Structural highlights
Function
ADH1E_HORSE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Atomic (1 A) resolution x-ray structures of horse liver alcohol dehydrogenase in complex with NADH revealed the formation of an adduct in the active site between a metal-bound water and NADH. Furthermore, a pronounced distortion of the pyridine ring of NADH was observed. A series of quantum chemical calculations on the water-nicotinamide adduct showed that the puckering of the pyridine ring in the crystal structures can only be reproduced when the water is considered a hydroxide ion. These observations provide fundamental insight into the enzymatic activation of NADH for hydride transfer.
On the enzymatic activation of NADH.,Meijers R, Morris RJ, Adolph HW, Merli A, Lamzin VS, Cedergren-Zeppezauer ES J Biol Chem. 2001 Mar 23;276(12):9316-21. Epub 2000 Dec 28. PMID:11134046[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Meijers R, Morris RJ, Adolph HW, Merli A, Lamzin VS, Cedergren-Zeppezauer ES. On the enzymatic activation of NADH. J Biol Chem. 2001 Mar 23;276(12):9316-21. Epub 2000 Dec 28. PMID:11134046 doi:10.1074/jbc.M010870200
