1A4Z

ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA COMPLEX WITH NAD (REDUCED) AND SAMARIUM (III)

Summary for 1A4Z

• Entry DOI: 10.2210/pdb1a4z/pdb
• Descriptor: ALDEHYDE DEHYDROGENASE, SAMARIUM (III) ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: oxidoreductase, alcohol metabolism, aldehyde oxidation, alpha/beta domain, dehydrogenase
• Biological source: Bos taurus (cattle)
• Cellular location: Mitochondrion matrix: P20000
• Total number of polymer chains: 4
• Total formula weight: 221234.00

Authors

Steinmetz, C.G.,Hurley, T.D. (deposition date: 1998-02-10, release date: 1998-04-08, Last modification date: 2024-02-07)

Primary citation

Steinmetz, C.G.,Xie, P.,Weiner, H.,Hurley, T.D.
Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion.
Structure, 5:701-711, 1997

PubMed Abstract: The single genetic factor most strongly correlated with reduced alcohol consumption and incidence of alcoholism is a naturally occurring variant of mitochondrial aldehyde dehydrogenase (ALDH2). This variant contains a glutamate to lysine substitution at position 487 (E487K). The E487K variant of ALDH2 is found in approximately 50% of the Asian population, and is associated with a phenotypic loss of ALDH2 activity in both heterozygotes and homozygotes. ALDH2-deficient individuals exhibit an averse response to ethanol consumption, which is probably caused by elevated levels of blood acetaldehyde. The structure of ALDH2 is important for the elucidation of its catalytic mechanism, to gain a clear understanding of the contribution of ALDH2 to the genetic component of alcoholism and for the development of specific ALDH2 inhibitors as potential drugs for use in the treatment of alcoholism.

PubMed: 9195888
DOI: 10.1016/S0969-2126(97)00224-4

Experimental method

X-RAY DIFFRACTION (2.75 Å)