Abstract
Copper was added to truncated, recombinant cystathionine β-synthase (CBS), and the enzyme activity was assessed by measuring the production of cystathionine. 10microM copper significantly decreased CBS activity by 50% while 25microM copper decreased CBS activity by 70%. This inhibition was negated when an analog of the N-terminus of human albumin, Asp-Ala-His-Lys (DAHK), a strong transition metal binding peptide, was added. The use of copper chelators could significantly reduce in vivo homocysteine levels.
Keywords: cystathionine synthase, inhibition, copper, chelation, homocysteine
Protein & Peptide Letters
Title: Inhibitory Effect of Copper on Cystathionine β-Synthase Activity: Protective Effect of an Analog of the Human Albumin N-Terminus
Volume: 12 Issue: 3
Author(s): David Bar-Or, Leonard T. Rael, Gregory W. Thomas and Jan P. Kraus
Affiliation:
Keywords: cystathionine synthase, inhibition, copper, chelation, homocysteine
Abstract: Copper was added to truncated, recombinant cystathionine β-synthase (CBS), and the enzyme activity was assessed by measuring the production of cystathionine. 10microM copper significantly decreased CBS activity by 50% while 25microM copper decreased CBS activity by 70%. This inhibition was negated when an analog of the N-terminus of human albumin, Asp-Ala-His-Lys (DAHK), a strong transition metal binding peptide, was added. The use of copper chelators could significantly reduce in vivo homocysteine levels.
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Cite this article as:
Bar-Or David, Rael T. Leonard, Thomas W. Gregory and Kraus P. Jan, Inhibitory Effect of Copper on Cystathionine β-Synthase Activity: Protective Effect of an Analog of the Human Albumin N-Terminus, Protein & Peptide Letters 2005; 12 (3) . https://dx.doi.org/10.2174/0929866053587048
DOI https://dx.doi.org/10.2174/0929866053587048 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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