Inhibitory Effect of Copper on Cystathionine β-Synthase Activity: Protective Effect of an Analog of the Human Albumin N-Terminus

Author(s): David Bar-Or, Leonard T. Rael, Gregory W. Thomas, Jan P. Kraus

Journal Name: Protein & Peptide Letters

Volume 12 , Issue 3 , 2005

Become EABM
Become Reviewer


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

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2005
Page: [271 - 273]
Pages: 3
DOI: 10.2174/0929866053587048
Price: $65

Article Metrics

PDF: 3