ライフサイエンスコーパス: Cys-Gly

1 k is a cyclic nine-amino acid peptide LyP-1 (Cys-Gly-Asn-Lys-Arg-Thr-Arg-Gly-Cys) that binds to the s

2 ProMMP-26 has the unique Pro-His(81)-Cys-Gly-Xaa-Xaa-Asp cysteine-switch motif that discrimin

3 Phe-His cleavage upstream of the Pro-His(81)-Cys-Gly-Xaa-Xaa-Asp motif induced the proteolytic activi

4 Here, we report that the Pro-His(81)-Cys-Gly-Xaa-Xaa-Asp motif is not functional in proMMP-26

5 ug1p has earlier been shown to function as a Cys-Gly-specific dipeptidase.

6 2 (Xaa = Phe, His, Tyr, Gly, and Thr) and Ac-Cys-Gly-Pro-Cys-NH2 and the peptide Ac-Ala-Gly-Pro-Ala-N

7 The peptides Ac-Cys-Pro-Xaa-Cys-NH2 and Ac-Cys-Gly-Pro-Cys-NH2 are model compounds for proline-cont

8 he ferredoxin consensus sequence Cys-Ile-Ala-Cys-Gly-Ala-Cys to bind the Fe(4)S(4) cluster.

9 ntains neither an Ala-Gly nor an alternative Cys-Gly dipeptide cleavage site anywhere in its linker s

10 e cleavage of glutathione into glutamate and Cys-Gly.

11 ystalysin could not catalyze glutathione and Cys-Gly degradation in vitro.

12 a 26-membered ring (analogue 1, H-Tyr-Val-c[Cys-Gly-His-Phe-Arg-Trp-Cys]-Arg-Phe-Gly-NH(2) with Gly(

13 ly-Cys-Sec-Gly, Ser-Cys-Cys-Ser, and Gly-Cys-Cys-Gly, respectively.

14 surface-exposed omega loop the sequence Cys-Cys-Gly-Pro-Cys-Cys, which binds specifically to a biars

15 catalyze the hydrolysis of cysteinylglycine (Cys-Gly) with the same kinetics as the native protein.

16 e and S-nitrosoglutathione to the dipeptide (Cys-Gly), which is then transported into the bacterium b

17 the C-terminal cysteine residue within each Cys-Gly-His-Cys active site is replaced with alanine.

18 The activity of CGase for Cys-Gly is optimum at pH 7.3 and is enhanced by Mn2+, Co

19 The binding site for Cys-Gly-3M3SH was predicted using modeling, which sugges

20 ived peptides, such as glutathione (gammaGlu-Cys-Gly), and anilides, such as gamma-glutamyl-7-amido-4

21 ates, namely, reduced glutathione (gamma-Glu-Cys-Gly) and the carrier protein, bovine serum albumin (

22 lycine carboxylate of glutathione (gamma-Glu-Cys-Gly) and the opposing hydrolysis of this amide bond.

23 hiol tripeptide, glutathione (GSH, gamma-Glu-Cys-Gly), and a diverse family of cysteine-rich low mole

24 lycine carboxylate of glutathione (gamma-Glu-Cys-Gly), with net hydrolysis of ATP.

25 and displacement with glutathione (gamma-Glu-Cys-Gly, GSH).

26 An endogenous Tc chelation site (Ala-Gly-Gly-Cys-Gly-His) was added to the N-terminus of annexin V to

27 Cysteinyl glycine (Cys-Gly) was also catabolized by the bacteria, yielding

28 ed substrate for the T. denticola protein is Cys-Gly (k cat/Km of 8.2 microm(-1) min(-1)) not l-Leu-p

29 ment deposition in a manner dependent on its Cys-Gly-Pro-Cys active site.

30 egradation was found to be restricted to its Cys-Gly peptidase activity, which functioned downstream

31 As the secreted odor precursor Cys-Gly-3M3SH contains a dipeptide, yet the final enzyme

32 amily PepV peptidase (ShPepV) as the primary Cys-Gly-3M3SH dipeptidase.

33 ue Ni-hook structural motif (His-Cys-X-X-Pro-Cys-Gly-X-Tyr) provides almost all interactions critical

34 into secretory vesicles, deglutamylated to S-Cys-Gly-3M3SH thiol, and exuded to skin surface.

35 rase (PDI) utilizes the active site sequence Cys-Gly-His-Cys (CGHC; E degrees ' = -180 mV) to effect

36 oxin (Trx) utilizes the active site sequence Cys-Gly-Pro-Cys (CGPC; E degrees ' = -270 mV) to effect

37 Here, the Cys-Gly-Cys-NH(2) (CGC) peptide is shown to have a disul

38 of the energy liberated upon cleavage of the Cys-Gly bonds of the gamma-Glu-Cys donors in the first p

39 ved into the vacuole and then metabolized to Cys-Gly-mBB and Cys-mBB in that order.

40 n containing the thioredoxin active site Trp-Cys-Gly-Pro-Cys that is localized to the mitochondria by