ライフサイエンスコーパス: phosphohistidine

1 t, 13.5 ppm) to the phosphoryl moiety of the phosphohistidine.

2 hoamino acid analysis showed the presence of phosphohistidine.

3 analogy to the NMR properties of the known 3-phosphohistidine.

4 ino acid found after alkaline hydrolysis was phosphohistidine.

5 nstants consistent with published values for phosphohistidine.

6 mblance to other enzymes known to contain N3-phosphohistidine.

7 rylated residue co-migrated with authentic 1-phosphohistidine.

8 e nitrogens can be phosphorylated, forming 1-phosphohistidine (1-pHis) or 3-phosphohistidine (3-pHis)

9 ed, forming 1-phosphohistidine (1-pHis) or 3-phosphohistidine (3-pHis).

10 osphoenzyme intermediate was consistent with phosphohistidine and the only radioactive amino acid fou

11 nd phosphotyrosine-containing proteins and 3-phosphohistidine- and phospholysine-containing amino aci

12 Upon formation of the phosphohistidine at His-258, the 13C and 1H resonances o

13 the phosphoaccepting histidine and from the phosphohistidine back to ADP seem to be essentially equa

14 using synthetic peptides, we conclude that 3-phosphohistidine cannot replace phosphotyrosine in confe

15 ced by glutamine, were phosphorylated by the phosphohistidine-containing phosphocarrier protein (HPr-

16 n the protein complex involving a 21-aa-long phosphohistidine-containing segment of the alpha subunit

17 transition-state (TS) analogue of enzymatic phosphohistidine dephosphorylation as an amino acid buil

18 reveals a three-domain molecule in which the phosphohistidine domain is flanked by the nucleotide and

19 ilitated by two conformational states of the phosphohistidine domain.

20 no acid that acts as a nucleophile forming a phosphohistidine-enzyme intermediate, and His(119) would

21 s limited overall homology to members of the phosphohistidine family of phosphatases.

22 of a fairly strong hydrogen bond to the same phosphohistidine implies that hydrolysis of the covalent

23 The secreted enzyme forms a phosphohistidine intermediate and shows broad specificit

24 -phosphate during formation of the transient phosphohistidine intermediate at the N3' of His-258, thi

25 HMQC spectra acquired from the transient N3' phosphohistidine intermediate complex in the wild-type e

26 This five-coordinate phosphohistidine intermediate energetically exists betwe

27 ray crystal structure of the five-coordinate phosphohistidine intermediate from Streptomyces sp .

28 The phosphohistidine intermediate is characterized by two hy

29 Attempts to detect a phosphohistidine intermediate with the H256A mutant enzy

30 ydrolysis involved the formation of a stable phosphohistidine intermediate.

31 tose-2,6-bisphosphate, and subsequently, the phosphohistidine intermediate.

32 xylamine, suggesting that the enzyme forms a phosphohistidine intermediate.

33 The phosphohistidine is stabilized in the His432Arg structur

34 ohistidine phosphatase in mammals, regulates phosphohistidine levels of several proteins including th

35 Furthermore, it has been suggested that phosphohistidine might substitute for phosphotyrosine in

36 de indicate a covalent H247-BeF(3)(-) as the phosphohistidine mimic.

37 Still, the detection of phosphohistidine (pHis) in the proteome has remained dif

38 m the intrinsic instability and isomerism of phosphohistidine (pHis).

39 Phosphohistidine phosphatase 1 (PHPT1), the only known p

40 The peptides are designed as inhibitors of phosphohistidine phosphatase and as a pull-down probe fo

41 tidine phosphatase 1 (PHPT1), the only known phosphohistidine phosphatase in mammals, regulates phosp

42 erate mutase family 5 (PGAM5) functions as a phosphohistidine phosphatase that specifically associate

43 d as a pull-down probe for identification of phosphohistidine phosphatases, respectively.

44 of the experimentally observed ''dead-end'' phosphohistidine product (PDB Code = 1V0W ).

45 favorability of the in vitro four-coordinate phosphohistidine product.

46 (31)P NMR spectra were not consistent with a phosphohistidine residue.

47 Formation of phosphohistidine residues in proteins has been found in

48 (i.e., His760), which was proposed to form a phosphohistidine species during catalysis.

49 sphotransfer event; however, analysis of the phosphohistidine species is made difficult by the instab

50 ition to its activity on phosphotyrosine and phosphohistidine substrates, Tdp1 also possesses a limit

51 We have analyzed the ability of 3-phosphohistidine to associate with the known phosphotyro

52 ohistidine even when they do not form stable phosphohistidines using the natural substrate ATP.

53 utant resting enzymes were reversed when the phosphohistidine was formed, generating spectra very sim