Protein Family Models

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

This entry represents the C-terminal domain of aspartate dehydrogenases that belong to a unique class of amino acid dehydrogenases. The structure of Thermotoga maritima TM1643 has been found to contain an N-terminal Rossmann fold domain (which binds the NAD(P)+ cofactor) and a C-terminal alpha/beta domain [1]. Enzymatic characterisation of TM1643 revealed that it possesses NAD or NADP-dependent dehydrogenase activity toward L-aspartate but no aspartate oxidase activity [1]. Members of this group share some structural similarity to several other NAD(P)+-dependent oxidoreductases, including inositol 1-phosphate synthase, dihydrodipicolinate reductase, and ASA-DH [1]. It has been proposed that in Thermotoga maritima, TM1643 catalyses the first reaction of de novo biosynthesis of NAD from aspartate, and it produces iminoaspartate required for this pathway. [1]. 12496312. Aspartate dehydrogenase, a novel enzyme identified from. structural and functional studies of TM1643.. Yang Z, Savchenko A, Yakunin A, Zhang R, Edwards A, Arrowsmith. C, Tong L;. J Biol Chem. 2003;278:8804-8808. (from Pfam)

Date:

2024-08-14

aspartate dehydrogenase specifically catalyzes the NAD(P)-dependent dehydrogenation of L-aspartate to iminoaspartate, which decomposes to oxaloacetate and ammonia in solution, in the first step of NAD biosynthesis from aspartate

Date:

2019-07-23

Date:

2020-10-26

Date:

2021-11-04