EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
3.4.19.15 | N6-SAMP1-[protein]-L-lysine + H2O |
broad spectrum of activity in removing SAMP1/2 from diverse proteins. HvJAMM1 is unable to hydrolyze bovine serum albumin, hemoglobin, creatine phosphokinase, carbonic anhydrase, beta-amylase or cytochrome c. Long-term incubation with the enzyme has little if any impact on the level or length of these proteins |
Haloferax volcanii |
SAMP1 + [protein]-L-lysine |
- |
? |
3.4.19.15 | N6-SAMP1-[protein]-L-lysine + H2O |
broad spectrum of activity in removing SAMP1/2 from diverse proteins. HvJAMM1 is unable to hydrolyze bovine serum albumin, hemoglobin, creatine phosphokinase, carbonic anhydrase, beta-amylase or cytochrome c. Long-term incubation with the enzyme has little if any impact on the level or length of these proteins |
Haloferax volcanii DSM 3757 |
SAMP1 + [protein]-L-lysine |
- |
? |
3.4.19.15 | N6-SAMP2-[protein]-L-lysine + H2O |
broad spectrum of activity in removing SAMP1/2 from diverse proteins. HvJAMM1 is unable to hydrolyze bovine serum albumin, hemoglobin, creatine phosphokinase, carbonic anhydrase, beta-amylase or cytochrome c. Long-term incubation with the enzyme has little if any impact on the level or length of these proteins |
Haloferax volcanii |
SAMP2 + [protein]-L-lysine |
- |
? |
3.4.19.15 | N6-SAMP2-[protein]-L-lysine + H2O |
broad spectrum of activity in removing SAMP1/2 from diverse proteins. HvJAMM1 is unable to hydrolyze bovine serum albumin, hemoglobin, creatine phosphokinase, carbonic anhydrase, beta-amylase or cytochrome c. Long-term incubation with the enzyme has little if any impact on the level or length of these proteins |
Haloferax volcanii DSM 3757 |
SAMP2 + [protein]-L-lysine |
- |
? |
3.4.19.15 | N6-[SAMP1]-[MoaE]-L-lysine + H2O |
MoaE, i.e. molybdopterin synthase large subunit homolog. Residue K240 of MoaE is isopeptide-linked to SAMP1 |
Haloferax volcanii |
[MoaE]-L-lysine + SAMP1 |
- |
? |
3.4.19.15 | N6-[SAMP1]-[MoaE]-L-lysine + H2O |
MoaE, i.e. molybdopterin synthase large subunit homolog. Residue K240 of MoaE is isopeptide-linked to SAMP1 |
Haloferax volcanii DSM 3757 |
[MoaE]-L-lysine + SAMP1 |
- |
? |
3.4.19.15 | N6-[SAMP3]-[MoaE]-L-lysine + H2O |
MoaE, i.e. molybdopterin synthase large subunit homolog |
Haloferax volcanii |
[MoaE]-L-lysine + SAMP3 |
SAMP3 protein conjugates are dependent on the ubiquitin-activating E1 enzyme homolog of archaea (UbaA) for synthesis and are cleaved by the JAMM/MPN+ domain metalloprotease JAMM1 |
? |
3.4.19.15 | N6-[SAMP3]-[MoaE]-L-lysine + H2O |
MoaE, i.e. molybdopterin synthase large subunit homolog |
Haloferax volcanii DSM 3757 |
[MoaE]-L-lysine + SAMP3 |
SAMP3 protein conjugates are dependent on the ubiquitin-activating E1 enzyme homolog of archaea (UbaA) for synthesis and are cleaved by the JAMM/MPN+ domain metalloprotease JAMM1 |
? |