EC Number |
Subunits |
Reference |
---|
5.4.3.5 | dimer |
2 * 95000-98000, SDS-PAGE |
2074 |
5.4.3.5 | heterotetramer |
alpha2beta2 |
-, 747193 |
5.4.3.5 | heterotetramer |
alpha2beta2, 2 * 12800, alpha-subunit, + 2 * 82900, beta-subunit, SDS-PAGE |
747073 |
5.4.3.5 | heterotetramer |
alpha2beta2, OraS, OraE, 2 * 12800 + 2 * 82900 |
704658 |
5.4.3.5 | More |
enzyme OAM is an alpha2beta2 heterodimer comprised of two strongly associating subunits, OraE (82.9 kDa) and OraS (12.8 kDa).7 Each OraE subunit comprises a triosephosphate isomerase (TIM) barrel domain and a Rossmann-like domain. A domain swap occurs in the heterodimer, whereby the Rossmann-like domain of one OraE subunit associates with the TIM barrel domain of a second OraE subunit and vice versa, such that two identical active sites are formed |
747073 |
5.4.3.5 | More |
protein KamDE comprised of the 30000 and 51000 Da subunits of the E1 component of D-alpha-lysine aminomutase is catalytically active in absence of the third 12800 kDa subunit, but ATP no longer has a regulatory effect on it. The S subunit of D-ornithine aminomutase, OraS, is capable of forming a complex with KamDE and restores the enzymes ATP-dependent allosteric regulation |
679913 |
5.4.3.5 | tetramer |
2 * 12800, subunit OraS + 2 * 82900, subunit OraE, alpha2beta2 |
-, 727131 |
5.4.3.5 | tetramer |
2 * 12800, subunit OraS + 2 * 90000, subunit OraE, alpha2beta2 |
727644 |
5.4.3.5 | tetramer |
alpha2beta2, 2 * 12800 + 2 * 82900, deduced from nucleotide sequence |
652199 |