Literature summary for 3.4.21.64 extracted from

Hosseini-Koupaei, M.; Shareghi, B.; Saboury, A.A.; Davar, F.; Sirotkin, V.A.; Hosseini-Koupaei, M.H.; Enteshari, Z.
Catalytic activity, structure and stability of proteinase K in the presence of biosynthesized CuO nanoparticles (2019), Int. J. Biol. Macromol., 122, 732-744 .

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KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Michaelis-Menten kinetics	Parengyodontium album

Organism

Organism	UniProt	Comment	Textmining
Parengyodontium album	P06873	i.e. Tritirachium album or Engyodontium album	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
commercial preparation	-	Parengyodontium album	-

Subunits

Subunits	Comment	Organism
?	x * 28900, SDS-PAGE	Parengyodontium album

Synonyms

Synonyms	Comment	Organism
Proteinase K	-	Parengyodontium album

General Information

General Information	Comment	Organism
evolution	proteinase K belongs to the class of subtilisin-like serine protease with the typical triad of Asp39-His69-Ser224. The protein is folded into alpha- and beta-rich regions without any clear domains	Parengyodontium album
additional information	carboxylic acids and compounds, e.g. chrysanthemin, quercetin, and valerenic acid, in Sambucus nigra plant extract can create stable Cu-carboxylic acid complexes. CuO nanoparticles, synthesized using Sambucus nigra (elderberry) fruit extract, bind proteinase K, and induce structural changes in enzyme accompanied by a decrease in Michaelis-Menten constant at 25°C. The enzyme affinity for the substrate is increased. Depending on the temperature, CuO nanoparticles show a dual effect on the thermodynamic stability and binding affinity of enzyme. The nanoparticles increase the stability of the native state of enzyme at room temperature. On the other hand, the nanoparticles stabilize the unfolded state of enzyme at 37-50°C. An overall favorable Gibbs energy change is observed for the binding process at 25-50°C. The enzyme-nanoparticle binding is enthalpically driven at room temperature. Hydrogen bonding plays a key role in the interaction of enzyme with nanoparticles at 25-37°C. At higher temperatures, the protein-ligand binding is entropically driven. Thus hydrophobic association plays a major role in the proteinase K-CuO binding at 37-50°C. Thermodynamics, overview	Parengyodontium album

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Release 2023.1 (January 2023)