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Literature summary for 3.4.21.53 extracted from

  • Pei, J.; Yan, J.; Jiang, Y.
    Characterization of the ATP-dependent Lon-like protease in Methanobrevibacter smithii (2016), Archaea, 2016, 5759765 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.53

Cloned(Commentary)

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

Inhibitors Comment Organism Structure
ADP moderate inhibition of 36% Methanobrevibacter smithii

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Methanobrevibacter smithii 5829
-

Metals/Ions

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

Organism UniProt Comment Textmining
Methanobrevibacter smithii A5UP31
-
-
Methanobrevibacter smithii ATCC 35061 A5UP31
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Methanobrevibacter smithii

Substrates and Products (Substrate)

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

Subunits Comment Organism
? x * 77000, recombinant His-tagged Lon-like-Ms, SDS-PAGE Methanobrevibacter smithii

Synonyms

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 recombinant enzyme Methanobrevibacter smithii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 recombinant enzyme Methanobrevibacter smithii

Cofactor

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

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