10 phopantothenoylcysteine decarboxylase (EC ), phosphopantetheine adenylyltransferase (EC ), and dephos
15 oof of concept, the method was applied to 4'-phosphopantetheine adenylyltransferase (PPAT) from Mycob
21 ied active Orf* confirmed the presence of 4'-phosphopantetheine and 27-hydroxyoctacosanoic acid in th
22 ing the terminal thiol of the E. coli ACP 4'-phosphopantetheine arm into a mixed disulfide with 2-nit
23 on of the extender unit from acyl-CoA to the phosphopantetheine arm of an acyl carrier protein (ACP)
24 ate the binding of adenosine, as well as the phosphopantetheine arm of CoA to LipB, akin to binding t
25 enzoic acid, followed by its transfer to the phosphopantetheine arm of holo-EntB, an aryl carrier pro
27 ing of a statically anchored, fully extended phosphopantetheine arm of the acyl carrier protein domai
29 ester (L-Phe-AMP), transferring it to the HS-phosphopantetheine arm of the holo-thiolation (holo-T) d
32 Although the phosphate moiety within the phosphopantetheine arm overlaps, the pantetheine arm bin
35 the acetyl-Coenzyme A precursor S-acetyl-4'-phosphopantetheine as a possible treatment for neurodege
36 y to cell wall proteins, and iniA contains a phosphopantetheine attachment site motif suggestive of a
37 fied) by AcpS, the PPTase responsible for 4'-phosphopantetheine attachment to the acyl carrier protei
38 king simulations that identified a potential phosphopantetheine binding groove, the structural and fu
44 carrier protein (apoACP) via transfer of 4'-phosphopantetheine from coenzyme A (CoA) to the conserve
45 covalent posttranslational attachment of 4'-phosphopantetheine from coenzyme A (CoA), and this modif
46 ence after transfer of fluorescently labeled phosphopantetheine from coenzyme A to PKS ACP domains in
47 rified ACP was properly modified with its 4'-phosphopantetheine functional group, (ii) it was not acy
48 yl intermediates linked to its prosthetic 4'-phosphopantetheine group among four acyltransferases, in
49 probable snapshots of ACP in action: the 4'-phosphopantetheine group of AcpP first binds an arginine
50 and holo-forms of AcpM revealed that the 4'-phosphopantetheine group oscillates between two states;
51 ly modified by covalent attachment of the 4'-phosphopantetheine group to the highly conserved serine
52 An unanticipated conformational shift of 4'-phosphopantetheine groups within the LpxD catalytic cham
55 A in vivo and excreted significantly more 4'-phosphopantetheine into the medium compared to cells exp
56 moiety is attached via a thioester bond to a phosphopantetheine linker that is in turn bound to a ser
58 strate binding and catalysis, and identify a phosphopantetheine localization channel and a deep two-p
60 interaction between the protein and the acyl phosphopantetheine moieties of acetyl, malonyl, or 3-oxo
62 e enzymes that catalyse the transfer of a 4'-phosphopantetheine moiety from CoA to a conserved serine
63 hase (AcpS) catalyzes the transfer of the 4'-phosphopantetheine moiety from coenzyme A (CoA) onto a s
64 is the precursor for the biosynthesis of the phosphopantetheine moiety of coenzyme A and acyl carrier
65 te (vitamin B(5)) is the precursor of the 4'-phosphopantetheine moiety of coenzyme A and acyl-carrier
66 The enzyme is capable of transferring the 4'-phosphopantetheine moiety of coenzyme A to a conserved s
68 e linkage with the sulfhydryl group from the phosphopantetheine moiety of the acyl carrier protein.
69 vely charged ACPS residues and the holo-ACPP phosphopantetheine moiety, indicating product contains m
72 action step, the inherent flexibility of the phosphopantetheine molecule weakens the position depende
73 contain additional cofactors, NADPH and two phosphopantetheine molecules, which are shown to be invo
75 ocation of saturated acyl chains from the 4'-phosphopantetheine of the acyl carrier protein to the ac
77 Specific, stepwise truncation of CoA to 4-phosphopantetheine, pantetheine, and finally cysteamine
78 ransferring an adenylyl group from ATP to 4'-phosphopantetheine (PhP) to form dephosphocoenzyme A.
80 with the uptake of pantetheine (PanSH) or 4'-phosphopantetheine (PPanSH) as initial CoA precursors al
81 active acyl intermediates with a swinging 4'-phosphopantetheine (Ppant) arm and interact with a suite
82 Nonribosomal peptide synthetases (NRPSs) use phosphopantetheine (pPant) bearing carrier proteins to c
83 ia a thioester linkage to a covalently bound phosphopantetheine (PPant) cofactor of a carrier protein
85 transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) in the presence of magnesium.
86 hway whose acyl carrier protein (mACP) and 4-phosphopantetheine (Ppant) prosthetic group provide a so
87 and then loaded with a salicyl group on the phosphopantetheine (Ppant) thiol by action of the YbtE,
88 onophosphate diester (L-Phe-AMP), L-Phe-S-4'-phosphopantetheine(Ppant)- and D-Phe-S-4'-Ppant-acyl enz
89 nsferase (PptT), an enzyme that transfers 4'-phosphopantetheine (Ppt) from coenzyme A (CoA) to divers
94 primed on its three thiolation domains with phosphopantetheine prosthetic groups, GliP activates and
95 , which remained covalently linked to the 4'-phosphopantetheine residues of the two acyl carrier prot
98 implies that the inherent flexibility of the phosphopantetheine "swinging arm" also contributes signi
99 ctanoyl-transferase mainly recognizes the 4'-phosphopantetheine-tethered acyl-chain of its donor subs
100 tereoselectively hydrolyzes d-tryptophanyl-S-phosphopantetheine thioester and thus represents a nonca
101 beta-ketoacyl synthase domain (C161A) or the phosphopantetheine thiol of the acyl carrier protein dom
103 nsfer of saturated acyl moieties from the 4'-phosphopantetheine thiol to the active site cysteine thi
104 droxyacyl fatty acids that are coupled via a phosphopantetheine to an acyl carrier protein (ACP).
105 that undergo posttranslational priming with phosphopantetheine to enable covalent tethering of salic
106 r of an adenylyl group from Mg(2+):ATP to 4'-phosphopantetheine to form 3'-dephospho-CoA (dPCoA) and
108 s and direct enzymatic transfer of aminoacyl-phosphopantetheine to the carrier domains allow the aden
109 ways require the protein's prosthetic group, phosphopantetheine, to assemble an acyl chain or to tran
113 ontrast to yeast, which utilizes separate 4'-phosphopantetheine transferases to service each of three
114 hway converting 4'-phosphopantothenate to 4'-phosphopantetheine, was confirmed in Escherichia coli.
115 close in space to the fatty acid and the 4'-phosphopantetheine were identified using filtered/edited
116 n carries the growing chain tethered to a 4'-phosphopantetheine whereas the TE domain catalyses hydro
117 ide mimetic tethered to a stably modified 4'-phosphopantetheine, which provides important empirical e
118 final steps of CoA biosynthesis by coupling phosphopantetheine with ATP to form dephospho-CoA and it
119 osynthesis: the reversible adenylation of 4'-phosphopantetheine yielding 3'-dephospho-CoA and pyropho
120 ransferring an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA).