Structural highlights
Function
O52942_PHOLP
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
The structure of the hexameric L-alanine dehydrogenase from Phormidium lapideum reveals that the subunit is constructed from two domains, each having the common dinucleotide binding fold. Despite there being no sequence similarity, the fold of alanine dehydrogenase is closely related to that of the family of D-2-hydroxyacid dehydrogenases, with a similar location of the active site, suggesting that these enzymes are related by divergent evolution. L-alanine dehydrogenase and the 2-hydroxyacid dehydrogenases also use equivalent functional groups to promote substrate recognition and catalysis. However, they are arranged differently on the enzyme surface, which has the effect of directing opposite faces of the keto acid to the dinucleotide in each case, forcing a change in absolute configuration of the product.
Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase.,Baker PJ, Sawa Y, Shibata H, Sedelnikova SE, Rice DW Nat Struct Biol. 1998 Jul;5(7):561-7. PMID:9665169[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Baker PJ, Sawa Y, Shibata H, Sedelnikova SE, Rice DW. Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase. Nat Struct Biol. 1998 Jul;5(7):561-7. PMID:9665169 doi:http://dx.doi.org/10.1038/817
