1PJB

L-ALANINE DEHYDROGENASE

Summary for 1PJB

• Entry DOI: 10.2210/pdb1pjb/pdb
• Descriptor: L-ALANINE DEHYDROGENASE (2 entities in total)
• Functional Keywords: oxidoreductase, nad
• Biological source: Phormidium lapideum
• Total number of polymer chains: 1
• Total formula weight: 38592.26

Authors

Baker, P.J.,Sawa, Y.,Shibata, H.,Sedelnikova, S.E.,Rice, D.W. (deposition date: 1998-06-05, release date: 1999-06-08, Last modification date: 2024-02-14)

Primary citation

Baker, P.J.,Sawa, Y.,Shibata, H.,Sedelnikova, S.E.,Rice, D.W.
Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase.
Nat.Struct.Biol., 5:561-567, 1998

PubMed Abstract: 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.

PubMed: 9665169
DOI: 10.1038/817

Experimental method

X-RAY DIFFRACTION (2.1 Å)