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Literature summary for 3.4.19.15 extracted from

  • Miranda, H.V.; Antelmann, H.; Hepowit, N.; Chavarria, N.E.; Krause, D.J.; Pritz, J.R.; Bไsell, K.; Becher, D.; Humbard, M.A.; Brocchieri, L.; Maupin-Furlow, J.A.
    Archaeal ubiquitin-like SAMP3 is isopeptide-linked to proteins via a UbaA-dependent mechanism (2013), Mol. Cell. Proteomics, 13, 220-239.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.19.15

Inhibitors

Inhibitors Comment Organism Structure
EDTA inactivation Haloferax volcanii

Organism

Organism UniProt Comment Textmining
Haloferax volcanii D4GTS4
-
-
Haloferax volcanii DSM 3757 D4GTS4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 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 ?
-
 ?
additional information 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 DSM 3757 ?
-
 ?
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 ?
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 ?

Synonyms

Synonyms Comment Organism
HVO_2505
-
 Haloferax volcanii
JAMM1
-
 Haloferax volcanii