Abstract
Copper was added to truncated, recombinant cystathionine beta-synthase (CBS), and the enzyme activity was assessed by measuring the production of cystathionine. 10 microM copper significantly decreased CBS activity by 50% while 25 microM 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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Albumins / chemistry*
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Albumins / metabolism*
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Copper / metabolism*
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Cystathionine / metabolism
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Cystathionine beta-Synthase / antagonists & inhibitors*
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Cystathionine beta-Synthase / genetics
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Cystathionine beta-Synthase / metabolism*
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Homocysteine / metabolism
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Humans
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Recombinant Proteins / antagonists & inhibitors
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
Substances
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Albumins
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Recombinant Proteins
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Homocysteine
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Cystathionine
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Copper
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Cystathionine beta-Synthase