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Information on EC 3.4.21.64 - peptidase K
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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 expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
endopeptidase k, tritirachium alkaline proteinase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 3.4.21.14
EC 3.4.4.16
-
-
formerly, part transferred
-
endopeptidase K
Proteinase K
Proteinase, Tritirachium album serine
-
-
-
-
Tritirachium album proteinase K
-
-
-
-
Tritirachium alkaline proteinase
-
-
-
-
EC 3.4.21.14
-
-
formerly
-
Proteinase K
-
-
-
-
Proteinase K
-
-
Proteinase K
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyses peptide amides
hydrolysis of keratin, and of other proteins with subtilisin-like specificity
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
39450-01-6
-
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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
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
-
-
?
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
-
-
?
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
-
-
-
-
?
creatine kinase + H2O
?
Tritirachium album Limber
-
inactivation of rabbit muscle creatine kinase by processing
-
?
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-Ala-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + p-nitroaniline
Tritirachium album Limber
-
-
-
?
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Leu + p-nitroaniline
-
-
-
-
?
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
-
-
?
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
?
poly(L-lactide) + H2O
?
-
enzyme moves on the surface of substrate film to hydrolyze the film around it
-
-
?
pro-recombinant transglutaminase + H2O
?
-
successful cleavage at the pro-sequence
-
-
?
succinyl-AAPF-4-nitroanilide + H2O
succinyl-AAPF + 4-nitroaniline
-
-
-
?
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
-
-
?
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
-
-
?
prion protein + H2O
?
specific cleavage, that does not occur at cross-linker-modified residues
-
-
?
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
-
-
?
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
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-
?
additional information
?
-
Tritirachium album Limber
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exhibits a preference for carboxy groups adjacent to aliphatic and aromatic acids and especially those adjacent to alanine residues
-
?
additional information
?
-
Tritirachium album Limber
-
PK is very effective in destroying cellular prion proteins and endogenous proteases present in brain homogenate
-
-
?
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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
?
-
-
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
-
-
?
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Calcium
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
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
ytterbium
1 mM YbCl3, differential scanning calorimetry analysis bound to the enzyme
additional information
differential scanning calorimetry curves for proteinase K derivatized with heavy atoms, showing the correlation between atomic number and denaturation temperature, overview
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
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Chloromethyl ketone derivatives
-
e.g. carboxybenzoyl-Ala-Gly-PheCH2Cl, carboxybenzoyl-Ala-PheCH2Cl
Cu2+
Tritirachium album Limber
-
at equilibrium two to three copper ions bind stoichiometrically to PK and destroy its activity. Initial reversible and weak binding phase and a slower, irreversible abolition of activity with a half-time of 6 min at saturating copper ion concentrations. PK digestion of cellular prion proteins and other proteins in brain homogenate is inhibited in a concentration-dependent manner at concentrations of more than 1 mM. Presence of calcium ions, up to 10 mM, has no effect on copper inhibition
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
-
-
-
MeOSuc-Ala-Ala-Ala-Pro-Phe-CH2Cl
-
inhibits proteinase K (100 microgram/ml) at concentrations as low as 0.25 mM
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)
-
Polyvalent proteinase inhibitor from albumin gland of Helix pomatia
-
-
-
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
Turkey ovomucoid
-
enzyme interacts with the third domain at the Leu18-Glu19 peptide bond, the reactive site of the inhibitor
-
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
EDTA
-
22°C, not inhibitory, 37%, 60% residual activity, 50°C, complete inhibition
PKI3
-
consists of 180 amino acids with a MW of 19641; natural inhibitor isolated from wheat
-
PKI3
-
crystallization of the inhibitor; natural inhibitor isolated from wheat
-
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
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
additional information
-
MeOSuc-Ala-Ala-Ala-Pro-Val-CH2Cl does not inhibit proteinase K (100 microgram/ml) at concentrations as high as 0.75 mM
-
additional information
-
immobilization of PK on magnetic latex microparticles (500A5 microparticles) and other chemically and structurally similar types of magnetic carriers
-
additional information
several DDI-1 structure analogues block Pron- but not ProK-induced spermiogenesis
-
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
-
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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
-
additional information
Tritirachium album Limber
-
presence of calcium ions, up to 10 mM, has no effect on enzymatic activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma, Ehrlich Tumor
Evidence for the presence of a trypsin inhibitor within rabbit and mouse tumour cells.
Carcinoma, Ehrlich Tumor
Inhibition of trypsin and chymotrypsin by thiols. Biphasic kinetics of reactivation and inhibition induced by sodium periodate addition.
Malnutrition
Comparative changes between pancreas and pancreatic juice digestive enzyme contents during nutritional rehabilitation following severe protein malnutrition in the rat.
Neoplasms
Evidence for the presence of a trypsin inhibitor within rabbit and mouse tumour cells.
Neoplasms
Inhibition of trypsin and chymotrypsin by thiols. Biphasic kinetics of reactivation and inhibition induced by sodium periodate addition.
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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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
88.6
additional information
additional information
Tritirachium album Limber
-
specific activity 8.8 U/mg, the activity unit used is absorbance unit, defined as increase of one in absorbance as measured by Lowry's method at 578 nm
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 7
-
proteinase K maintains structural integrity in the range of pH 3.0-7.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
70
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
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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