CATH Classification

Domain Context

CATH Clusters

Superfamily Dihydrodipicolinate Reductase; domain 2
Functional Family Bifunctional aspartokinase/homoserine dehydrogenase

Enzyme Information

1.1.1.3
Homoserine dehydrogenase.
based on mapping to UniProt P31116
L-homoserine + NAD(P)(+) = L-aspartate 4-semialdehyde + NAD(P)H.
-!- The enzyme from Saccharomyces cerevisiae acts most rapidly with NAD(+); the Neurospora enzyme with NADP(+). -!- The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 2.7.2.4.

UniProtKB Entries (1)

P31116
DHOM_YEAST
Saccharomyces cerevisiae S288C
Homoserine dehydrogenase

PDB Structure

PDB 1EBF
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases.
DeLaBarre, B., Thompson, P.R., Wright, G.D., Berghuis, A.M.
Nat.Struct.Biol.