Protein Family Models

Homoserine dehydrogenase (HSD) coordinates a critical branch point of the metabolic pathway that leads to the synthesis of bacterial cell-wall components such as L-lysine and m-DAP in addition to other amino acids such as L-threonine, L-methionine and L-isoleucine. The enzyme structure consists of three domains. This entry represents the C-terminal domain that folds into a four-stranded antiparallel beta-sheet with two alpha-helices packed on one side [1]. Paper describing PDB structure 4pg4. [1]. 25945586. Structural basis for the catalytic mechanism of homoserine dehydrogenase. Navratna V, Reddy G, Gopal B;. Acta Crystallogr D Biol Crystallogr. 2015;71:1216-1225. (from Pfam)

Date:

2024-10-16

This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

homoserine dehydrogenase catalyzes the conversion from L-homoserine and NAD(P)(+) to L-aspartate 4-semialdehyde and NAD(P)H

Date:

2023-03-03

Catalyzes the formation of L-aspartate 4-semialdehyde from L-homoserine

Date:

2021-08-24