ライフサイエンスコーパス: lipoylation

1 through the covalent attachment of lipoate (lipoylation).

2 s that are responsible for bacterial protein lipoylation.

3 on and independent of traditional N-terminal lipoylation.

4 cid levels and drastically decreases protein lipoylation.

5 (173) mutants, only E170Q mutation prevented lipoylation.

6 ontain two different routes of mitochondrial lipoylation, an arrangement that has not been described

7 ion system and establish a crosstalk between lipoylation and mono-ADP-ribosylation.

8 nstructed, has a consensus motif (LTG C) for lipoylation and signal peptide cleavage.

9 ative damage but did not reverse the protein lipoylation defect.

10 A) and LipL2, restored lipoate scavenging in lipoylation-deficient bacteria, indicating that Plasmodi

11 a wild-type strain robustly outcompeted the lipoylation-deficient mutant in a murine model of lister

12 dy investigated the potential of recombinant lipoylation enzymes lipoate activating enzyme and lipoyl

13 er protein synthase is not vital for protein lipoylation in Arabidopsis (Arabidopsis thaliana) and do

14 yl domain, is sufficient to prevent aberrant lipoylation in E.coli.

15 Prevention of L1 lipoylation in K46AE2 removed this competitive L1 role a

16 We propose a model for protein lipoylation in which Lip2, Lip3, Lip5, and Gcv3 function

17 Similar to protein lipoylation in yeast, LIP2 likely also transfers octanoy

18 from the target for biotinylation to one for lipoylation, in vivo and in vitro.

19 that a target of lipoylation is required for lipoylation is a novel result.

20 Demonstration that a target of lipoylation is required for lipoylation is a novel resul

21 ally, GCV3, encoding the H protein target of lipoylation, is itself absolutely required for lipoylati

22 or with alanines substituted at the sites of lipoylation (Lys-46 in L1 or Lys-173 in L2).

23 Redox-dependent lipoylation may regulate processes such as central metab

24 LA and LIP2 together provide a basal protein lipoylation network to plants that is similar to that in

25 Lipoylation occurs via a novel redox-gated mechanism tha

26 LIP2 and LIP5 are required for lipoylation of all three mitochondrial target proteins:

27 ate-protein ligase homolog, is necessary for lipoylation of Lat1 and Kgd2, and the enzymatic activity

28 poylation, is itself absolutely required for lipoylation of Lat1 and Kgd2.

29 ient medium results in substantially reduced lipoylation of mitochondrial (but not apicoplast) protei

30 rized plant morphology, slow growth, reduced lipoylation of mitochondrial proteins, and the hyperaccu

31 Patients were deficient in lipoylation of mitochondrial proteins.

32 Whereas lipoylation of PDC-E2 is essential for enzymatic activit

33 recursors required for the posttranslational lipoylation of pyruvate and alpha-ketoglutarate dehydrog

34 fatty acid synthase system, namely depleted lipoylation of the H subunit of the photorespiratory enz

35 de in the mitochondrion and it catalyses the lipoylation of the H-protein; however, we show that LipL

36 orm of the domain become less flexible after lipoylation of the lysine residue.

37 iency in photorespiration due to the reduced lipoylation of the photorespiratory glycine decarboxylas

38 pyogenes, the activity is dependent on prior lipoylation of the target protein and can be reversed by

39 novo synthesis of precursors for the protein lipoylation pathway plays a vital role in maintenance of

40 The presence of an alternative lipoylation pathway that utilizes exogenous free lipoate

41 anoyl-ACP precursor required for the protein lipoylation pathway.

42 precursor required for the essential protein lipoylation pathway.

43 biosynthesis and haem biosynthesis, the two lipoylation pathways of P. falciparum might be attractiv

44 Plasmodium falciparum possesses two distinct lipoylation pathways that are found in separate subcellu

45 The observation of decreased lipoylation raises the possibility of a potential therap

46 mitochondrial lipoylation, while apicoplast lipoylation relies on biosynthesis.

47 d octanoyl moieties were translocated to the lipoylation site on the acceptor protein.

48 ts a 2-fold axis of quasi-symmetry, with the lipoylation site, Lys43, located at the tip of an expose

49 PDC in place of lipoic acid by the exogenous lipoylation system; the relative levels of lipoic acid a

50 e of utilizing exogenous lipoic acid for the lipoylation Therefore, host-derived lipoic acid may be i

51 al cysteine and therefore being incapable of lipoylation via a thioether linkage, the mutant protein

52 alysis of the role of these genes in protein lipoylation, we conclude that only one pathway for de no

53 that lipoate scavenging drives mitochondrial lipoylation, while apicoplast lipoylation relies on bios