EC Number   |
Substrates |
Organism  |
Products |
Reversibility |
|---|
   3.4.19.15 | an N6-[small archaeal modifier protein]-[protein]-L-lysine + H2O |
Hvo_2505 mixed with Ta0895_VSGG-Ta0547 results cleavage products at 18 kDa (Ta0547) and 14 kDa (Ta0895_VSGG). Hvo_2505 is active at 24°C, 37°C and 48°C cleaving a substantial percentage of Ta0895_VAGG-ScRpn11 and Ta0895_VSGG-Ta0547. No cleavage activity is detected at lower (10°C) temperature. Inactive on Ta1019-ScRpn11 and Mbur_1415-ScRpn11 fusion protein substrates |
Haloferax volcanii |
a [protein]-L-lysine + a small archaeal modifier protein |
- |
? |
| 3.4.19.15 | more |
the enzyme can cleave proteins attached to SAMP1 by linear and isopeptide bonds. The enzyme is inactive in hydrolyzing the amide bond that links aminomethylcoumarin to the C-terminus of monomeric ubiquinone or diglycine |
Haloferax volcanii |
? |
- |
? |
| 3.4.19.15 | more |
JAMM1 is a metalloprotease with relatively broad substrate specificity, able to cleave a wide variety of proteins conjugated to SAMP3 as well as SAMP1/2 |
Haloferax volcanii |
? |
- |
? |
| 3.4.19.15 | N6-SAMP1-[molybdopterin synthase MoaE]-L-lysine + H2O |
- |
Haloferax volcanii |
SAMP1 + [molybdopterin synthase MoaE]-L-lysine |
- |
? |
| 3.4.19.15 | N6-SAMP1-[molybdopterin synthase MoaE]-L-lysine + H2O |
the enzyme cleaves isopeptide-liked SAMP1 from molybdopterin synthase MoaE. It also cleaves linear fusions of SAMP to molybdopterin synthase MoaE |
Haloferax volcanii |
SAMP1 + [molybdopterin synthase MoaE]-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 |
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-[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-[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 | an N6-[small archaeal modifier protein]-[protein]-L-lysine + H2O |
Hvo_2505 mixed with Ta0895_VSGG-Ta0547 results cleavage products at 18 kDa (Ta0547) and 14 kDa (Ta0895_VSGG). Hvo_2505 is active at 24°C, 37°C and 48°C cleaving a substantial percentage of Ta0895_VAGG-ScRpn11 and Ta0895_VSGG-Ta0547. No cleavage activity is detected at lower (10°C) temperature. Inactive on Ta1019-ScRpn11 and Mbur_1415-ScRpn11 fusion protein substrates |
Haloferax volcanii ATCC 29605 |
a [protein]-L-lysine + a small archaeal modifier protein |
- |
? |
