EC Number   |
Subunits |
Reference |
|---|
   1.2.1.30 | ? |
x * 128300, deduced from gene sequence, x * 132400, SDS-PAGE, recombinant enzyme carrying His-tag |
654277 |
| 1.2.1.30 | monomer |
1 * 140000, SDS-PAGE |
-, 288184 |
| 1.2.1.30 | More |
the carboxylate reductase three-domain architecture is modular. CARs are comprised of three domains: an adenylation domain (A-domain), a phosphopantetheinyl binding domain (also called transthiolation domain (T-domain), or peptidyl carrier protein (PCP domain)), and a reductase domain (R-domain). The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine |
-, 763290 |
| 1.2.1.30 | More |
the structure of CARs is characterized through three functional domains: an N-terminal adenylation domain (A-domain), a thiolation or peptidyl carrier protein domain (T-domain), and a C-terminal reduction domain (R-domain). Structure comparisons, overview. The A-domains of CARs are members of the ANL superfamily of adenylating enzymes. The T-domain is between 80 and 120 residues in length and is highly dynamic in nature, due to the flexible linker regions connecting the alpha helix bundle to neighboring domains in NRPSs and CARs. Domain crystal structures of CARs have demonstrated the dynamic nature of the T-domain, with the activated phosphopantetheinyl-serine positioned away from A-domains in the adenylation state (ATP bound) and situated between 20-50 A from A-domains in the thiolation state (AMP bound). While the T-domain is flexible, its short amino acid length and current domain crystal structures indicate that domain shifts involve dynamic rearrangement in both the A- and R-domains as well. Reduction domain structure and activity, molecular dynamics (MD) study |
-, 763297 |
