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Literature summary for 3.2.1.151 extracted from

  • Menon, V.; Rao, M.
    Mechanistic insights into the inhibition of endo-beta 1,4 xyloglucan hydrolase by a classical aspartic protease inhibitor (2013), J. Fluoresc., 23, 311-321.
    View publication on PubMed
Search for more literature for 3.2.1.151

Inhibitors

Inhibitors Comment Organism Structure
pepstatin A a specific inhibitor towards aspartic proteases, inactivates the enzyme, reversible, competitive, two-step inhibition mechanism Thermomonospora sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics, kinetic analysis, overview Thermomonospora sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Thermomonospora sp.
-
-

Organism

Organism UniProt Comment Textmining
Thermomonospora sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native extracellular enzyme from culture filtrate by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration Thermomonospora sp.

Synonyms

Synonyms Comment Organism
endo-beta 1,4 xyloglucan hydrolase
-
 Thermomonospora sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
 assay at Thermomonospora sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Thermomonospora sp.

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
125
-
 pepstatin A pH 7.0, 50°C Thermomonospora sp.

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0035
-
 pH 7.0, 50°C Thermomonospora sp. pepstatin A