Information on EC 3.4.21.64 - peptidase K

Word Map on EC 3.4.21.64
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.4.21.64
-
RECOMMENDED NAME
GeneOntology No.
peptidase K
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyses peptide amides
show the reaction diagram
hydrolysis of keratin, and of other proteins with subtilisin-like specificity
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
39450-01-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Engyodontium album
-
-
-
Manually annotated by BRENDA team
commercial preparation from Roche Diagnostics
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Tritirachium album Limber
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
Engyodontium album
-
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
physiological function
Engyodontium album
-
proteinase K eliminate DNA from injured or dead bacteria but not from living bacteria in microbial reference systems and natural drinking water biofilms
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
AAPA + H2O
?
show the reaction diagram
Engyodontium album
-
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
-
-
?
Acetyl-Tyr ethyl ester + H2O
?
show the reaction diagram
Engyodontium album
-
-
-
-
-
Aldolase + H2O
Hydrolyzed aldolase
show the reaction diagram
Engyodontium album
-
-
-
-
-
Alkynyl carboxylates + H2O
?
show the reaction diagram
Engyodontium album
-
-
-
-
-
asialofetuin + H2O
?
show the reaction diagram
Engyodontium album
-
-
-
-
?
Bap protein + H2O
?
show the reaction diagram
Engyodontium album
-
degradation
-
-
?
Bovine ribonuclease + H2O
Hydrolyzed bovine ribonuclease
show the reaction diagram
Engyodontium album
-
-
-
-
-
Bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
Engyodontium album
-
-
-
-
?
casein + H2O
hydrolyzed casein
show the reaction diagram
Engyodontium album
-
-
-
-
-
creatine kinase + H2O
?
show the reaction diagram
Tritirachium album Limber
-
inactivation of rabbit muscle creatine kinase by processing
-
?
fetuin + H2O
?
show the reaction diagram
Engyodontium album
-
-
-
-
?
Glucose dehydrogenase + H2O
Hydrolyzed glucose dehydrogenase
show the reaction diagram
Engyodontium album
-
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
?
show the reaction diagram
Engyodontium album
-
proteolytic activity and specificity of PK is maintained after its immobilization to magnetic particles
-
-
?
human sensitive prion protein Sc + H2O
?
show the reaction diagram
Keratin + H2O
?
show the reaction diagram
Engyodontium album
-
-
-
-
?
Keratin + H2O
Hydrolyzed keratin
show the reaction diagram
Engyodontium album
-
-
-
-
-
Lactate dehydrogenase + H2O
Hydrolyzed lactate dehydrogenase
show the reaction diagram
Engyodontium album
-
-
-
-
-
N-Acetylated amino acid esters + H2O
?
show the reaction diagram
Engyodontium album
-
-
-
-
-
N-Acetylated peptide esters + H2O
?
show the reaction diagram
Engyodontium album
-
-
-
-
-
N-succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + p-nitroaniline
show the reaction diagram
Tritirachium album Limber
-
-
-
?
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Leu + p-nitroaniline
show the reaction diagram
Engyodontium album
-
-
-
-
?
normal cellular prion protein + H2O
pathogenic cellular prion protein + ?
show the reaction diagram
Engyodontium album
-
in mouse brain
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
show the reaction diagram
Engyodontium album
-
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
-
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
Tritirachium album Limber
-
-
-
-
?
poly(L-lactide) + H2O
?
show the reaction diagram
-
enzyme moves on the surface of substrate film to hydrolyze the film around it
-
-
?
prion protein + H2O
?
show the reaction diagram
pro-recombinant transglutaminase + H2O
?
show the reaction diagram
Engyodontium album
-
successful cleavage at the pro-sequence
-
-
-
Propynyl benzoate + H2O
?
show the reaction diagram
Engyodontium album
-
-
-
-
-
ribonuclease A + H2O
proteolytic fragments
show the reaction diagram
Tritirachium album Limber
-
-
-
?
Serum albumin + H2O
Hydrolyzed serum albumin
show the reaction diagram
Engyodontium album
-
-
-
-
-
succinyl-AAPF-4-nitroanilide + H2O
?
show the reaction diagram
Succinyl-Ala-Ala-Ala 2-nitroanilide + H2O
?
show the reaction diagram
Engyodontium album
-
-
-
-
-
Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
?
show the reaction diagram
Engyodontium album
-
-
-
-
-
succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
succinyl-Ala-Ala-Ala + p-nitroaniline
show the reaction diagram
Engyodontium album
-
-
-
-
?
Synthetic peptide substrates + H2O
?
show the reaction diagram
Engyodontium album
-
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
show the reaction diagram
Engyodontium album
-
-
-
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Bap protein + H2O
?
show the reaction diagram
Engyodontium album
-
degradation
-
-
?
human sensitive prion protein Sc + H2O
?
show the reaction diagram
Engyodontium album
-
degradation, pathogenic isoform, sensitive prion protein complexes show higher molecular weight than resistant prions
-
-
?
Keratin + H2O
?
show the reaction diagram
Engyodontium album
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Calcium
SDS
Engyodontium album
-
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
Engyodontium album
-
stimulates hydrolysis of serum albumin in a dose-dependent manner, caused primarily by denaturation of the protein substrate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Carbobenzoxy-Ala-Ala-chloromethyl ketone
Engyodontium album
-
-
Chloromethyl ketone derivatives
Engyodontium album
-
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
DFP
Engyodontium album
-
-
fructose 1,6-diphosphate
Engyodontium album
-
mixed-type inhibition, more than one inhibitor molecule binds to proteinase K
glucose 6-phosphate
Engyodontium album
-
mixed-type inhibition, more than one inhibitor molecule binds to proteinase K
Hg2+
Engyodontium album
-
-
Inhibitor from Helix aspersa
Engyodontium album
-
weak
-
Low-molecular-weight protein proteinase inhibitors from the granule-rich fraction of equine neutrophilic granulocytes
Engyodontium album
-
-
-
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
Engyodontium album
-
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
MeOSuc-Ala-Ala-Pro-Val-CH2Cl
-
strong inhibitor
MeOSuc-Ala-Pro-Ala-Leu-CH2Cl
-
weak inhibitor
N-Acetyl-L-Pro-L-Ala-L-Pro-L-Phe-D-Ala-L-Ala-NH2
Engyodontium album
-
substrate analogue
phenylmethylsulfonyl fluoride
Engyodontium album
-
-
PKI3
-
PMSF
Engyodontium album
-
-
Polyvalent proteinase inhibitor from albumin gland of Helix pomatia
Engyodontium album
-
-
-
Proteinase-inhibitors from the albumin gland of Achatina fulica
Engyodontium album
-
-
-
SDS
Engyodontium album
-
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
Engyodontium album
-
enzyme interacts with the third domain at the Leu18-Glu19 peptide bond, the reactive site of the inhibitor
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetonitrile
Tritirachium album Limber
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
acetyl-(Ala)2-Ala methyl ester
Engyodontium album
-
-
0.8
acetyl-(Ala)2-Phe methyl ester
Engyodontium album
-
-
45
Acetyl-Ala methyl ester
Engyodontium album
-
-
30
acetyl-Leu methyl ester
Engyodontium album
-
-
12
acetyl-Phe ethyl ester
Engyodontium album
-
-
5.6
acetyl-Trp ethyl ester
Engyodontium album
-
-
8.8
Acetyl-Tyr ethyl ester
Engyodontium album
-
-
26
acetyl-Val methyl ester
Engyodontium album
-
-
3.3
benzoyl-Arg ethyl ester
Engyodontium album
-
-
0.9
carboxybenzoyl-(Ala)2-Lys methyl ester
Engyodontium album
-
-
3
carboxybenzoyl-Ala-Lys methyl ester
Engyodontium album
-
carboxybenzoyl-Phe-Lys methyl ester
20
carboxybenzoyl-D-Ala-Lys methyl ester
Engyodontium album
-
-
19
carboxybenzoyl-Gly-Lys methyl ester
Engyodontium album
-
-
9
carboxybenzoyl-Leu-Lys methyl ester
Engyodontium album
-
-
21
carboxybenzoyl-Lys methyl ester
Engyodontium album
-
-
0.46 - 2.76
succinyl-AAPF-4-nitroanilide
1.29 - 4.23
succinyl-Ala-Ala-Ala-p-nitroanilide
additional information
additional information
Engyodontium album
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
51 - 827
succinyl-AAPF-4-nitroanilide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 12
Engyodontium album
-
urea-denatured hemoglobin
7.5
Engyodontium album
-
assay at
8 - 8.5
Engyodontium album
-
assay at
8
Engyodontium album
-
-
10.5
-
-
additional information
Engyodontium album
-
pI: 8.9
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 7
Engyodontium album
-
proteinase K maintains structural integrity in the range of pH 3.0-7.0
6.7 - 7.4
Tritirachium album Limber
-
-
8 - 9.5
Engyodontium album
-
-
8 - 11
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
Engyodontium album
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
Engyodontium album
-
soluble and immobilized enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.4
Engyodontium album
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Engyodontium album
-
-
Manually annotated by BRENDA team
Engyodontium album
-
secretion starts when the stationary phase of growth is reached, and when the culture medium is depleted of glucose and amino acids
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Engyodontium album
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28930
Engyodontium album
-
Tritirachium album, amino acid sequence analysis, the enzyme contains 2 disulfide bonds and a free cysteine residue
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 65500, precursor-protein, calculated, x * 34000, mature protein, SDS-PAGE
monomer
Engyodontium album
-
1 * 28930, Tritirachium album, amino acid sequence analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
sequence consists of preproregion, catalytic domain and two C-terminal domains. Catalytic domain with the two C-terminal domains is an active protein of 56 kDa that converts at 50C by autolytic cleavage to mature 34 kDa protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Engyodontium album
-
at 0.15 nm resolution
Engyodontium album
-
at 1.5 A resolution
Engyodontium album
-
at 3.3 A resolution
Engyodontium album
-
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
Engyodontium album
-
crystallographic study of its complex with a dipeptide chloromethyl ketone inhibitor
Engyodontium album
-
Langmuir-Blodgett nanotemplate method and hanging drop vapor diffusion method, using 400 mM Na/K-tartrate in 25 mM HEPES pH 7.0
Engyodontium album
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
Engyodontium album
-
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
Engyodontium album
-
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
Engyodontium album
-
three-dimensional structure at 1.48 A resolution
Engyodontium album
-
three-dimensional structure of the complex of proteinase K with its naturally occuring protein inhibitor, PKI3
Engyodontium album
-
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
Engyodontium album
-
to 2.3 A resolution, space group P43212
Engyodontium album
-
X-ray crystal structure at 1.5 A resolution shows that it has 2 binding sites for Ca2+
Engyodontium album
-
-
Tritirachium album Limber
-
space group P4(3)2(1)2, cell dimensions a = b = 67.3 A, c = 106.6 A
Tritirachium album Limber
-
space group P4(3)2(1)2, cell dimensions a = b = 68.3, c = 108.4
Tritirachium album Limber
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5
Engyodontium album
-
the enzyme acquires partially unfolded conformation at pH 2.5 with lower activity
707588
4 - 12
Engyodontium album
-
-
668577
5.5 - 9.5
-
-
668577
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
30 min, about 90% residual activity even in presence of 1% sodium dodecylsulfate
46
Engyodontium album
-
15 min, 50% loss of activity of Ca2+-free enzyme
60
Tritirachium album Limber
-
retains 83% activity after 2 h
65
Engyodontium album
-
15 min, 50% loss of activity of Ca2+-saturated enzyme
66
Engyodontium album
-
thermal unfolding is cooperative at pH 7.0 with transition midpoint of 66C
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
Engyodontium album
-
proteinase K is losing the proteolytic activity as the enzyme is attaining beta conformation
Engyodontium album
-
Relatively resistant to SDS, 0.2% in 50 mM Tris/HCl, pH 7.4
Engyodontium album
-
Relatively stable towards heat and denaturing agents
Engyodontium album
-
Urea, 4 M, stable
Engyodontium album
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isopropanol
Engyodontium album
-
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
4C, stable for at least 12 months
Engyodontium album
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutants purified over a Ni-NTA column
Engyodontium album
-
tagged cellular Bac-prion protein fusion partially 37fold from SF21 insect cells using immobilized metal ion affinity chromatography
Engyodontium album
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene encoding proteinase K re-synthesized with an Escherichia coli codon bias and cloned into an arabinose-inducible Escherichia coli expression vector
Engyodontium album
-
recombinant expression of tagged cellular Bac-prion protein fusion in Spodoptera frugiperda SF21 insect cells via baculovirus transfection system
Engyodontium album
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A199S
Engyodontium album
-
no effect on activity
A236V
Engyodontium album
-
lethal
E138A
Engyodontium album
-
lethal, increased stability of the serine protease subtilisin
G293A
Engyodontium album
-
strong positive effect on activity
I132V
Engyodontium album
-
positive effect on activity
I310K
Engyodontium album
-
no effect on activity, increased stability of the serine protease subtilisin
K208H
Engyodontium album
-
positive effect on activity
K332R
Engyodontium album
-
positive effect on activity
L180I
Engyodontium album
-
positive effect on activity
L299C
Engyodontium album
-
lethal, increased stability of the serine protease subtilisin
M145F
Engyodontium album
-
no effect on activity, increased stability of the serine protease subtilisin
N95C
Engyodontium album
-
lethal, increased stability of the serine protease subtilisin
P265S
Engyodontium album
-
no effect on activity, increased stability of the serine protease subtilisin
P355S
Engyodontium album
-
no effect on activity, increased stability of the serine protease subtilisin
P97S
Engyodontium album
-
lethal, increased stability of the serine protease subtilisin
R237N
Engyodontium album
-
no effect on activity
S107D
Engyodontium album
-
no effect on activity
S123A
Engyodontium album
-
positive effect on activity
S273T
Engyodontium album
-
positive effect on activity
S337N
Engyodontium album
-
positive effect on activity
V167I
Engyodontium album
-
no effect on activity
V267I
Engyodontium album
-
positive effect on activity
Y151A
Engyodontium album
-
strong positive effect on activity
Y194S
Engyodontium album
-
no effect on activity, random mutation obtained during synthesis of wild-type proteinase K
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
biotechnology
degradation
-
use of enzyme to degrade poly(L-lactide) film. Adsorption of enzyme to film is irreversible, enzyme moves on the surface of substrate to hydrolyze the film around it
diagnostics
Engyodontium album
-
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)
medicine
molecular biology
Engyodontium album
-
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
pharmacology
Engyodontium album
-
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
synthesis
Engyodontium album
-
chemoenzymatic synthesis of oligo(L-phenylalanine) by the enzyme as a green and clean chemical reaction compared to organic synthesis