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Literature summary for 3.4.21.62 extracted from

  • Gamble, M.; Kuenze, G.; Brancale, A.; Wilson, K.S.; Jones, D.D.
    The role of substrate specificity and metal binding in defining the activity and structure of an intracellular subtilisin (2012), FEBS open bio, 2, 209-215.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.62

Inhibitors

Inhibitors Comment Organism Structure
EDTA inactivates the enzyme at 0.01 mM, the enzyme protein becomes less structured and potentially monomeric. Removal of Ca2+ at sites close to the dimer interface and the S1 pocket are involved enzyme inhhibition by EDTA Alkalihalobacillus clausii

Localization

Localization Comment Organism GeneOntology No. Textmining
intracellular
-
 Alkalihalobacillus clausii 5622
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ is important for ISP activity through structural changes. The looped turn constituted by residues Ala180-Pro197 binds Ca2+. Removal of Ca2+ at sites close to the dimer interface and the S1 pocket are involved enzyme inhhibition by EDTA Alkalihalobacillus clausii
additional information metal ions are not involved in the subtilisin catalytic mechanism but are an important structural element Alkalihalobacillus clausii

Organism

Organism UniProt Comment Textmining
Alkalihalobacillus clausii D0AB41
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-Ala-Pro-Leu-4-nitroanilide + H2O low activity Alkalihalobacillus clausii Ala-Ala-Pro-Leu + 4-nitroaniline
-
 ?
Ala-Ala-Pro-Lys-4-nitroanilide + H2O low activity Alkalihalobacillus clausii Ala-Ala-Pro-Lys + 4-nitroaniline
-
 ?
Ala-Ala-Pro-Met-4-nitroanilide + H2O low activity Alkalihalobacillus clausii Ala-Ala-Pro-Met + 4-nitroaniline
-
 ?
Ala-Ala-Pro-Nle-4-nitroanilide + H2O low activity Alkalihalobacillus clausii Ala-Ala-Pro-Nle + 4-nitroaniline
-
 ?
Ala-Ala-Pro-Phe-4-nitroanilide + H2O low activity Alkalihalobacillus clausii Ala-Ala-Pro-Phe + 4-nitroaniline
-
 ?
Ala-Ala-Val-Ala-4-nitroanilide + H2O low activity Alkalihalobacillus clausii Ala-Ala-Val-Ala + 4-nitroaniline
-
 ?
Bovine serum albumin + H2O poor substrate in native form, but can be digested in heat-denatured form Alkalihalobacillus clausii ?
-
 ?
lactate dehydrogenase + H2O poor substrate in native form, but can be digested in heat-denatured form Alkalihalobacillus clausii ?
-
 ?
malate dehydrogenase + H2O poor substrate in native form, but can be digested in heat-denatured form Alkalihalobacillus clausii ?
-
 ?
additional information substrate specificity, substrate docking simulations, overview. No activity with Ala-Ala-Pro-Glu-4-nitroanilide and Tyr-Val-Ala-Asp-4-nitroanilide. Substrate specificity and the role of stress signals such as divalent metal ions play roles in defining the proteolytic activity of Bacillus clausii intracellular subtilisin protease, molecular basis, overview. The enzyme unfolds under stress conditions. Heat-denatured whole proteins are found to be better substrates for the enzyme than the native forms Alkalihalobacillus clausii ?
-
 ?
Phe-Ala-Ala-Phe-4-nitroanilide + H2O highly preferred substrate Alkalihalobacillus clausii Phe-Ala-Ala-Phe + 4-nitroaniline
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Alkalihalobacillus clausii

Synonyms

Synonyms Comment Organism
intracellular subtilisin protease
-
 Alkalihalobacillus clausii
ISP
-
 Alkalihalobacillus clausii

General Information

General Information Comment Organism
evolution the enzyme belongs to a structurally distinct class of the subtilase family Alkalihalobacillus clausii
additional information substrate specificity and the role of stress signals such as divalent metal ions play roles in defining the proteolytic activity of Bacillus clausii intracellular subtilisin protease, molecular basis, overview. Heat-denatured whole proteins are found to be better substrates for the enzyme than the native forms. The S1, S2 and S4 sites form defined substrate binding pockets Alkalihalobacillus clausii
physiological function modeling of intracellular subtilisin protease regulation within the cell Alkalihalobacillus clausii