EC Number   |
Subunits |
Reference |
|---|
    4.1.1.112 | tetramer |
4 * 31700, SDS-PAGE |
4276 |
| 4.1.1.112 | tetramer |
oxaloacetate decarboxylase OAD-2 |
-, 663796 |
| 4.1.1.112 | tetramer |
the enzyme consists of alpha-, beta-, and gamma-subunits as well as a biotin carboxyl carrier protein domain. The 65 kDa hydrophilic alpha-subunit consists of an N-terminal carboxyltransferase domain connected to a C-terminal biotin carboxyl carrier protein domain. The 45 kDa beta-subunit is an integral membrane protein with nine transmembrane segments, which serves to couple the decarboxylation of carboxybiotin to the translocation of Na+ from the cytoplasm to the periplasm. The small 9 kDa gamma-subunit is an integral membrane protein with a single membrane-spanning helix at the N-terminus, followed by a hydrophilic C-terminal domain which interacts with the alpha-subunit. The gamma-subunit is essential for the overall stability of the complex, and likely serves as an anchor to hold the alpha- and beta-subunits in place |
726821 |
| 4.1.1.112 | tetramer |
the enzyme consists of alpha-, beta-, and gamma-subunits as well as a biotin carboxyl carrier protein domain. The about 65 kDa hydrophilic alpha-subunit consists of an N-terminal carboxyltransferase domain connected to a C-terminal biotin carboxyl carrier protein domain. The about 45 kDa beta-subunit is an integral membrane protein with nine transmembrane segments, which serves to couple the decarboxylation of carboxybiotin to the translocation of Na+ from the cytoplasm to the periplasm. the site of interaction with the gamma-subunit in Vibrio cholerae OADC is located in an intervening region between the carboxyltransferase and biotin carboxyl carrier protein domains of the alpha-subunit, termed the association domain. Tetramerization of alpha-OADC is mediated by an interaction between the association domain of the alpha-subunit and the cytosolic portion of the gamma-subunit in a manner. A biotin binding pocket, termed the exo-binding site, is located at the interface between the association domain and the carboxyltransferase domain. The interaction is facilitated by the tetramerization of alpha-OADC through interactions between the association domain and the the cytosolic portion of the gamma-subunit, which maintain two of the four alpha-OADC molecules in close proximity to the membrane-bound beta-subunit |
726821 |
| 4.1.1.112 | tetramer |
the enzyme is constituted of four subunits: catalytic subunit OadA (termed Ef-A), membrane pump Ef-B, biotin acceptor protein Ef-D, and subunit Ef-H. Subunits Ef-A, Ef-D, and Ef-H form a cytoplasmic soluble complex, Ef-AHD, which is also associated with the membrane. The Ef-H subunit is involved in the cytoplasmic Ef-AHD complex formation. Analysis of subunit interactions and complex formation, overview |
-, 726737 |
| 4.1.1.112 | trimer |
alpha, beta, gamma |
650185, 651122, 653877 |
