ライフサイエンスコーパス: leader peptidase

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1 scence resonance energy transfer for E. coli leader peptidase.

2 d for stop-transfer segments engineered into leader peptidase.

3 double-spanning protein that is derived from leader peptidase.

4 Escherichia coli leader peptidase, an integral membrane protein, is respo

5 ellular protein secretion, in its roles as a leader peptidase and MTase.

6 Lys96 which were differentially affected in leader peptidase and N-methyltransferase function were c

7 ted with bovine trypsin and Escherichia coli leader peptidase and subsequently applied to determine t

8 eavage first between residues 68 and 69, via leader peptidase, and next between residues 441 and 442.

9 genes: pilD, a homologue of type IV prepilin leader peptidases; and pilG, pilH and pilI, which have n

10 t and its function for Pf3 coat and possibly leader peptidase are genetically separable and suggest t

11 strate can be cleaved effectively by E. coli leader peptidase as detected by both HPLC and fluorescen

12 nted the processing of the pVIII pro-coat by leader peptidase at the inner membrane of the Escherichi

13 by propilin insertion leads to processing by leader peptidase B to generate the 7-kDa peptide, which

14 t the nonpermissive temperature in a LepBts (leader peptidase B) host, propilin processing was inhibi

15 he lysine modifier maleic anhydride inhibits leader peptidase by reacting with lysine 145.

16 usly that the first transmembrane segment of leader peptidase can function to translocate the polar a

17 more typical signal peptide with a predicted leader peptidase cleavage site after the amino acid at p

18 orescent peptide substrate incorporating the leader peptidase cleavage site of maltose binding protei

19 lso formed in a pilD mutant, which lacks the leader peptidase enzyme, demonstrating that the leader p

20 hesis that the lysine at the 145-position of leader peptidase functions as the active site general ba

21 an Escherichia coli mutant defective in its leader peptidase gene.

22 cursor protein with a putative 24-amino-acid leader peptidase I signal sequence.

23 cannot be processed in vitro by the purified leader peptidase I.

24 mino-acid signal peptide encoding a putative leader peptidase II cleavage site, indicating that the 4

25 at protein is blocked, and the Sec-dependent leader peptidase is inhibited at the nonpermissive tempe

26 A model of the active site region of leader peptidase is presented based on the structure of

27 E. coli UmuD', and a mechanism for bacterial leader peptidase is proposed.

28 ted transmembrane domain (TMD) followed by a leader peptidase (Lep) reporter tag, as analyzed by the

29 at the central residue of a TM helix of the Leader peptidase might reside close to the interface and

30 ctivity can be restored to an inactive K145C leader peptidase mutant by reacting it with 2-bromoethyl

31 ed to restore activity to the inactive K145C leader peptidase mutant.

32 contrast, inactivation of pilD (encoding the leader peptidase) or pilC (encoding a protein required f

33 We find that leader peptidase processes the pre-protein substrate, pr

34 ane insertion of the Sec-independent procoat-leader peptidase protein.

35 This leader peptidase removes specific octapeptides from the

36 iberated upon cleavage of the peptide by the leader peptidase, resulting in increased fluorescence th

37 ngle-span model membrane proteins based upon leader peptidase that determines whether the proteins in

38 he membrane insertion of the M13 procoat and leader peptidase that were previously shown to depend on

39 ential lysine 145 in the activity of E. coli leader peptidase, we have combined site-directed mutagen

40 Pf3 phage coat protein and the Sec-dependent leader peptidase were not strongly inhibited at the rest

41 Escherichia coli leader peptidase, which catalyzes the cleavage of signal

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