Cloned (Comment) | Organism |
---|---|
gene Msm_1754, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Methanobrevibacter smithii |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ADP | moderate inhibition of 36% | Methanobrevibacter smithii |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Methanobrevibacter smithii | 5829 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | 80-83% activity in presence of ATP compared to Mg2+ | Methanobrevibacter smithii | |
Co2+ | 65-70% activity in presence of ATP compared to Mg2+ | Methanobrevibacter smithii | |
Mg2+ | strictly dependent on, activates. Enzyme Lon-like-Ms exhibits no cleavage activity without Mg2+, regardless of the presence or absence of ATP | Methanobrevibacter smithii | |
Mn2+ | 72-89% activity in presence of ATP compared to Mg2+ | Methanobrevibacter smithii | |
additional information | the enzyme activity depends on divalent cations, no activity with Zn2+ | Methanobrevibacter smithii | |
Ni2+ | 16-20% activity in presence of ATP compared to Mg2+ | Methanobrevibacter smithii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methanobrevibacter smithii | A5UP31 | - |
- |
Methanobrevibacter smithii ATCC 35061 | A5UP31 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Methanobrevibacter smithii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-casein + H2O | - |
Methanobrevibacter smithii | ? | - |
? | |
alpha-casein + H2O | - |
Methanobrevibacter smithii ATCC 35061 | ? | - |
? | |
glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide + H2O | - |
Methanobrevibacter smithii | ? | - |
? | |
glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide + H2O | - |
Methanobrevibacter smithii ATCC 35061 | ? | - |
? | |
additional information | recombinant Lon-like-Ms exhibits ATPase activity and cleavage activity toward fluorogenic peptides and casein. The peptidase activity of Lon-like-Ms relies strictly on Mg2+ (or other divalent cations) and ATP | Methanobrevibacter smithii | ? | - |
? | |
additional information | recombinant Lon-like-Ms exhibits ATPase activity and cleavage activity toward fluorogenic peptides and casein. The peptidase activity of Lon-like-Ms relies strictly on Mg2+ (or other divalent cations) and ATP | Methanobrevibacter smithii ATCC 35061 | ? | - |
? | |
succinyl-Phe-Leu-Phe-4-methoxy-beta-naphthylamide + H2O | - |
Methanobrevibacter smithii | ? | - |
? | |
succinyl-Phe-Leu-Phe-4-methoxy-beta-naphthylamide + H2O | - |
Methanobrevibacter smithii ATCC 35061 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 77000, recombinant His-tagged Lon-like-Ms, SDS-PAGE | Methanobrevibacter smithii |
Synonyms | Comment | Organism |
---|---|---|
La protease | - |
Methanobrevibacter smithii |
lon-like protease | - |
Methanobrevibacter smithii |
Lon-like-Ms | - |
Methanobrevibacter smithii |
Msm 1754 | - |
Methanobrevibacter smithii |
Msm_1754 | - |
Methanobrevibacter smithii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
recombinant enzyme | Methanobrevibacter smithii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
recombinant enzyme | Methanobrevibacter smithii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ADP | results in 72% activity with substrate alpha-casein, and 64% with peptide substrate glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide compared to ATP in presence of Mg2+ | Methanobrevibacter smithii | |
AMPPNP | 5'-adenylyl imidodiphosphate, results in 80% activity with substrate alpha-casein, and 92% with peptide substrate glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide compared to ATP in presence of Mg2+ | Methanobrevibacter smithii | |
ATP | dependent on | Methanobrevibacter smithii | |
CTP | results in 122% activity with substrate alpha-casein, and 131% with peptide substrate glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide compared to ATP in presence of Mg2+ | Methanobrevibacter smithii | |
GTP | results in 85% activity with substrate alpha-casein, and 90% with peptide substrate glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide compared to ATP in presence of Mg2+ | Methanobrevibacter smithii | |
UTP | results in 55% activity with substrate alpha-casein, and 64% with peptide substrate glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide compared to ATP in presence of Mg2+ | Methanobrevibacter smithii |
General Information | Comment | Organism |
---|---|---|
evolution | phylogenetic analysis reveals that Lon-like-Ms and its homologs are members of the Lon family. The ATP-dependent Lon (La) protease is the most highly conserved member of the energy-dependent protease present in the cytosol of prokaryotes and in the mitochondria and peroxisomes of eukaryotes. While the LonA group is found in eukaryotes and bacteria, the LonB subfamily proteins are only found in archaea. Two genes (Msm 1569 and Msm 1754) encoding Lon occur in the genome sequence, and the encoded proteins may play different roles. Msm 1569 encodes a canonical LonB protease (Lon-Ms). Msm 1754 (Lon-like-Ms) differs considerably from previously reported Lon proteases | Methanobrevibacter smithii |