ライフサイエンスコーパス: phosphopantetheine

1 nsensus sequence, DSLD, for attachment of 4'-phosphopantetheine.

2 l protein modification, the attachment of 4'-phosphopantetheine.

3 4'-phospho-N-pantothenoylcysteine to form 4'-phosphopantetheine.

4 HlyC was also able to bind in vivo 4'-phosphopantetheine.

5 ed by attachment of the prosthetic group, 4'-phosphopantetheine (4'-PP), which is transferred from Co

6 nsferases (PPTs) catalyze the transfer of 4'-phosphopantetheine (4-PP) from coenzyme A to a conserved

7 of ACP depends upon its covalently bound 4'-phosphopantetheine (4-PP)-conjugated acyl chain to suppo

8 ities and a site for the prosthetic group 4'-phosphopantetheine (acyl carrier protein).

9 phopantothenoylcysteine decarboxylase (EC ), phosphopantetheine adenylyltransferase (EC ), and dephos

10 Phosphopantetheine adenylyltransferase (PPAT) catalyzes

11 Phosphopantetheine adenylyltransferase (PPAT) catalyzes

12 Phosphopantetheine adenylyltransferase (PPAT) from Esche

13 Phosphopantetheine adenylyltransferase (PPAT) is an esse

14 Phosphopantetheine adenylyltransferase (PPAT) is an esse

15 Phosphopantetheine adenylyltransferase (PPAT) regulates

16 Each phosphopantetheine adenylyltransferase (PPAT) subunit di

17 Human recombinant bifunctional phosphopantetheine adenylyltransferase/dephospho-CoA kin

18 ied active Orf* confirmed the presence of 4'-phosphopantetheine and 27-hydroxyoctacosanoic acid in th

19 on of the extender unit from acyl-CoA to the phosphopantetheine arm of an acyl carrier protein (ACP)

20 enzoic acid, followed by its transfer to the phosphopantetheine arm of holo-EntB, an aryl carrier pro

21 malonyl moiety of methylmalonyl-CoA onto the phosphopantetheine arm of the ACP domain.

22 ing of a statically anchored, fully extended phosphopantetheine arm of the acyl carrier protein domai

23 the aminoacyl-AMPs and transferred to the HS-phosphopantetheine arm of the holo-T domain.

24 ester (L-Phe-AMP), transferring it to the HS-phosphopantetheine arm of the holo-thiolation (holo-T) d

25 Each substrate could be loaded onto the phosphopantetheine arm of the thiolation domain as obser

26 d then transfers it to the free thiol of the phosphopantetheine arm of VibB's ArCP domain.

27 Although the phosphate moiety within the phosphopantetheine arm overlaps, the pantetheine arm bin

28 ino acid substrates delivered via prosthetic phosphopantetheine arms.

29 enzymes that carry covalent intermediates on phosphopantetheine arms.

30 the acetyl-Coenzyme A precursor S-acetyl-4'-phosphopantetheine as a possible treatment for neurodege

31 y to cell wall proteins, and iniA contains a phosphopantetheine attachment site motif suggestive of a

32 fied) by AcpS, the PPTase responsible for 4'-phosphopantetheine attachment to the acyl carrier protei

33 king simulations that identified a potential phosphopantetheine binding groove, the structural and fu

34 pI of 4.3, an alpha-helical structure, and a phosphopantetheine binding motif.

35 er formation between serine and its attached phosphopantetheine cofactor.

36 The structure also reveals the 4'-phosphopantetheine-conjugated acyl-group of ACP occupies

37 AcpS catalyzes the transfer of 4'-phosphopantetheine from coenzyme A (CoA) to apo-ACP, thu

38 carrier protein (apoACP) via transfer of 4'-phosphopantetheine from coenzyme A (CoA) to the conserve

39 covalent posttranslational attachment of 4'-phosphopantetheine from coenzyme A (CoA), and this modif

40 ence after transfer of fluorescently labeled phosphopantetheine from coenzyme A to PKS ACP domains in

41 rified ACP was properly modified with its 4'-phosphopantetheine functional group, (ii) it was not acy

42 yl intermediates linked to its prosthetic 4'-phosphopantetheine group among four acyltransferases, in

43 probable snapshots of ACP in action: the 4'-phosphopantetheine group of AcpP first binds an arginine

44 and holo-forms of AcpM revealed that the 4'-phosphopantetheine group oscillates between two states;

45 ly modified by covalent attachment of the 4'-phosphopantetheine group to the highly conserved serine

46 An unanticipated conformational shift of 4'-phosphopantetheine groups within the LpxD catalytic cham

47 not prevent binding of the fatty acyl or 4'-phosphopantetheine groups.

48 A in vivo and excreted significantly more 4'-phosphopantetheine into the medium compared to cells exp

49 moiety is attached via a thioester bond to a phosphopantetheine linker that is in turn bound to a ser

50 e features including the conformation of the phosphopantetheine linker.

51 strate binding and catalysis, and identify a phosphopantetheine localization channel and a deep two-p

52 he phenylalanyl moiety presented as Phe-S-4'-phosphopantetheine-modified (Ppant) acyl enzyme.

53 interaction between the protein and the acyl phosphopantetheine moieties of acetyl, malonyl, or 3-oxo

54 ral information about the orientation of the phosphopantetheine moiety during LpxA catalysis.

55 e enzymes that catalyse the transfer of a 4'-phosphopantetheine moiety from CoA to a conserved serine

56 hase (AcpS) catalyzes the transfer of the 4'-phosphopantetheine moiety from coenzyme A (CoA) onto a s

57 is the precursor for the biosynthesis of the phosphopantetheine moiety of coenzyme A and acyl carrier

58 te (vitamin B(5)) is the precursor of the 4'-phosphopantetheine moiety of coenzyme A and acyl-carrier

59 The enzyme is capable of transferring the 4'-phosphopantetheine moiety of coenzyme A to a conserved s

60 ctivation of MIA and MIA's attachment to the phosphopantetheine moiety of NosJ.

61 e linkage with the sulfhydryl group from the phosphopantetheine moiety of the acyl carrier protein.

62 vely charged ACPS residues and the holo-ACPP phosphopantetheine moiety, indicating product contains m

63 ation was due, at least in part, to the acyl-phosphopantetheine moiety.

64 nal modification of the ACP(L) domain with a phosphopantetheine moiety.

65 action step, the inherent flexibility of the phosphopantetheine molecule weakens the position depende

66 contain additional cofactors, NADPH and two phosphopantetheine molecules, which are shown to be invo

67 CoA, NAD, and FAD, from their precursors, 4'-phosphopantetheine, NMN, and FMN, respectively.

68 ocation of saturated acyl chains from the 4'-phosphopantetheine of the acyl carrier protein to the ac

69 tases suggests nucleophilic attack by the 4'-phosphopantetheine on the alpha-phosphate of ATP.

70 Specific, stepwise truncation of CoA to 4-phosphopantetheine, pantetheine, and finally cysteamine

71 ransferring an adenylyl group from ATP to 4'-phosphopantetheine (PhP) to form dephosphocoenzyme A.

72 The enzyme utilizes Mg-ATP and phosphopantetheine (PhP) to generate dephospho-CoA (dPCo

73 active acyl intermediates with a swinging 4'-phosphopantetheine (Ppant) arm and interact with a suite

74 Nonribosomal peptide synthetases (NRPSs) use phosphopantetheine (pPant) bearing carrier proteins to c

75 ia a thioester linkage to a covalently bound phosphopantetheine (PPant) cofactor of a carrier protein

76 The free phosphopantetheine (Ppant) cofactor of ACP occupies a co

77 transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) in the presence of magnesium.

78 and then loaded with a salicyl group on the phosphopantetheine (Ppant) thiol by action of the YbtE,

79 onophosphate diester (L-Phe-AMP), L-Phe-S-4'-phosphopantetheine(Ppant)- and D-Phe-S-4'-Ppant-acyl enz

80 By contrast, the phosphopantetheine prosthetic group is not required for

81 The 4'-phosphopantetheine prosthetic group of a holo-ACP is a l

82 n assembly intermediates attached via the 4'-phosphopantetheine prosthetic group.

83 ) and stearate (18:0-ACP) attached to the 4'-phosphopantetheine prosthetic group.

84 primed on its three thiolation domains with phosphopantetheine prosthetic groups, GliP activates and

85 , which remained covalently linked to the 4'-phosphopantetheine residues of the two acyl carrier prot

86 The phosphopantetheine stoichiometry correlated with the sub

87 A 4'-phosphopantetheine swinging arm bound through a phosphoe

88 implies that the inherent flexibility of the phosphopantetheine "swinging arm" also contributes signi

89 beta-ketoacyl synthase domain (C161A) or the phosphopantetheine thiol of the acyl carrier protein dom

90 These carrier proteins use the 4'-phosphopantetheine thiol to shuttle intermediates betwee

91 nsfer of saturated acyl moieties from the 4'-phosphopantetheine thiol to the active site cysteine thi

92 droxyacyl fatty acids that are coupled via a phosphopantetheine to an acyl carrier protein (ACP).

93 that undergo posttranslational priming with phosphopantetheine to enable covalent tethering of salic

94 r of an adenylyl group from Mg(2+):ATP to 4'-phosphopantetheine to form 3'-dephospho-CoA (dPCoA) and

95 CP complex and the subsequent transfer of 4'-phosphopantetheine to the apo-ACP of the complex.

96 s and direct enzymatic transfer of aminoacyl-phosphopantetheine to the carrier domains allow the aden

97 ways require the protein's prosthetic group, phosphopantetheine, to assemble an acyl chain or to tran

98 Nocardia phosphopantetheine transferase (PPTase) expressed in E.

99 The human 4'-phosphopantetheine transferase is also capable of phosph

100 A single candidate 4'-phosphopantetheine transferase, identified by BLAST sear

101 ontrast to yeast, which utilizes separate 4'-phosphopantetheine transferases to service each of three

102 hway converting 4'-phosphopantothenate to 4'-phosphopantetheine, was confirmed in Escherichia coli.

103 close in space to the fatty acid and the 4'-phosphopantetheine were identified using filtered/edited

104 n carries the growing chain tethered to a 4'-phosphopantetheine whereas the TE domain catalyses hydro

105 ide mimetic tethered to a stably modified 4'-phosphopantetheine, which provides important empirical e

106 final steps of CoA biosynthesis by coupling phosphopantetheine with ATP to form dephospho-CoA and it

107 osynthesis: the reversible adenylation of 4'-phosphopantetheine yielding 3'-dephospho-CoA and pyropho

108 ransferring an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA).