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 1Q7G
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Enzyme assisted suicide: Molecular basis for the antifungal activity of 5-hydroxy-4-oxonorvaline by potent inhibition of homoserine dehydrogenase
Jacques, S.L., Mirza, I.A., Ejim, L., Koteva, K., Hughes, D.W., Green, K., Kinach, R., Honek, J.F., Lai, H.K., Berghuis, A.M., Wright, G.D.
Chem.Biol.
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