EC Number   |
General Information |
Reference |
|---|
   3.6.1.18 | evolution |
there likely are two classes of Ftps, one associated with FAD-binding and the other with FAD hydrolysis |
-, 757628 |
| 3.6.1.18 | malfunction |
a single amino acid substitution Y60N converts it from an FAD-binding protein to a Mg2+-dependent FAD diphosphatase (Ftp_Tp-like). The engineered protein variant (Ftp_EcY60A) shows Mg2+-dependent FAD diphosphatase activity, but also retains its Mg2+-dependent FMN transferase (EC 2.7.1.180) activity on the protein substrate, indicating that the protein variant enzyme has dual activity |
757628 |
| 3.6.1.18 | more |
the critical residue that contacts the isoalloxazine ring of FAD, is a tyrosine residue in the FAD-binding Ftps |
-, 757628 |
| 3.6.1.18 | physiological function |
the flavin-trafficking protein (Ftp) catalyzes the transfer of the FMN moiety of FAD to a threonine residue in a target flavoprotein |
757628 |
| 3.6.1.18 | physiological function |
the flavin-trafficking protein (Ftp) in the syphillis spirochete Treponema pallidum (Ftp_Tp) is a bacterial metal-dependent FAD diphosphatase that hydrolyzes FAD into AMP and FMN in the periplasm |
-, 757628 |
