Journal
BIOCHEMISTRY
Volume 39, Issue 51, Pages 15668-15673Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi0022184
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- NIDDK NIH HHS [DK 28607] Funding Source: Medline
- NIGMS NIH HHS [GM 42025] Funding Source: Medline
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Lysine 2,3-aminomutase (KAM) belongs to a class of enzymes that use FeS clusters and S-adenosyl-L-methionine to initiate radical-dependent chemistry. Selenium K-edge X-ray absorption spectroscopic analysis of KAM poised at various stages of catalysis, in the presence of selenomethionine or Se-adenosyl-L-selenomethionine, reveals that the cofactor is cleaved only in the presence of dithionite and the substrate analogue trans-4,5-dehydrolysine. A new Fourier transform peak at 2.7 Angstrom, assigned as a Se-Fe interaction, appears concomitant with this cleavage. This is the first demonstration of a direct interaction of S-adenosyl-L-methionine, or its cleavage products, with the FeS cluster in this class of enzymes.
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