Any feedback?
Information on EC 3.4.21.64 - peptidase K and Organism(s) Parengyodontium album and UniProt Accession P06873
for references in articles please use BRENDA:EC3.4.21.64Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.21.64 peptidase KSpecify your search results
Word Map
- 3.4.21.64
-
3.4.21.4
- chymotrypsin
- subtilisins
- alpha-chymotrypsin
-
carlsberg
-
3.1.1.3
- synthesis
- degradation
- beta-trypsin
- diagnostics
- analysis
- pharmacology
- molecular biology
- medicine
- detergent
-
3.4.17.1
- biotechnology
The taxonomic range for the selected organisms is: Parengyodontium album
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
endopeptidase k, tritirachium alkaline proteinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Proteinase K
-
Proteinase K
Proteinase, Tritirachium album serine
-
-
-
-
Tritirachium album proteinase K
-
-
-
-
Tritirachium alkaline proteinase
-
-
-
-
Proteinase K
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
39450-01-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-galactosidase + H2O
?
proteinase K activity determination with beta-galactosidase as sensitive macromolecular substrate, comparison of the native protein-attacking ability of free and immobilized proK, method evaluation, overview. beta-Galactosidase is inactivated by proK. Compared to free proK, immobilized proK is much less efficient in inactivating beta-galactosidase, most likely due to a decreased mobility of immobilized proK and a restricted accessibility of the substrate to the active site of proK
-
-
?
N-succinyl-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Phe + 4-nitroaniline
-
-
-
?
normal cellular prion protein + H2O
pathogenic cellular prion protein + ?
in mouse brain
-
-
?
prion protein + H2O
?
specific cleavage, that does not occur at cross-linker-modified residues
-
-
?
succinyl-AAPF-4-nitroanilide + H2O
succinyl-AAPF + 4-nitroaniline
-
-
-
?
AAPA + H2O
?
-
molecular dynamics simulations of the proteinase K alone and in complex with the peptide substrate AAPA are performed to investigate the effect of substrate binding on the dynamics/molecular motions of proteinase K
-
-
?
carboxybenzoyl-(Ala)2-Lys methyl ester + H2O
carboxybenzoyl-(Ala)2-Lys + methanol
-
-
-
-
?
carboxybenzoyl-D-Ala-L-Lys methyl ester + H2O
carboxybenzoyl-D-Ala-L-Lys + methanol
-
-
-
-
?
carboxybenzoyl-Gly-Lys methyl ester + H2O
carboxybenzoyl-Gly-Lys + methanol
-
-
-
-
?
carboxybenzoyl-L-Ala-L-Lys methyl ester + H2O
carboxybenzoyl-L-Ala-L-Lys + methanol
-
-
-
-
?
carboxybenzoyl-L-Lys methyl ester + H2O
carboxybenzoyl-L-Lys + methanol
-
-
-
-
?
carboxybenzoyl-Leu-Lys methyl ester + H2O
carboxybenzoyl-Leu-Lys + methanol
-
-
-
-
?
Glucose dehydrogenase + H2O
Hydrolyzed glucose dehydrogenase
-
upon proteolysis the enzyme is inactivated and the polypeptide chain is cleaved into 2 distinct fragments (K-protein, MW 26000 and K-peptide, MW 3000), the cleavage occurs in the C-terminal region of the polypeptide chain.-Leu-Ala-+-Ser-Ser-Glu is proposed as the cleavage site, the term -+- depicts the point of cleavage
upon proteolysis the enzyme is inactivated and the polypeptide chain is cleaved into 2 distinct fragments (K-protein, MW 26000 and K-peptide, MW 3000), the cleavage occurs in the C-terminal region of the polypeptide chain. Leu-Ala-+-Ser-Ser-Glu is proposed as the cleavage site, the term -+- depicts the point of cleavage
?
human growth hormone + H2O
?
-
proteolytic activity and specificity of PK is maintained after its immobilization to magnetic particles
-
-
?
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Leu + p-nitroaniline
-
-
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
main cleavage sites: Gln4-His5, Ser9-His10, Leu11-Val12, Leu15-Tyr16, Leu17-Val18, Phe24-Phe25, Tyr26-Thr27
main cleavage sites: Gln4-His5, Ser9-His10, Leu11-Val12, Leu15-Tyr16, Leu17-Val18, Phe24-Phe25, Tyr26-Thr27
?
prion protein + H2O
?
-
for mouse RML prions, the majority of proteinase K-sensitive disease-related prion protein isoforms do not appear to contribute significantly to infectivity. In human variant Creutzfeldt-Jakob disease, up to 90% of total prion protein present in the brain resists degradation with thermolysin, whereas only 15% of this material resists digestion by proteinase K
-
-
?
pro-recombinant transglutaminase + H2O
?
-
successful cleavage at the pro-sequence
-
-
?
succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
succinyl-Ala-Ala-Ala + p-nitroaniline
-
-
-
-
?
Synthetic peptide substrates + H2O
?
-
primarily specific against aromatic or hydrophobic amino acid residues at the carboxyl side of the splitting point, activity is markedly promoted by elongating the peptide chain to the N-terminal from the splitting point
-
-
?
Urea-denatured hemoglobin + H2O
Hydrolyzed urea-denatured hemoglobin
-
-
-
-
?
human sensitive prion protein Sc + H2O
?
degradation, pathogenic isoform, sensitive prion protein complexes show higher molecular weight than resistant prions
-
-
?
additional information
?
-
intact Staphylococcus aureus cells, heat-killed Pseudomonas aeruginosa cells, free genomic DNA of Salmonella enterica, and a mixture of these targets are treated by a DNase I/proteinase K mixture, overview
-
-
?
additional information
?
-
resistant and sensitive prion protein fractions, obtained by limited proteolysis and mass spectrometry, show that both have similar enzyme-cleavage maps and therefore seems to share the same basic architecture. In vivo proteinase K-resistance of prions may not be the rule but the exception
-
-
?
additional information
?
-
chemoenzymatic synthesis of oligo(L-phenylalanine) mediated by proteinase K from Tritirachium album, the synthesized linear oligo-phenylalanine showed a unique self-assembly in aqueous solutions, overview
-
-
?
additional information
?
-
substrate synthesis: a synthetic gene corresponding to the Syrian hamster prion protein sequence 90-232 with a 23-residue N-terminal fusion tag containing His6 and a thrombin cleavage site (MGSSHHHHHHSSGLVPRGSHMLE) is specifically synthesized and expressedas substrate for the enzyme
-
-
?
additional information
?
-
beta-galactosidase activity is measured spectrophotometrically with 2-nitrophenyl-beta-galactopyranoside. Hen egg lysozyme, horseradish peroxidase, or Aspergillus sp. glucose oxidase are not inactivated by proteinase K
-
-
?
additional information
?
-
the enzyme has a broad substrate specificity. Evaluation of aminolytic activity by polymerization of glutamic acid diethyl ester oligo(glutamic acid ethyl ester)
-
-
?
additional information
?
-
the enzyme has a broad-spectrum degradation capability to degrade proteins
-
-
?
additional information
?
-
-
the smallest peptide hydrolyzable should be a tetrapeptide, so that the enzyme could be used as an appropriate tool for sequence analysis of medium size peptides
-
-
?
additional information
?
-
-
the combined action of detergent and proteinase K is effective in degrading `masked' proteins in a poly(adenosine diphosphoribose) preparation which cannot be attacked by the proteinase alone
-
-
?
additional information
?
-
-
specificity for peptide bonds adjacent to the carboxylic group of aliphatic and aromatic amino acids
-
-
?
additional information
?
-
-
segment GGG of human prion protein strongly binds as a substrate at the substrate recognition site
-
-
?
additional information
?
-
-
digestion of mouse cell lysates overexpressing prion proteins
-
-
?
additional information
?
-
-
anti-biofilm activity of proteinase K in combination with antibiotics, streptomycin, gentamycin and ampicillin used against bap-positive Sthaphylococcus aureus V329 biofilms. Recovery of Bap, a large, multi-domain, cell surface-anchored Ca2+-dependent protein, which has a crucial role in the early stages of Staphylococcus aureus biofilm development, within 3 h after proteinase K treatment, overview. Binding of Ca2þ to Bap does not confer any immunity against proteolytic degradation
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
human sensitive prion protein Sc + H2O
?
degradation, pathogenic isoform, sensitive prion protein complexes show higher molecular weight than resistant prions
-
-
?
additional information
?
-
intact Staphylococcus aureus cells, heat-killed Pseudomonas aeruginosa cells, free genomic DNA of Salmonella enterica, and a mixture of these targets are treated by a DNase I/proteinase K mixture, overview
-
-
?
additional information
?
-
resistant and sensitive prion protein fractions, obtained by limited proteolysis and mass spectrometry, show that both have similar enzyme-cleavage maps and therefore seems to share the same basic architecture. In vivo proteinase K-resistance of prions may not be the rule but the exception
-
-
?
additional information
?
-
-
segment GGG of human prion protein strongly binds as a substrate at the substrate recognition site
-
-
?
additional information
?
-
-
anti-biofilm activity of proteinase K in combination with antibiotics, streptomycin, gentamycin and ampicillin used against bap-positive Sthaphylococcus aureus V329 biofilms. Recovery of Bap, a large, multi-domain, cell surface-anchored Ca2+-dependent protein, which has a crucial role in the early stages of Staphylococcus aureus biofilm development, within 3 h after proteinase K treatment, overview. Binding of Ca2þ to Bap does not confer any immunity against proteolytic degradation
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
1 mM CaCl2, the denaturation temperature of proteinase K derivatized with praseodymium (Pr) ions is 16.2°C, which is 5.9°C higher than those of metal-free and Ca2+-bound proteinase K, respectively. Isothermal titration calorimetry (ITC) measurements demonstrate that Pr-ion binding to proteinase K shows endothermic peaks, whereas Ca2+-ion binding shows exothermic peaks, indicating that the binding mode of Pr ions is different from that of Ca2+ ions, even though the crystal structures of proteinase K with Pr and Ca2+ ions are identical
Cu2+
proteinase K and Cu2+ ions are used to synthesize enzyme-inorganic hybrid nanoflowers (P-hNFs). The P-hNFs exhibit better activity than free proteinase K in the presence of all surfactants, i.e. CHAPS, DOC, SDS, Triton X-100 and Tergitol, except for Tween 80. synthesized enzyme-inorganic hybrid nanoflowers (P-hNFs) can potentially be used as an additive in detergent formulations
dysprosium
1 mM DyCl3, differential scanning calorimetry analysis bound to the enzyme
europium
1 mM EuCl33, differential scanning calorimetry analysis bound to the enzyme
gadolinium
1 mM GdCl33, differential scanning calorimetry analysis bound to the enzyme
holmium
1 mM HoCl3, differential scanning calorimetry analysis bound to the enzyme
lanthanum
1 mM La(NO3)3, differential scanning calorimetry analysis bound to the enzyme
lutetium
1 mM LuCl3, differential scanning calorimetry analysis bound to the enzyme
neodymium
1 mM NdCl3, differential scanning calorimetry analysis bound to the enzyme
Pr3+
1 mM PrCl3, the denaturation temperature of proteinase K derivatized with praseodymium (Pr) ions is 16.2°C, which is 5.9°C higher than those of metal-free and Ca2+-bound proteinase K, respectively. Isothermal titration calorimetry (ITC) measurements demonstrate that Pr-ion binding to proteinase K shows endothermic peaks, whereas Ca2+-ion binding shows exothermic peaks, indicating that the binding mode of Pr ions is different from that of Ca2+ ions, even though the crystal structures of proteinase K with Pr and Ca2+ ions are identical. Hydrolytic activity of Pr-derivatized proteinase K shows that the hydrolytic activity is 46fold higher at 70°C using synthetic nitroanilide substrate and 9 and 76fold higher at 70°C and 80°C using fluorescein isothiocyanate-labeled casein, respectively, in comparison with the native proteinase K. Furthermore, based on the yield of chemoenzymatic peptide syntheses, the aminolysis activity of Pr-derivatized proteinase K is 3.5 and 9.5fold higher than that of the native proteinase K at 50°C and 60°C, respectively. Analysis of the mechanism by which Pr ions enhance the thermal stability of proteinase K, overview
samarium
1 mM SmCl3, differential scanning calorimetry analysis bound to the enzyme
ytterbium
1 mM YbCl3, differential scanning calorimetry analysis bound to the enzyme
Ca2+
Calcium
SDS
-
stimulates hydrolysis of serum albumin in a dose-dependent manner, caused primarily by denaturation of the protein substrate, inactivates with an oligopeptide as substrate
Urea
-
stimulates hydrolysis of serum albumin in a dose-dependent manner, caused primarily by denaturation of the protein substrate
additional information
differential scanning calorimetry curves for proteinase K derivatized with heavy atoms, showing the correlation between atomic number and denaturation temperature, overview
Calcium
-
the second more mobile Ca2+ site bridges 2 loops close to the amino and the carboxy termini
Calcium
-
X-ray studies show that it has 2 binding sites for Ca2+, Ca2+ is not directly involved in the catalytic mechanism and is 16.6 A away from the alpha-carbon atoms of the catalytic triad Asp39-His69-Ser224, the activity of the enzyme towards the synthetic substrate succinyl-Ala-Ala-Ala 4-nitroanilide drops slowly to about 20% of its original value when it is depleted of Ca2+
Calcium
-
2 calcium ions are bound to the native enzyme, activity drops by 70% if this Ca2+ is removed by EDTA
Calcium
-
the first calcium site is formed by the loop of the residues 174-178 and Asp200
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
MeOSuc-Ala-Ala-Pro-Phe-CH2Cl
examination of inhibitory activity using a real-time reverse transcription-polymerase chain reaction assay in the presence of proteinase K. The AAPF inhibitor at a concentration of 0.05 mM allows a signal to be obtained for exogenous target Xeno RNA at 30 cycles
N-benzyl-Nalpha-(tert-butoxycarbonyl)-L-phenylalaninamide
DDI-1, inhibits proteinase K (ProK) as well as pronase (Pron)
-
SDS
5% v/v, SDS causes about 62% and 56% inhibition of proteolytic activity for free proteinase K and the enzyme-inorganic hybrid nanoflowers (P-hNFs), respectively
spermidine
effect of spermidine on the structure, kinetics and stability of proteinase K, analysis with respect to industrial and biological applications of the enzyme. Molecular docking study and simulations, molecular dynamics data analysis, overview
tergitol
5% v/v, compared to the free enzyme, a significant increase in the activity of enzyme-inorganic hybrid nanoflowers (P-hNFs) in the presence of tergitol, maybe resulting from both non-ionic surfactants and hybrid nanoflowers structure, by positively regulating the structural dynamics and flexibility of the enzyme
Tween 20
5% v/v, compared to the free enzyme, a significant increase in the activity of enzyme-inorganic hybrid nanoflowers (P-hNFs) in the presence of Tween 20, maybe resulting from both non-ionic surfactants and hybrid nanoflowers structure, by positively regulating the structural dynamics and flexibility of the enzyme
Chloromethyl ketone derivatives
-
e.g. carboxybenzoyl-Ala-Gly-PheCH2Cl, carboxybenzoyl-Ala-PheCH2Cl
fructose 1,6-diphosphate
-
mixed-type inhibition, more than one inhibitor molecule binds to proteinase K
glucose 6-phosphate
-
mixed-type inhibition, more than one inhibitor molecule binds to proteinase K
Low-molecular-weight protein proteinase inhibitors from the granule-rich fraction of equine neutrophilic granulocytes
-
-
-
Polyvalent proteinase inhibitor from albumin gland of Helix pomatia
-
-
-
SDS
-
stimulates hydrolysis of serum albumin in a dose-dependent manner, caused primarily by denaturation of the protein substrate, inactivates with an oligopeptide as substrate
Turkey ovomucoid
-
enzyme interacts with the third domain at the Leu18-Glu19 peptide bond, the reactive site of the inhibitor
-
additional information
non-ionic surfactants poorly bind to the proteins; but they can affect the free energy of the solvent forces on the surface of a protein and may causes slight movements of a protein which results in changes in an enzyme activity. Poor effects by 5% v/v CHAPS
-
additional information
several DDI-1 structure analogues block Pron- but not ProK-induced spermiogenesis
-
additional information
-
immobilization of PK on magnetic latex microparticles (500A5 microparticles) and other chemically and structurally similar types of magnetic carriers
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
spermine
interaction of proteinase K with spermine, multispectroscopic study and molecular simulation, structure-function analysis, overview. The stability and enzyme activity of proteinase K-spermine complex are significantly enhanced as compared to the pure enzyme, secondary structure alteration of proteinase K with an increase in alpha-helicity and a decrease in beta-sheet of proteinase K upon spermine conjugation. Spermine interacts with proteinase K spontaneously at single binding site
additional information
-
highest activity using 3 mg of PK per mg of the carrier
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
carboxybenzoyl-L-Ala-L-Lys methyl ester
-
carboxybenzoyl-Phe-Lys methyl ester
-
additional information
additional information
kinetics and thermodynamics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
enzyme kinetics, overview
-
additional information
additional information
Michaelis-Menten kinetic analysis of free enzyme and enzyme in presence of spermidine, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 7
-
proteinase K maintains structural integrity in the range of pH 3.0-7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
maximum degree of polymerization is achieved at 60°C using Pr-derivatized proteinase K, and at 50°C using the native proteinase K with Ca2+ ions. The yield of oligo(glutamic acid ethyl ester) is highest at 30°C using both the native and Pr-derivatized proteinase K
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
secretion starts when the stationary phase of growth is reached, and when the culture medium is depleted of glucose and amino acids
-
recombinant enzyme expressed from Pichia pastoris
-
from Merck
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
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
metabolism
the central event in prion infection is the conformational conversion of host-encoded cellular prion protein into the pathogenic isoform. For the in vitro replication of pathogenic prion protein by protein-misfolding cyclic amplification, cofactors are required that are not produced by lower organism, e.g. insects, but by mammalia, e.g. C57BL/6J mice. Brain-derived factors are also necessary for the in vitro replication of glycosylphosphatidylinositol-anchored baculovirus-derived recombinant prion protein. Cofactor activity of insect cell lysates becomes functional after proteinase K digestion and heat treatment, following protease digestion and heat treatment, insect cell lysates had the functional cofactor activity required for Bac-prion protein replication by protein-misfolding cyclic amplification. Not only RNA, but also DNA, are the key components of protein-misfolding cyclic amplification, although other cellular factors were necessary for the expression of the cofactor activity of nucleic acids in insect cells
metabolism
SPE-8 class proteins, such as Pron and ProK, act in the hermaphrodite- and male-dependent spermiogenesis pathways. Some spermatid proteins presumably working downstream of spermiogenesis pathways, including MAP kinases, are preferentially involved in the SPE-8 class-dependent pathway. Construction of a model in which Caenorhabditis elegans male and hermaphrodite spermiogenesis each has its own distinct, parallel pathway. proteinase K (ProK), a bacterial serine protease, can activate the SPE-8 class-independent pathway, SPE-8 class-dependent and class-independent pathways, overview. The spe-8 class genes are involved in both hermaphrodite- and male-dependent spermiogenesis and MAPKs are preferentially involved in the Pron- and Zn2+-activated SPE-8 class-dependent pathways
physiological function
proteinase K eliminate DNA from injured or dead bacteria but not from living bacteria in microbial reference systems and natural drinking water biofilms
physiological function
proteinase K (ProK) is an activator for the male-dependent spermiogenesis pathway in Caenorhabditis elegans. Caenorhabditis elegans spermiogenesis involves spermatid activation into spermatozoa. Activation occurs through either SPE-8 class-dependent or class-independent pathways. The microbe-derived serine protease ProK can also induce spermiogenesis in male-derived spermatids from N2 and spe-8 class mutants, i.e. spe-8(hc40), spe-12(hc76), spe-19(eb52) and spe-27(it110)
additional information
nonspecific protease proteinase K can be used as an alternative to trypsin for cross-linking studies, digestion by proteinase K results in a family of related cross-linked peptides, all of which contained the same cross-linking sites, thus providing additional verification of the cross-linking results. Using proteinase K, the affinity-purifiable CID-cleavable and isotopically coded cross-linker cyanurbiotindipropionylsuccinimide and MALDI-MS cross-links are found for all of the possible cross-linking sites of native and oligomeric forms of prion protein substrates, overview. After digestion with proteinase K, the mass distribution of the crosslinked peptides is very suitable for MALDI-MS analysis, detailed overview of cross-links in prion proteins
additional information
proteinase K-resistant Bac-prion protein is generated by protein-misfolding cyclic amplification using insect cells expressing the protein and prionprotein null mouse brain homogenate
additional information
dynamics of serine protease proteinase K, and effect of the solvent temperatures, proteinase K structure-function analysis, simulations, detailed overview
additional information
the catalytic triad and oxyanion hole of proteinase K are formed by Asp39, His69 and Ser224, and Asn161, respectively. Furthermore, two segments Asn99-Tyr104 and Ser132-Gly136 form substrate recognition site of proteinase K. Spermine quenches the intensity of proteinase K with static mechanism. Molecular docking using structure PDB ID 2ID8
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PRTK_PARAQ
384
0
40300
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28930
-
Tritirachium album, amino acid sequence analysis, the enzyme contains 2 disulfide bonds and a free cysteine residue
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
proteinase K is a monomeric and globular protein with 279 amino acid residues
additional information
the enzyme is a medium-sized globular protein (279 amino acids)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
computer modeling studies indicates the presence of a small binding pocket in the vicinity of the proteinase K active site, which may be filled by the aromatic phenylalanine moiety
Langmuir-Blodgett nanotemplate method and hanging drop vapor diffusion method, using 400 mM Na/K-tartrate in 25 mM HEPES pH 7.0
purified enzyme, oil microbatch method, mixing of 0.001 ml of 40 mg/ml protein solution in 50 mM MES-NaOH, pH 6.5, with 0.001 ml of precipitant solution composed of 250 mM NaNO3, 50 mM CaCl2, and 50 mM MES-NaOH, pH 6.5, to form Pr3+-derivatized crystals, the precipitant solution containing additionally 25 mM PrCl3 is used, X-ray diffraction structure determination and analysis at 1.45 A resolution
to 1.32 A resolution. final model contains two Ca2+ ions, a molecule of digalacturonic acid and a partially occupied HEPES molecule. The digalacturonic acid molecule has one sugar moiety disposed exactly on a crystallographic twofold axis and is bound through hydrogen-bonding networks involving residue S150 and water molecules
crystallographic study of its complex with a dipeptide chloromethyl ketone inhibitor
-
mercury-inhibited protein in presence of synthetic peptides GGGWGQPH and HGGGW, derived from N-terminal domain of human prion protein. Segment GGG is strongly bound as a substrate at the substrate recognition site
-
structure of the complex of proteinase K with a substrate analogue hexapeptide inhibitor at 2.2 A resolution, N-acetyl-L-Pro-L-Ala-L-Pro-L-Phe-D-Ala-L-Ala-NH2
-
the crystallization of proteinase K using PEG 8000 is performed at various degrees of solvent deuteration and X-ray crystallographic analysis at 1.1 A resolution confirms that deuteration has no effect on crystal quality or crystal structure in this case
-
three-dimensional structure of the complex of proteinase K with its naturally occuring protein inhibitor, PKI3
-
X-ray crystal structure at 1.5 A resolution shows that it has 2 binding sites for Ca2+
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
proteinase K is widely used in molecular biology for its broad substrate specificity, wide pH stability, and high hydrolysis activity. Aminolysis by proteinase K is also attractive for chemoenzymatic peptide synthesis
I310K
-
no effect on activity, increased stability of the serine protease subtilisin
M145F
-
no effect on activity, increased stability of the serine protease subtilisin
P265S
-
no effect on activity, increased stability of the serine protease subtilisin
P355S
-
no effect on activity, increased stability of the serine protease subtilisin
Y194S
-
no effect on activity, random mutation obtained during synthesis of wild-type proteinase K
additional information
additional information
immobilization of the enzyme proK. Compared to free proK, immobilized proK is much less efficient in inactivating beta-galactosidase, most likely due to a decreased mobility of immobilized proK and a restricted accessibility of the substrate to the active site of proK
additional information
proteinase K and Cu2+ ions are used to synthesize enzyme-inorganic hybrid nanoflowers (P-hNFs), method overview. The proteolytic activities and some important characteristics such as optimum pH and temperature of the P-hNFs are also evaluated by comparison with free proteinase K. Optimum pH values of free proteinase K and P-hNFs are determined as pH 10.0 and pH 11.0, respectively. Optimum temperatures recorded for both free proteinase K (at pH 10) and P-hNFs (at pH 11) are 40°C. The P-hNFs exhibit better activity than free proteinase K in the presence of all surfactants, i.e. CHAPS, DOC, SDS, Triton X-100 and Tergitol, except for Tween 80. Importantly, the P-hNFs is more stable and compatible with all tested solid laundry detergents. The P-hNFs can potentially be used as an additive in detergent formulations
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5
-
the enzyme acquires partially unfolded conformation at pH 2.5 with lower activity
707588
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16.2 - 80
the denaturation temperature of proteinase K derivatized with praseodymium (Pr) ions is 16.2°C, which is 5.9°C higher than those of metal-free and Ca2+-bound proteinase K, respectively. Isothermal titration calorimetry (ITC) measurements demonstrate that Pr-ion binding to proteinase K shows endothermic peaks, whereas Ca2+-ion binding shows exothermic peaks, indicating that the binding mode of Pr ions is different from that of Ca2+ ions, even though the crystal structures of proteinase K with Pr and Ca2+ ions are identical. Hydrolytic activity of Pr-derivatized proteinase K shows that the hydrolytic activity is 46fold higher at 70°C using synthetic nitroanilide substrate and 9 and 76fold higher at 70°C and 80°C using fluorescein isothiocyanate-labeled casein, respectively, in comparison with the native proteinase K. Furthermore, based on the yield of chemoenzymatic peptide syntheses, the aminolysis activity of Pr-derivatized proteinase K is 3.5 and 9.5fold higher than that of the native proteinase K at 50°C and 60°C, respectively
50
-
30 min, 19% residual activity in presence of 1% sodium dodecylsulfate
66
-
thermal unfolding is cooperative at pH 7.0 with transition midpoint of 66°C
additional information
additional information
-
Ca2+ contributes to the overal stability of the surface regions and improves the thermal stability
additional information
-
depletion of Ca2+ increases the rate of autolysis after about 48 h, it reduces the thermal stability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
interaction of proteinase K with spermine, multispectroscopic study and molecular simulation, structure-function analysis, overview. The stability and enzyme activity of proteinase K-spermine complex are significantly enhanced as compared to the pure enzyme, secondary structure alteration of proteinase K with an increase in alpha-helicity and a decrease in beta-sheet of proteinase K upon spermine conjugation
Depletion of Ca2+ increases the rate of autolysis after about 48 h, it reduces the thermal stability and enhances the deactivation by 8 M urea
-
proteinase K is losing the proteolytic activity as the enzyme is attaining beta conformation
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isopropanol
-
at 40% (v/v) isopropanol nearly half and at 50% (v/v) isopropanol all the tertiary structure is lost, beyond 30% (v/v) isopropanol there is some perturbation in the secondary structure of the protein
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
tagged cellular Bac-prion protein fusion partially 37fold from SF21 insect cells using immobilized metal ion affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of tagged cellular Bac-prion protein fusion in Spodoptera frugiperda SF21 insect cells via baculovirus transfection system
gene encoding proteinase K re-synthesized with an Escherichia coli codon bias and cloned into an arabinose-inducible Escherichia coli expression vector
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
DNase I and proteinase K eliminate DNA from injured or dead bacteria but not from living bacteria in microbial reference systems and natural drinking water biofilms for subsequent molecular biology analyses, method evaluation, overview
detergent
synthesized enzyme-inorganic hybrid nanoflowers (P-hNFs) can potentially be used as an additive in detergent formulations
diagnostics
prion disease diagnosis relies on the relative resistance of sensitive prion protein Sc, PtPSc, to the non-specific protease proteinase K in brain samples to discriminate between resistant and senstive prions, PrPC and PrPSc, in combination with immunological detection of the main enzyme-resistant part of PrPSc (PrP27-30)
molecular biology
proteinase K from Tritirachium album, which is one of the most widely used proteases in molecular biological studies. The synthesized linear oligo-phenylalanine shows a unique self-assembly in aqueous solutions
synthesis
chemoenzymatic synthesis of oligo(L-phenylalanine) by the enzyme as a green and clean chemical reaction compared to organic synthesis
analysis
-
protein engineering approach for increasing activity and heat stability of proteinase K. Protein design algorithms that only require the testing of a small number of variants represent a significant step towards a generic, resource-optimized protein engineering process
biotechnology
-
proteinase K is successfully applied for the activation of purified pro-recombinant transglutaminase either as free or immobilized enzyme and the free enzyme is also applicable directly in the crude cell extract of Escherichia coli. Proteinase K enables a simple two-step activation/purification procedure resulting in protease-free and almost pure transglutaminase preparations
medicine
pharmacology
-
In human variant CreutzfeldtJakob disease, up to 90% of total prion protein present in the brain resists degradation with thermolysin, whereas only ?15% of this material resists digestion by proteinase K. Detection of proteinase K-sensitive isoforms of disease-related prion protein using thermolysin should be useful for improving diagnostic sensitivity in human prion diseases
analysis
nonspecific protease proteinase K can be used as an alternative to trypsin for cross-linking studies, digestion by proteinase K results in a family of related cross-linked peptides, all of which contained the same cross-linking sites, thus providing additional verification of the cross-linking results. Using proteinase K, the affinity-purifiable CID-cleavable and isotopically coded cross-linker cyanurbiotindipropionylsuccinimide and MALDI-MS cross-links are found for all of the possible cross-linking sites of native and oligomeric forms of prion protein substrates, overview. After digestion with proteinase K, the mass distribution of the crosslinked peptides is very suitable for MALDI-MS analysis
analysis
improvement of RNA extraction from papillary cancer-derived K1 cells and thyroid fine-needle aspiration biopsy (FNAB) specimens suspended in liquid-based cytology (LBC) solutions during fine-needle aspiration biopsy diagnostics of thyroid diseases. Commercial proteinase K treatment is essential for efficient RNA extraction from the fixed cells. Proteinase K treatment facilitates RNA recovery from rigid cells after dehydration. RNA molecules are largely released from the fixed cells even after 1-h treatment. U6 small nuclear RNA was detected in these RNA samples by reverse transcription-PCR. Method overview
medicine
-
segment GGG of functionally important N-terminal octapeptide region of human prion protein, involved in spongifirm encephalopathy, strongly binds as a substrate at the substrate recognition site
medicine
-
PK magnetic reactor is a useful tool for prion protein digestion
medicine
-
proteinase K can be used in combination with antibiotics to enhance the dispersal/control of biofilms
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Betzel, C.; Teplyakov, A.V.; Harutyunyan, E.H.; Saenger, W.; Wilson, K.S.
Thermitase and proteinase K: a comparison of the refined three-dimensional structures of the native enzymes
Protein Eng.
3
161-172
1990
Parengyodontium album
Ebeling, W.; Hennrich, N.; Klockow, M.; Metz, H.; Orth, H.D.; Lang, H.
Proteinase K from Tritirachium album Limber
Eur. J. Biochem.
47
91-97
1974
Parengyodontium album
Morihara, K.; Tsuzuki, H.
Specificity of proteinase K from Tritirachium album Limber for synthetic peptides
Agric. Biol. Chem.
39
1489-1492
1975
Parengyodontium album
-
Kraus, E.; Kiltz, H.H.; Femfert, U.F.
The specificity of proteinase K against oxidized insulin B chain
Hoppe-Seyler's Z. Physiol. Chem.
357
233-237
1976
Parengyodontium album
Jany, K.D.; Lederer, G.; Mayer, B.
Amino acid sequence of proteinase K from the mold Tritirachium album Limber
FEBS Lett.
199
139-144
1986
Parengyodontium album
-
Hilz, H.; Wiegers, U.; Adamietz, P.
Stimulation of proteinase K action by denaturing agents: application to the isolation of nucleic acids and the degradation of masked proteins
Eur. J. Biochem.
56
103-108
1975
Parengyodontium album
Dattagupta, J.K.; Fujiwara, T.; Grishin, E.V.; Lindner, K.; Manor, P.C.; Pieniazek, N.J.; Saenger, W.; Suck, D.
Crystallization of the fungal enzyme proteinase K and amino acid composition
J. Mol. Biol.
97
267-271
1975
Parengyodontium album
Hilz, H.; Fanick, W.
Divergent denaturation of proteases by urea and dodecylsulfate in the absence of substrate
Hoppe-Seyler's Z. Physiol. Chem.
359
1447-1450
1978
Parengyodontium album
Pellegrini, A.; Hgeli, G.; von Fellenberg, R.
Isolation and characterization of two new low-molecular-weight protein proteinase inhibitors from the granule-rich fraction of equine neutrophilic granulocytes
Biochim. Biophys. Acta
952
309-316
1988
Parengyodontium album
Bajorath, J.; Hinrichs, W.; Saenger, W.
The enzymatic activity of proteinase K is controlled by calcium
Eur. J. Biochem.
176
441-447
1988
Parengyodontium album
Betzel, C.; Pal, G.P.; Saenger, W.
Three-dimensional structure of proteinase K at 0.15-nm resolution
Eur. J. Biochem.
178
155-171
1988
Parengyodontium album
Ardelt, W.; Laskowski, M.
Turkey ovomucoid third domain inhibits eight different serine proteinases of varied specificity on the same ...Leu18-Glu19 ... reactive site
Biochemistry
24
5313-5320
1985
Parengyodontium album
Betzel, C.; Pal, G.P.; Struck, M.; Jany, K.D.; Saenger, W.
Active-site geometry of proteinase K. Crystallographic study of its complex with a dipeptide chloromethyl ketone inhibitor
FEBS Lett.
197
105-110
1986
Parengyodontium album
Phler, A.; Banerjee, A.; Dattagupta, J.K.; Fujiwara, T.; Lindner, K.; Pal, G.P.; Suck, D.; Weber, G.; Saenger, W.
Three-dimensional structure of fungal proteinase K reveals similarity to bacterial subtilisin
EMBO J.
3
1311-1314
1984
Parengyodontium album
Muller, A.; Hinrichs, W.; Wolf, W.M.; Saenger, W.
Crystal structure of calcium-free proteinase K at 1.5-A resolution
J. Biol. Chem.
269
23108-23111
1994
Parengyodontium album
Betzel, C.; Singh, T.P.; Visanji, M.; Peters, K.; Fittkau, S.; Saenger, W.; Wilson, K.S.
Structure of the complex of proteinase K with a substrate analogue hexapeptide inhibitor at 2.2-A resolution
J. Biol. Chem.
268
15854-15858
1993
Parengyodontium album
Segal, D.; Shalitin, Y.; Wingert, H.; Kitamura, T.; Stang, P.J.
The interaction of alkynyl carboxylates with serine enzymes. A potent new class of serine enzyme inhibitors
FEBS Lett.
247
217-220
1989
Parengyodontium album
Jany, K.D.; Nitsche, E.
Limited proteolysis of glucose dehydrogenase from Bacillus megaterium by proteinase K
Hoppe-Seyler's Z. Physiol. Chem.
364
839-844
1983
Parengyodontium album
Pal, G.P.; Kavounis, C.A.; Jany, K.D.; Tsernoglou, D.
The three-dimensional structure of the complex of proteinase K with its naturally occurring protein inhibitor, PKI3
FEBS Lett.
341
167-170
1994
Parengyodontium album
Bajorath, J.; Raghunathan, S.; Hinrichs, W.; Saenger, W.
Long-range structural changes in proteinase K triggered by calcium ion removal
Nature
337
481-484
1989
Parengyodontium album
Okotore, R.O.; Uhlenbruck, G.
Proteinase inhibitors in albumin glands of Achatina fulica
Z. Naturforsch. C
37
142-144
1982
Parengyodontium album
-
Orstan, A.; Gafni, A.
Inhibition of proteinase K by phosphorylated sugars
Biochem. Int.
25
657-662
1991
Parengyodontium album
Uhlenbruck, G.; Sprenger, I.; Ishiyama, I.
A new polyvalent proteinase-inhibitor occurring in the albumin gland of Helix pomatia
Z. Klin. Chem. Klin. Biochem.
9
361-362
1971
Parengyodontium album
Sprenger, I.; Uhlenbruck, G.; Hermann, G.
Snail albumin gland: a new source of proteinase inhibitors
Enzymologia
43
83-88
1972
Parengyodontium album
Georgieva, D.; Rypniewski, W.; Echner, H.; Perbandt, M.; Koker, M.; Clos, J.; Redecke, L.; Bredehorst, R.; Voelter, W.; Genov, N.; Betzel, C.
Synthetic human prion protein octapeptide repeat binds to the proteinase K active site
Biochem. Biophys. Res. Commun.
325
1406-1411
2004
Parengyodontium album
Larsen, A.N.; Moe, E.; Helland, R.; Gjellesvik, D.R.; Willassen, N.P.
Characterization of a recombinantly expressed proteinase K-like enzyme from a psychrotrophic Serratia sp
FEBS J.
273
47-60
2006
Parengyodontium album, Serratia sp.
Slovakova, M.; Peyrin, J.M.; Bilkova, Z.; Juklickova, M.; Hernychova, L.; Viovy, J.L.
Magnetic proteinase K reactor as a new tool for reproducible limited protein digestion
Bioconjug. Chem.
19
966-972
2008
Parengyodontium album
Liao, J.; Warmuth, M.K.; Govindarajan, S.; Ness, J.E.; Wang, R.P.; Gustafsson, C.; Minshull, J.
Engineering proteinase K using machine learning and synthetic genes
BMC Biotechnol.
7
16
2007
Parengyodontium album
Gardberg, A.S.; Blakeley, M.P.; Myles, D.A.
A preliminary neutron crystallographic study of proteinase K at pD 6.5
Acta Crystallogr. Sect. F
65
184-187
2009
Parengyodontium album (P06873)
Larson, S.B.; Day, J.S.; Nguyen, C.; Cudney, R.; McPherson, A.
High-resolution structure of proteinase K cocrystallized with digalacturonic acid
Acta Crystallogr. Sect. F
65
192-198
2009
Parengyodontium album (P06873)
Cronier, S.; Gros, N.; Tattum, M.H.; Jackson, G.S.; Clarke, A.R.; Collinge, J.; Wadsworth, J.D.
Detection and characterization of proteinase K-sensitive disease-related prion protein with thermolysin
Biochem. J.
416
297-305
2008
Parengyodontium album
Kore, A.R.; Shanmugasundaram, M.; Hoang, Q.; Kuo, M.; Chapman, L.M.; Chen, H.H.
Synthesis and application of MeOSuc-Ala-Ala-Pro-Phe-CH2Cl as potent proteinase K inhibitor
Bioorg. Med. Chem. Lett.
19
1296-1300
2009
Parengyodontium album (P06873)
Tomar, R.; Dubey, V.K.; Jagannadham, M.V.
Effect of alkyl alcohols on partially unfolded state of proteinase K: Differential stability of alpha-helix and beta-sheet rich regions of the enzyme
Biochimie
91
951-960
2009
Parengyodontium album
Liu, S.; Meng, Z.; Fu, Y.; Zhang, K.
Insights derived from molecular dynamics simulation into the molecular motions of serine protease proteinase K
J. Mol. Model.
16
17-28
2010
Parengyodontium album
Liu, S.Q.; Tao, Y.; Meng, Z.H.; Fu, Y.X.; Zhang, K.Q.
The effect of calciums on molecular motions of proteinase K
J. Mol. Model.
17
289-300
2011
Parengyodontium album
Zauner, G.; Koeleman, C.A.; Deelder, A.M.; Wuhrer, M.
Protein glycosylation analysis by HILIC-LC-MS of Proteinase K-generated N- and O-glycopeptides
J. Sep. Sci.
33
903-910
2010
Parengyodontium album
Pechkova, E.; Tripathi, S.; Ravelli, R.B.; McSweeney, S.; Nicolini, C.
Radiation stability of proteinase K crystals grown by LB nanotemplate method
J. Struct. Biol.
168
409-418
2009
Parengyodontium album (P06873)
Panek, J.J.; Mazzarello, R.; Novic, M.; Jezierska-Mazzarello, A.
Impact of mercury(II) on proteinase K catalytic center: investigations via classical and Born-Oppenheimer molecular dynamics
Mol. Divers.
15
215-226
2011
Parengyodontium album
Chatake, T.; Ishikawa, T.; Yanagisawa, Y.; Yamada, T.; Tanaka, I.; Fujiwara, S.; Morimoro, Y.
High-resolution X-ray study of the effects of deuteration on crystal growth and the crystal structure of proteinase K
Acta Crystallogr. Sect. F
67
1334-1338
2011
Parengyodontium album
Sommer, C.; Hertel, T.; Schmelzer, C.; Pietzsch, M.
Investigations on the activation of recombinant microbial pro-transglutaminase: in contrast to proteinase K, dispase removes the histidine-tag
Amino Acids
42
997-1006
2012
Parengyodontium album
Tao, Y.; Rao, Z.; Liu, S.
Insight derived from molecular dynamics simulation into substrate-induced changes in protein motions of proteinase K
J. Biomol. Struct. Dyn.
28
143-157
2010
Parengyodontium album
Tiberti, M.; Papaleo, E.
Dynamic properties of extremophilic subtilisin-like serine-proteases
J. Struct. Biol.
174
69-83
2011
Parengyodontium album
Ageitos, J.M.; Baker, P.J.; Sugahara, M.; Numata, K.
Proteinase K-catalyzed synthesis of linear and star oligo(L-phenylalanine) conjugates
Biomacromolecules
14
3635-3642
2013
Parengyodontium album (P06873)
Kumar Shukla, S.; Rao, T.S.
Dispersal of Bap-mediated Staphylococcus aureus biofilm by proteinase K
J. Antibiot.
66
55-60
2013
Parengyodontium album
Villarreal, J.V.; Jungfer, C.; Obst, U.; Schwartz, T.
DNase I and proteinase K eliminate DNA from injured or dead bacteria but not from living bacteria in microbial reference systems and natural drinking water biofilms for subsequent molecular biology analyses
J. Microbiol. Methods
94
161-169
2013
Parengyodontium album (P06873)
Petrotchenko, E.V.; Serpa, J.J.; Hardie, D.B.; Berjanskii, M.; Suriyamongkol, B.P.; Wishart, D.S.; Borchers, C.H.
Use of proteinase K nonspecific digestion for selective and comprehensive identification of interpeptide cross-links: application to prion proteins
Mol. Cell. Proteomics
11
M111.013524
2012
Parengyodontium album (P06873)
Imamura, M.; Kato, N.; Okada, H.; Yoshioka, M.; Iwamaru, Y.; Shimizu, Y.; Mohri, S.; Yokoyama, T.; Murayama, Y.
Insect cell-derived cofactors become fully functional after proteinase K and heat treatment for high-fidelity amplification of glycosylphosphatidylinositol-anchored recombinant scrapie and BSE prion proteins
PLoS ONE
8
e82538
2013
Parengyodontium album (P06873)
Sajnani, G.; Requena, J.R.
Prions, proteinase K and infectivity
Prion
6
430-432
2012
Parengyodontium album (P06873)
Yazawa, K.; Sugahara, M.; Yutani, K.; Takehira, M.; Numata, K.
Derivatization of proteinase K with heavy atoms enhances its thermal stability
ACS Catal.
6
3036-3046
2016
Parengyodontium album (P06873)
-
Gheczy, N.; Kuechler, A.; Walde, P.
Proteinase K activity determination with beta-galactosidase as sensitive macromolecular substrate
Anal. Biochem.
513
54-60
2016
Parengyodontium album (P06873)
Jikuzono, T.; Horikawa, A.; Ishikawa, T.; Hirokawa, M.; Sugitani, I.; Inui, T.; Ishibashi, O.
Proteinase K treatment improves RNA recovery from thyroid cells fixed with liquid-based cytology solution
BMC Res. Notes
11
822
2018
Parengyodontium album (P06873)
Tajima, T.; Ogawa, F.; Nakamura, S.; Hashimoto, M.; Omote, M.; Nishimura, H.
Proteinase K is an activator for the male-dependent spermiogenesis pathway in Caenorhabditis elegans Its application to pharmacological dissection of spermiogenesis
Genes Cells
24
244-258
2019
Parengyodontium album (P06873)
Gulmez, C.; Altinkaynak, C.; Oezdemir, N.; Atakisi, O.
Proteinase K hybrid nanoflowers (P-hNFs) as a novel nanobiocatalytic detergent additive
Int. J. Biol. Macromol.
119
803-810
2018
Parengyodontium album (P06873)
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
Int. J. Biol. Macromol.
122
732-744
2019
Parengyodontium album (P06873)
Hosseini-Koupaei, M.; Shareghi, B.; Saboury, A.A.; Davar, F.
Molecular investigation on the interaction of spermine with proteinase K by multispectroscopic techniques and molecular simulation studies
Int. J. Biol. Macromol.
94
406-414
2017
Parengyodontium album (P06873)
Sang, P.; Yang, Q.; Du, X.; Yang, N.; Yang, L.Q.; Ji, X.L.; Fu, Y.X.; Meng, Z.H.; Liu, S.Q.
Effect of the solvent temperatures on dynamics of serine protease proteinase K
Int.J. Mol. Sci.
17
254
2016
Parengyodontium album (P06873)
Hosseini-Koupaei, M.; Shareghi, B.; Saboury, A.; Davar, F.; Raisi, F.
The effect of spermidine on the structure, kinetics and stability of proteinase K spectroscopic and computational approaches
RSC Adv.
6
105476-105486
2016
Parengyodontium album (P06873)
-
EXTERNAL LINKS (specific for EC-Number 3.4.21.64)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
