ライフサイエンスコーパス: transamidase

1 ould not interact with other subunits of the transamidase.

2 tion is carried out by an ER enzyme, GPtdIns transamidase.

3 ing the presumed substrate for the yeast GPI transamidase.

4 provide a potential means for isolating the transamidase.

5 gnition of the omega site by the GPI-protein transamidase.

6 ered to be an intermediate in catalysis by a transamidase.

7 udy COOH-terminal processing by the putative transamidase.

8 small number of individuals: loss of FXIIIa (transamidase-activated form) crosslinking leads to defec

9 cadaverine (MDC), which binds to the enzyme (transamidase) active site of tissue transglutaminase (TG

10 Ala abolishes glutaminase and Gln-dependent transamidase activities of Glu-AdT (>300-fold), but reta

11 or ATP-gammaS hydrolysis and glutaminase and transamidase activities reveals tight coupling among the

12 ar to that with ATP, but without concomitant transamidase activity and with a very low level of ATP-g

13 Transamidase activity is inhibited by direct inhibitor b

14 The transamidase activity of transglutaminase 2 (TGase 2) is

15 The transamidase activity potential of factor XIII, measured

16 We recently showed that GTP binding, but not transamidase activity, is required for TG2-dependent can

17 g/GTPase activity, and the open conformation transamidase activity.

18 y at the TG2 transamidase site, inhibit both transamidase and GTP-binding activities.

19 zure onset than individuals with variants in transamidase and remodelling stage genes of the GPI-AP (

20 e that the interaction between a protein-GPI transamidase and the COOH-terminal GPI signal sequence p

21 me that catalyzes a large number of amidase, transamidase, and ester hydrolysis reactions.

22 also identify signal recognition by the GPI-transamidase as a potential step for selective small mol

23 or must first undergo cleavage by a putative transamidase between the omega and omega + 1 positions w

24 ons to an open conformation that exposes the transamidase catalytic site involved in protein-protein

25 n near the carboxyl terminus, and a putative transamidase cleavage site in the proprotein.

26 tachment 1) is an essential component of the transamidase complex along with PIGK, PIGS, PIGT, and PI

27 ts of the glycosylphosphatidylinositol (GPI) transamidase complex in human breast cancer.

28 These findings highlight the role of the transamidase complex in the development and function of

29 These results suggest that the GPI transamidase complex is composed of a group of proto-onc

30 osphatidylinositol glycan class U (PIG-U), a transamidase complex unit in the glycosylphosphatidylino

31 he ER-localized glycosylphosphatidylinositol transamidase complex, are retained in the ER.

32 it of the glycosylphosphatidylinositol (GPI)-transamidase complex, PIGK.

33 PIGK encodes a component of the GPI transamidase complex, which attaches the GPI anchor to p

34 identified subunits of the mammalian GPtdIns transamidase complex.

35 ee form of PIG-T, normally a part of the GPI transamidase complex.

36 Genetic studies with yeast indicate that the transamidase consists of a dynamic complex of at least t

37 ryl alkylating reagents, suggesting that the transamidase enzyme contains a functionally important su

38 rexpression of different subunits of the GPI transamidase, from strong suppression by Gpi8p and Gpi17

39 I) anchoring of proteins is catalyzed by GPI transamidase (GPIT), a multisubunit, endoplasmic reticul

40 Glycosylphosphatidylinositol (GPI) transamidase (GPIT), the enzyme that attaches GPI anchor

41 iple subunit enzyme complex known as the GPI transamidase (GPIT).

42 rocessed in the endoplasmic reticulum by GPI transamidase (GPIT).

43 reticulum membrane, and GPI-anchored by GPI transamidase (GPIT).

44 GPI-attachment signal can be modified by the transamidase irrespective of whether it is first release

45 ant K cells are defective in part of the GPI transamidase machinery.

46 r glycosylphosphatidylinositol (GPI):protein transamidase, metacaspase and separase, and their differ

47 gs with HDZ provide further evidence for the transamidase nature of the enzyme and also provide a sta

48 ed on the human glycosylphosphatidylinositol transamidase protein.

49 These results suggest the carboxy-terminal transamidase recognizes a more extended structure simila

50 blocked because inhibitor interaction at the transamidase site locks the protein in the extended/open

51 inhibited by direct inhibitor binding at the transamidase site, and GTP binding is blocked because in

52 and VA5, which react exclusively at the TG2 transamidase site, inhibit both transamidase and GTP-bin

53 These findings suggest that transamidase site-specific inhibitors can inhibit GTP bi

54 However, we were surprised that transamidase site-specific inhibitors reduce cancer stem

55 w that proproteins can be crosslinked to the transamidase subunit Gpi8p, as well as to ER proteins of

56 strate and one of the genetically identified transamidase subunits.

57 In addition to being a transamidase, TG undergoes a GTP-binding/GTPase cycle ev

58 r coordinated coupling of Gln hydrolysis and transamidase transition states during catalysis, and val

59 ach by isolating binders toward Sortase A, a transamidase which is required for virulence of Staphylo

60 s suggest that Gab1p is a subunit of the GPI transamidase with distinct relationships to other subuni