Inhibitory effect of copper on cystathionine beta-synthase activity: protective effect of an analog of the human albumin N-terminus.
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.
Bar-Or
David
D
Department of Trauma Research and Trauma Services, Swedish Medical Center, 501 E. Hampden Avenue, Englewood, CO 80113, USA.
Rael
Leonard T
LT
Thomas
Gregory W
GW
Kraus
Jan P
JP
D000418:Albumins / Q000737:chemistry* / Q000378:metabolism*; D003300:Copper / Q000378:metabolism*; D003540:Cystathionine / Q000378:metabolism; D003541:Cystathionine beta-Synthase / Q000037:antagonists & inhibitors* / Q000235:genetics / Q000378:metabolism*; D006710:Homocysteine / Q000378:metabolism; D006801:Humans; D011994:Recombinant Proteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism
D000418:Albumins; D011994:Recombinant Proteins; D006710:Homocysteine; D003540:Cystathionine; D003300:Copper; D003541:Cystathionine beta-Synthase