The effect of N-terminal acetylation and the inhibition activity of acetylated enkephalins on the aminopeptidase M-catalyzed hydrolysis of enkephalins☆
Identifieur interne : 001939 ( Main/Exploration ); précédent : 001938; suivant : 001940The effect of N-terminal acetylation and the inhibition activity of acetylated enkephalins on the aminopeptidase M-catalyzed hydrolysis of enkephalins☆
Auteurs : Dhammika S. Jayawardene [États-Unis] ; Chhabil Dass [États-Unis]Source :
- Peptides [ 0196-9781 ] ; 1999.
English descriptors
- KwdEn :
- Teeft :
- Academic press, Acetylated, Acetylated enkephalins, Acetylated methionine enkephalin, Acetylation, Amino acids, Aminopeptidase, Aminopeptidase hydrolysis, Aminopeptidases, Ammonium acetate, Ammonium acetate solution, Biochem pharmacol, Chromatogram, Chromatographic conditions, Competitive inhibitors, Control experiment, Corresponding values, Current chromatograms, Das, Dass peptides, Degradation, Different concentrations, Electrospray ionization mass spectrometry, Elsevier science, Enkephalin, Enzymatic degradation, Enzyme, Enzyme kinetics, Enzyme reaction, Ggfm, High performance, Hplc, Human plasma, Hydrolysis, Hydrolysis reaction, Incubation period, Inhibition, Inhibition activity, Inhibitor, Ionization mass spectrometry, Jayawardene, Kinetic constants, Leucine, Leucine enkephalin, Methionine enkephalin, Mobile phase, Molecular ions, Molecular pharmacology, Nida research monograph series, Noninhibited, Noninhibited reaction, Opioid, Opioid peptides, Opoid peptides, Original amount, Peak area, Peak areas, Peptide, Porcine aminopeptidase, Present study, Proteolytic, Proteolytic stability, Reaction mixture, Reaction products, Reaction rate, Retention times, Sequential removal, Spectrometry, Substrate concentration, Taylor francis, Time interval, Uncompetitive inhibition, Vmax, Vmax values, Zinc metalloproteases.
Abstract
Abstract: High performance liquid chromatography and high performance liquid chromatography/electrospray ionization-mass spectrometry were used to study the effect of N-terminal acetylation and the inhibition activity of acetylated enkephalins on the aminopeptidase M (EC 3.4.11.2)-catalyzed hydrolysis of methionine (Met-enk) and leucine enkephalins (Leu-enk). Acetylation imparts a significant enhancement in the proteolytic stability of these two peptides. After 30 min of the reaction, <10% of both acetylated enkephalins was hydrolyzed. In an 8-h incubation period, only a maximum of 54% acetylated (Ac)-Met-enk and 38% Ac-Leu-enk was hydrolyzed. Vmax and Km [infi] for the degradation of Ac-Met-enk were 1.4 nmol/min/50 ng and 2.2 mM, respectively. The corresponding values for the reaction of Ac-Leu-enk were 0.5 nmol/min/50 ng and 0.9 mM. Also, the aminopeptidase M activity on Met-enk can be inhibited in the presence of Ac-Met-enk, which acts as a mixed-type inhibitor with the inhibition constant (Ki) of 1 × 10−3 M.
Url:
DOI: 10.1016/S0196-9781(99)00089-3
Affiliations:
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Acetylation imparts a significant enhancement in the proteolytic stability of these two peptides. After 30 min of the reaction, <10% of both acetylated enkephalins was hydrolyzed. In an 8-h incubation period, only a maximum of 54% acetylated (Ac)-Met-enk and 38% Ac-Leu-enk was hydrolyzed. Vmax and Km [infi] for the degradation of Ac-Met-enk were 1.4 nmol/min/50 ng and 2.2 mM, respectively. The corresponding values for the reaction of Ac-Leu-enk were 0.5 nmol/min/50 ng and 0.9 mM. Also, the aminopeptidase M activity on Met-enk can be inhibited in the presence of Ac-Met-enk, which acts as a mixed-type inhibitor with the inhibition constant (Ki) of 1 × 10−3 M.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Tennessee</li></region></list><tree><country name="États-Unis"><region name="Tennessee"><name sortKey="Jayawardene, Dhammika S" sort="Jayawardene, Dhammika S" uniqKey="Jayawardene D" first="Dhammika S" last="Jayawardene">Dhammika S. Jayawardene</name></region><name sortKey="Dass, Chhabil" sort="Dass, Chhabil" uniqKey="Dass C" first="Chhabil" last="Dass">Chhabil Dass</name><name sortKey="Dass, Chhabil" sort="Dass, Chhabil" uniqKey="Dass C" first="Chhabil" last="Dass">Chhabil Dass</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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