1LEH

LEUCINE DEHYDROGENASE FROM BACILLUS SPHAERICUS

Summary for 1LEH

Entry DOI	10.2210/pdb1leh/pdb
Descriptor	LEUCINE DEHYDROGENASE (2 entities in total)
Functional Keywords	oxidoreductase
Biological source	Lysinibacillus sphaericus
Total number of polymer chains	2
Total formula weight	78172.45
Authors	Baker, P.J.,Turnbull, A.P.,Sedelnikova, S.E.,Stillman, T.J.,Rice, D.W. (deposition date: 1995-06-09, release date: 1996-12-23, Last modification date: 2024-02-14)
Primary citation	Baker, P.J.,Turnbull, A.P.,Sedelnikova, S.E.,Stillman, T.J.,Rice, D.W. A role for quaternary structure in the substrate specificity of leucine dehydrogenase. Structure, 3:693-705, 1995 Cited by PubMed Abstract: Glutamate, phenylalanine and leucine dehydrogenases catalyze the NAD(P)(+)-linked oxidative deamination of L-amino acids to the corresponding 2-oxoacids, and sequence homology between these enzymes clearly indicates the existence of an enzyme superfamily related by divergent evolution. We have undertaken structural studies on a number of members of this family in order to investigate the molecular basis of their differential amino acid specificity. PubMed: 8591046 DOI: 10.1016/S0969-2126(01)00204-0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation