Abstract:
:The final step in the biosynthesis of nicotinamide-adenine dinucleotide, a major coenzyme in cellular redox reactions and involved in intracellular signaling, is catalyzed by the enzyme nicotinamide mononucleotide adenylyltransferase (NMNAT). The X-ray structure of human NMNAT in complex with nicotinamide mononucleotide was solved by the single-wavelength anomalous dispersion method at a resolution of 2.9 A. Human NMNAT is a symmetric hexamer whose subunit is formed by a large six-stranded parallel beta-sheet with helices on both sides. Human NMNAT displays a different oligomerization compared to the archaeal enzyme. The protein-nicotinamide mononucleotide interaction pattern provides insight into ligand binding in the human enzyme.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Werner E,Ziegler M,Lerner F,Schweiger M,Heinemann Udoi
10.1016/s0014-5793(02)02556-5keywords:
subject
Has Abstractpub_date
2002-04-10 00:00:00pages
239-44issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302025565journal_volume
516pub_type
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