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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
5 the N-acylated substrate by an L-amino acid acylase and its subsequent oxidation by an FAD-dependent
6 to describe the roles and regulation of de-S-acylases and how extracellular signals drive dynamic (de
12 precursor mutant (Thr263Gly) of penicillin G acylase from Escherichia coli, which reveals that the sp
14 cetyl-L-alanine at 298.35K by porcine kidney acylase I (EC 3.5.1.14) was monitored by the heat releas
16 ine, and N-acetyl-L-phenylalanine by porcine acylase I in 0.1M phosphate buffer, which is inhibited b
18 openicillanic acid catalyzed by Penicillin G acylase in miniaturized stirred batch reactors or contin
20 lts reveal that ligand binding in penicillin acylase is facilitated by certain amino acid residues th
22 e report that SIRT2, a potent lysine defatty-acylase, is upregulated by the transcription factor CREB
25 inactivation mutant of tem25 encoding a (de)acylase, structurally elucidated, and then shown to be d
27 tructural protoxin, and lktC encodes a trans-acylase that adds fatty acid chains to internal lysine r
29 ant has been coupled with an enantiospecific acylase to give a preparative scale dynamic kinetic reso
31 neglecting acetate product inhibition of the acylase, values for k(cat) were up to a factor of 2.3 la
32 spired by the extraordinary selectivities of acylases, we envisioned the use of lipophilic oligopepti