EC Number   |
Natural Substrates |
|---|
   6.2.1.55 | ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine |
- |
| 6.2.1.55 | ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine |
the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates |
| 6.2.1.55 | ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine |
- |
| 6.2.1.55 | ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine |
the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates |
| 6.2.1.55 | ATP + [SAMP2]-Gly-Gly + [UbaA]-L-cysteine |
- |
| 6.2.1.55 | ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine |
- |
| 6.2.1.55 | ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine |
SAMP3 is a small protein modifier. It is suggested that samp3ylation regulates a variety of cellular functions including MoCo biosynthesis |
| 6.2.1.55 | ATP + [SAMP3]-Gly-Gly + [UbaA]-L-cysteine |
- |
| 6.2.1.55 | more |
many of the sampylated proteins that are identified (from cells grown aerobically on DMSO) are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA) |
| 6.2.1.55 | more |
the molybdopterin (MPT) synthase large subunit homologue MoaE is samp3ylated at conserved active site lysine residues determined by MS/MS analysis, immunoprecipitation, and tandem affinity purifications. Samp3ylation is covalent and reversible and controls the activity of enzymes such as MPT synthase |
