ライフサイエンスコーパス: carboxypeptidase A

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1 ical zinc hydrolases such as thermolysin and carboxypeptidase A.

2 asis of an assumed mechanistic homology with carboxypeptidase A.

3 itive inhibition of catalysis for the enzyme carboxypeptidase A.

4 pK(a) of 6) from the active-site zinc ion of carboxypeptidase A.

5 cted Rubisco from loss of activity caused by carboxypeptidase A.

6 rHCII-CHis(6) was reversed by treatment with carboxypeptidase A.

7 ich is identical to the properties of bovine carboxypeptidase A.

8 development, including insulin, glucagon and carboxypeptidase A.

9 eir expression of serglycin proteoglycan and carboxypeptidase A.

10 el of aspartoacylase based on zinc dependent carboxypeptidase A.

11 that of zinc-dependent hydrolases related to carboxypeptidases A.

12 o and are not substrates for wild type human carboxypeptidases A.

13 tructure, 6-fold more reactive C terminus to carboxypeptidase A, 2-fold less binding of anti-SCP-2, a

14 competitive inhibitors, an inhibitor of the carboxypeptidase A and B family purified from potato tub

15 in place of Glu300 (equivalent to Glu270 of carboxypeptidase A and B).

16 d when ZGPpNA was replaced by substrates for carboxypeptidase A and B, chymotrypsin, subtilisin, and

17 e G2, Aeromonas proteolytica aminopeptidase, carboxypeptidase A and leucine aminopeptidase reveals a

18 lity of D-PEN to catalyze metal removal from carboxypeptidase A and other zinc proteases suggests a p

19 ology in mice, at least in part by releasing carboxypeptidase A and possibly other proteases, which c

20 scribed for other zinc metalloamidases, like carboxypeptidase A and thermolysin.

21 inc site are different from that observed in carboxypeptidase A and would predict a lower pKa for the

22 tifying protein targets of namalide selected carboxypeptidase A as the third highest scoring hit.

23 ogs containing l-Lys or l-allo-Ile inhibited carboxypeptidase A at submicromolar concentrations.

24 s that it bears little similarity to that of carboxypeptidase A, but instead resembles neurolysin and

25 The racemic amino acid was resolved by carboxypeptidase A-catalyzed hydrolysis of the N-trifluo

26 fference, we solved the crystal structure of carboxypeptidase A complexed with D-cysteine (D-Cys) at

27 by the cellular reduced folate carrier, with carboxypeptidase A (CPA), which can remove the blocking

28 ic extracts more than 80 years ago and named carboxypeptidase A (CPA; now known as CPA1).

29 modeling (periostin, POSTN), and mast cells (carboxypeptidase A, CPA3).

30 ethyl groups on the beta-carbon yet inhibits carboxypeptidase A (CPD) by a distinct mechanism: D-cyst

31 mast cell protease 1, cationic trypsinogen, carboxypeptidase A, IL-5, and phospholipase Cgamma.

32 is efficiently cleaved by the enzyme bovine carboxypeptidase A into fragments anisole, molecular nit

33 Experiments in which carboxypeptidase A is used to probe the lysozyme-induced

34 ric geometries markedly differ such that the carboxypeptidase A makes only Ndelta1 contacts, thermoly

35 Furthermore, serglycin, tryptase, and carboxypeptidase A messenger RNA transcripts were detect

36 PrMCTriad lacked mouse mast cell carboxypeptidase A (mMC-CPA) protein, required SCF for I

37 ouse mast-cell protease (mMCP)-4, mMCP-5 and carboxypeptidase A (mMC-CPA), even though they contained

38 5, the tryptase mMCP-6, and the exopeptidase carboxypeptidase A (mMC-CPA).

39 l Glu), but did not hydrolyse substrates for carboxypeptidase A or B (FAPP or FAAK, C-terminal Phe or

40 val of the C-terminal isoleucine (Ile152) by carboxypeptidase A or truncation by mutagenesis eliminat

41 The A. aegypti carboxypeptidase A promoter was used to express the IR R

42 nd acini generate immunoreactive insulin and carboxypeptidase A, respectively.

43 For example, carboxypeptidase A, thermolysin, and sonic hedgehog poss

44 ine (D-PEN) catalyzes zinc(II) transfer from carboxypeptidase A to chelators such as thionein and EDT

45 thiol group with N-ethyl-maleimide and using carboxypeptidase-A to stabilize the R-quaternary conform

46 m the well known crystal structure of bovine carboxypeptidase A, we have designed and synthesized nov

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