ライフサイエンスコーパス: acylase

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1 was prepared and resolved by porcine kidney acylase.

2 applicable to the characterization of other acylases.

3 nas aeruginosa, as a template to generate an acylase able to effectively hydrolyze C8-HSL, the major

4 It also exhibits an acylase activity, capable of deacylating N-acetyl-Met-Le

5 the N-acylated substrate by an L-amino acid acylase and its subsequent oxidation by an FAD-dependent

6 study of the substrate specificity of other acylases and peptidases.

7 stances, including vitamin B(12), penicillin acylase, and amylases.

8 trates the effectiveness of quorum-quenching acylases as potential novel antimicrobial drugs.

9 The crystal structure of penicillin G acylase from Escherichia coli has been determined to a r

10 precursor mutant (Thr263Gly) of penicillin G acylase from Escherichia coli, which reveals that the sp

11 cetyl-L-alanine at 298.35K by porcine kidney acylase I (EC 3.5.1.14) was monitored by the heat releas

12 ine, and N-acetyl-L-phenylalanine by porcine acylase I in 0.1M phosphate buffer, which is inhibited b

13 This protein was identified as the N-acylase IA (or N(alpha)-acyl-l-amino acid amidohydrolase

14 openicillanic acid catalyzed by Penicillin G acylase in miniaturized stirred batch reactors or contin

15 Penicillin G acylase is a periplasmic protein, cytoplasmically expres

16 lts reveal that ligand binding in penicillin acylase is facilitated by certain amino acid residues th

17 Since the acylase is thermally stable and the pH of the phosphate

18 The enzyme penicillin acylase (penicillin amidohydrolase EC 3.5.1.11) catalyse

19 inactivation mutant of tem25 encoding a (de)acylase, structurally elucidated, and then shown to be d

20 tructural protoxin, and lktC encodes a trans-acylase that adds fatty acid chains to internal lysine r

21 For penicillin and cephalosporin acylases, this discrepancy between structure and functio

22 ant has been coupled with an enantiospecific acylase to give a preparative scale dynamic kinetic reso

23 neglecting acetate product inhibition of the acylase, values for k(cat) were up to a factor of 2.3 la

24 spired by the extraordinary selectivities of acylases, we envisioned the use of lipophilic oligopepti

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