Publication Date:
1984-11-23
Description:
X-ray analysis of the free-acid crystal form of the coenzyme nicotinamide adenine dinucleotide (NAD+) revealed a conformational difference between the free NAD+ molecule and one bound in enzymes or complexed to Li+ ions. The pyrophosphate group showed asymmetry in the phosphate-oxygen bonds of the phosphate-oxygen-phosphate link; this bond at the nicotinamide side of the link is longer than that at the adenosine side by 0.04 angstrom. The crystal structure showed a novel intermolecular stacking of adenine and water molecules on opposite sides of nicotinamide that gives rise to a nicotinamide sandwich.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parthasarathy, R -- Fridey, S M -- GM-24864/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 23;226(4677):969-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6239374" target="_blank"〉PubMed〈/a〉
Keywords:
Alcohol Dehydrogenase
;
Alcohol Oxidoreductases/metabolism
;
Animals
;
Geobacillus stearothermophilus/enzymology
;
Glyceraldehyde-3-Phosphate Dehydrogenases/metabolism
;
L-Lactate Dehydrogenase/metabolism
;
Liver/enzymology
;
Malate Dehydrogenase/metabolism
;
Models, Molecular
;
Molecular Conformation
;
*NAD/metabolism
;
Nephropidae
;
Niacinamide
;
Protein Binding
;
X-Ray Diffraction
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
