| Type: | Domain | Name: | Allosteric substrate binding domain |
| Description: | This entry represents a domain found at the N terminus of the L-serine dehydratases beta chain and in some but not all D-3-phosphoglycerate dehydrogenases (PGDH) and related enzymes. This domain covers the intervening domain (also known as the allosteric substrate binding domain) found in D-3-phosphoglycerate dehydrogenase (PGDH) from Mycobacterium tuberculosis []. The intervening domain, which serves as an anion binding site, is located between the substrate-binding domain and the regulatory domain (L-serine binding) [, , ]. The intervening domain may be an allosteric site for the control of enzyme activity []. Interestingly, the intervening domain is found in PGDH from bacteria such as Mycobacterium, Bacillus subtilis, Corynebacterium, plants such as Arabidopsis, and higher order eukaryotes, including mammals. This domain is not present in the PGDH from E. coli and some lower eukaryotes, such as yeast and Neurospora []. L-serine dehydratase is found as a heterodimer of alpha and beta chain or as a fusion of the two chains in a single protein. This domain is found in the beta chain. Similar to PGDH, this domain may serve as a noncatalytic site for L-serine []. | Short Name: | ASB_dom |
