ライフサイエンスコーパス: deacylase

1 itutes the first known extracellular protein deacylase.

2 B and D-1, respectively, by the R. etli 3-O-deacylase.

3 y conserved class of NAD(+)-dependent lysine deacylases.

4 such as DNA methyltransferases, and histone deacylases.

5 cotinamide to inhibit these NAD(+)-dependent deacylase activities of the sirtuins.

6 All tested sirtuin deacylase activities showed sensitivity to NADH in this

7 -B is shown to display both D-aminoacyl-tRNA deacylase activity and ATPase activity.

8 f class I leucyl-tRNA synthetase inactivates deacylase activity and produces misacylated tRNA.

9 hat there is redundancy in T.brucei inositol deacylase activity and that there is another enzyme whos

10 pagL) was identified by assaying for loss of deacylase activity in extracts of 14 random TnphoA::pag

11 K-12, for expression of Ca2+-dependent 3'-O-deacylase activity in membranes.

12 ork demonstrates that SseJ is an enzyme with deacylase activity in vitro and identifies three active-

13 However, total inositol deacylase activity was only reduced in GPIdeAc(-/-) tryp

14 n of the entire CP1 domain also disabled the deacylase activity, the deletion-bearing enzyme produced

15 HA-tagged GPIdeAc was shown to have inositol deacylase activity.

16 on in the gene (dtd) encoding D-tyrosyl-tRNA deacylase, an enzyme that prevents the misincorporation

17 SIRT5 is a NAD(+)-dependent lysine deacylase and removes both succinyl and malonyl groups.

18 Both deacylase and transacylase activities were inhibited 50-

19 rial sirtuins, SIRT3-5, are NAD(+)-dependent deacylases and ADP-ribosyltransferases that are critical

20 Sirtuins are a family of deacylases and ADP-ribosyltransferases with clear links

21 Thus, Notum is a Wnt deacylase, and palmitoleoylation is obligatory for the W

22 rtuins are a family of protein deacetylases, deacylases, and ADP-ribosyltransferases that regulate li

23 adenine dinucleotide (NAD)-dependent lysine deacylases, catalyzes the removal of fatty acylation fro

24 human acid ceramidase (AC; N-acylsphingosine deacylase) cleavage and activation.

25 ns are an ancient family of NAD(+)-dependent deacylases connected with the regulation of fundamental

26 We found that deacylase depletion increased K122 acylation on SOD1, wh

27 ene encoding the S. typhimurium lipid A 3'-O-deacylase, designated lpxR, by screening an ordered S. t

28 rystal structure of dimeric D-aminoacyl-tRNA deacylase (DTD) from Plasmodium falciparum in complex wi

29 underlies the inability of D-aminoacyl-tRNA deacylase (DTD) to discriminate between D-amino acids an

30 n of the properties of SIRT2 as a long chain deacylase enzyme.

31 s a form of protein "carbon stress" that the deacylases evolved to remove as a part of a global prote

32 ession of the pagL gene encoding lipid A 3-O-deacylase from Bordetella bronchiseptica and by inactiva

33 We now describe a membrane-bound deacylase from R. leguminosarum that removes a single es

34 The deacylase gene (pagL) was identified by assaying for los

35 An inositol deacylase gene, T. brucei GPIdeAc, has been identified.

36 n-encoding genes, and lpxR, the lipid A 3'-O-deacylase gene, was reduced in low temperature and after

37 ilD, including lpxR, which encodes a lipid A deacylase important for immune evasion.

38 Tiki protease in the Organizer and the Notum deacylase in presumptive neuroectoderm orchestrate verte

39 esting that YbaK functions as a Cys-tRNA Pro deacylase in vivo.

40 The sirtuin enzymes are important regulatory deacylases in a variety of biochemical contexts and may

41 Sirtuins are NAD(+) dependent lysine deacylases involved in many regulatory processes like co

42 D-Tyr-tRNA(Tyr) deacylase is an editing enzyme that removes d-tyrosine a

43 The class III lysine deacylases (KDACs), also known as the sirtuins, have eme

44 Sirtuins (SIRTs) are NAD-dependent deacylases, known to be involved in a variety of pathoph

45 enic functions of the secreted extracellular deacylase Notum, which restricts Wg signaling by cleavin

46 a periplasmic IM marker and the lipid A 3-O-deacylase PagL as an OM marker, we show that core-lipid

47 -deacylated form by heterologous lipid A 3-O-deacylase (PagL) expression.

48 expression of the P. aeruginosa lipid A 3-O-deacylase (PagL) in isolates from CF infants compared to

49 bronchiseptica contain an outer membrane 3-O-deacylase (PagL) that has been implicated in host immune

50 to regulate the expression of a lipid A 3-O-deacylase, PagL, and a lipid A palmitoyltransferase, Pag

51 The Salmonella lipid A 3-O-deacylase, PagL, is an outer membrane protein whose expr

52 1H NMR spectroscopy of the deacylase reaction product, generated with lipid IVA as

53 Sirtuins are protein deacylases regulating metabolism and stress responses, a

54 Sirtuins are NAD(+)-dependent lysine deacylases, regulating a variety of cellular processes.

55 The ProX protein acted as an aminoacyl-tRNA deacylase that cleaves preferentially Ala-tRNA and Gly-t

56 sirtuin SIRT5 is an NAD(+)-dependent protein deacylase that controls several metabolic pathways.

57 Jhp0634 was identified as an outer membrane deacylase that removes the 3'-linked acyl chains of H. p

58 (pagL) in Salmonella typhimurium, encoding a deacylase that removes the R-3-hydroxymyristate moiety a

59 Sirtuins are NAD(+)-dependent protein deacylases that are conserved in all domains of life and

60 nine dinucleotide (NAD(+))-dependent protein deacylases that are important for response to cellular s

61 -tRNA Pro and Cys-tRNA Cys and are also weak deacylases that cleave Gly-tRNA, Ala-tRNA, Ser-tRNA, Pro

62 Sirtuins are NAD(+)-dependent protein deacylases that cleave off acetyl but also other acyl gr

63 ily of NAD(+)-dependent protein deacetylases/deacylases that dynamically regulate transcription, meta

64 e the sirtuins, a family of NAD(+)-dependent deacylases that have evolved as coordinators of physiolo

65 namide adenine dinucleotide (NAD+)-dependent deacylases that have traditionally been linked with calo

66 oteins are moderately general aminoacyl-tRNA deacylases that preferentially hydrolyze Cys-tRNA Pro an

67 Sirtuins are NAD(+)-dependent deacylases that regulate numerous biological processes i

68 Sirtuins are class III histone deacylases that use NAD(+)as a co-substrate during amide

69 Inositol deacylase was affinity labelled with [3H]DFP and purifie