Information on EC 3.4.21.50 - lysyl endopeptidase

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

EC NUMBER
COMMENTARY hide
3.4.21.50
-
RECOMMENDED NAME
GeneOntology No.
lysyl endopeptidase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage: Lys-/-, including -Lys-/-Pro-
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
78642-25-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
gene kgp
-
-
Manually annotated by BRENDA team
strain PA103
-
-
Manually annotated by BRENDA team
strain PA103-29
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
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
50S ribosomal protein L7/L12 + H2O
?
show the reaction diagram
6-phosphogluconate dehydrogenase + H2O
?
show the reaction diagram
acetyl-Lys-p-nitroaniline + H2O
acetyl-Lys + p-nitroanilide
show the reaction diagram
-
-
?
acid soluble collagen + H2O
?
show the reaction diagram
-
from the cartilages of brownbanded bamboo shark Chiloscyllium punctatum and blacktip shark Carcharhinus limbatus
-
-
?
ACTH + H2O
?
show the reaction diagram
-
hydrolysis of the bonds: Lys11-Pro12, Lys16-Lys16, Lys16-Arg17, Lys21-Val22
-
-
?
acyl carrier protein + H2O
?
show the reaction diagram
albacore tuna pepsin-solubilised collagen + H2O
?
show the reaction diagram
-
-
-
-
?
amyloid beta-protein + H2O
?
show the reaction diagram
B-chain of insulin + H2O
?
show the reaction diagram
benzoyl-Arg ethyl ester + H2O
benzoyl-Arg + ethanol
show the reaction diagram
-
-
-
-
?
benzoyl-L-Lys-4-nitroanilide + H2O
benzoyl-L-Lys + 4-nitroaniline
show the reaction diagram
benzoyl-Lys methyl ester + H2O
benzoyl-Lys + methanol
show the reaction diagram
benzoyl-Lys-NH2 + H2O
benzoyl-Lys + NH3
show the reaction diagram
benzoyl-Lys-p-nitroanilide + H2O
benzoyl-Lys + p-nitroaniline
show the reaction diagram
benzoyl-Lys-p-nitroaniline + H2O
benzoyl-Lys + p-nitroanilide
show the reaction diagram
-
-
?
benzoyl-Orn methyl ester + H2O
benzoyl-Orn + methanol
show the reaction diagram
-
-
?
Boc-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
Boc-Val-Leu-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
bovine trypsinogen + H2O
trypsin + ?
show the reaction diagram
-
the enzyme activates the zymogens
-
-
?
casein + H2O
?
show the reaction diagram
chaperone protein DNA kinase + H2O
?
show the reaction diagram
chymotrypsinogen + H2O
chymotrypsin + ?
show the reaction diagram
-
-
-
-
?
Denatured hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
elongation factor G + H2O
?
show the reaction diagram
elongation factor Tu + H2O
?
show the reaction diagram
enolase + H2O
?
show the reaction diagram
fibrinogen + H2O
fibrin + ?
show the reaction diagram
-
-
-
-
?
fructose-bisphosphate aldolase class 2 + H2O
?
show the reaction diagram
Glucagon + H2O
?
show the reaction diagram
glyceraldehyde-3-phosphate dehydrogenase A + H2O
?
show the reaction diagram
Ile-Asn-Leu-Lys-Ala-leu-Ala-Ala-Leu-Ala-Lys-Lys-Ile-Leu-NH2
?
show the reaction diagram
-
i.e. mastoparan. Cleavage sites: Ile-Asn-Leu-Lys-/-Ala-Leu-Ala-Ala-Leu-Ala-Lys-/-Lys-/-Ile-Leu-NH2
-
-
?
Ile-Asn-Leu-Lys-Ala-Leu-Ala-Ala-Leu-Ala-Lys-Lys-Ile-Leu-NH2 + H2O
?
show the reaction diagram
-
i.e. mastoparan, cleavage sites: Lys4-Ala5, Lys11-Lys12, Lys12-Ile13
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
show the reaction diagram
Lys-p-nitroanilide + H2O
Lys + p-nitroaniline
show the reaction diagram
lysine vasopressin + H2O
?
show the reaction diagram
N-acetyl-L-lysine + H2O
N-acetyl-L-lysine + H2O
show the reaction diagram
-
-
incorporation of O18 atom into the carboxyl group
-
?
N-benzoyl-L-Lys-p-nitroanilide + H2O
N-benzoyl-L-Lys + p-nitroaniline
show the reaction diagram
N-benzoyl-L-Orn methyl ester + H2O
N-benzoyl-L-Orn + methanol
show the reaction diagram
N-tert-butyloxycarbonyl-Ala-Ala-Lys-4-methylcoumarin 7-amide + H2O
N-tert-butyloxycarbonyl-Ala-Ala-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-tert-butyloxycarbonyl-Ala-Lys-4-methylcoumarin 7-amide + H2O
N-tert-butyloxycarbonyl-Ala-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-tert-butyloxycarbonyl-Lys-4-methylcoumarin 7-amide + H2O
N-tert-butyloxycarbonyl-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-tosyl-Gly-Pro-Lys + p-nitroaniline
show the reaction diagram
N-tosyl-L-Arg methyl ester + H2O
N-tosyl-L-Arg + methanol
show the reaction diagram
N-tosyl-L-Lys methyl ester + H2O
N-tosyl-L-Lys + methanol
show the reaction diagram
native hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
oxidized insulin B chain + H2O
?
show the reaction diagram
pepsin soluble collagen + H2O
?
show the reaction diagram
-
from the cartilages of brownbanded bamboo shark Chiloscyllium punctatum and blacktip shark Carcharhinus limbatus
-
-
?
phosphoglycerate kinase + H2O
?
show the reaction diagram
plasminogen + H2O
plasmin + ?
show the reaction diagram
-
-
-
-
?
porcine pepsin-solubilised collagen + H2O
?
show the reaction diagram
-
is more resistant to hydrolysis compared with albacore tuna pepsin-solubilised collagen
-
-
?
pyroglutamyl-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn + H2O
pyroglutamyl-Ala-Lys + Ser-Gln-Gly-Gly-Ser-Asn
show the reaction diagram
-
i.e. serum thymic factor
-
-
?
serum thymic factor + H2O
?
show the reaction diagram
-
cleavage of the Lys-Ser bond
-
-
?
single-chain human insulin-like peptide 5 precursor + H2O
two-chain human insulin-like peptide 5
show the reaction diagram
-
endoproteinase Lys-C can cleave the peptide bond at the C-terminal side of lysine residues
-
-
?
somatropin + H2O
?
show the reaction diagram
-
protein digested with either trypsin or endoproteinase Lys-C prior to MALDI-MS analysis as a rapid method based on MALDI-TOF-MS peptide mass finger printing for identification of somatropin: sequence coverage obtained from individual trypsin and Lys-C is 79% and 60%, respectively, sequence coverage of both maps together is 98%
-
-
?
Substance P + H2O
?
show the reaction diagram
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Ala-Ala-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Ala-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
tosyl-Gly-Pro-Lys + 4-nitroaniline
show the reaction diagram
tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
tosyl-Gly-Pro-Lys + p-nitroaniline
show the reaction diagram
tosyl-Lys methyl ester + H2O
tosyl-Lys + methanol
show the reaction diagram
Type I collagen + H2O
?
show the reaction diagram
-
from calf skin
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Gln-Phe-Lys-Val-Val-Thr + H2O
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Gln-Phe-Lys + Val-Val-Thr
show the reaction diagram
-
i.e. dynorphin B
-
?
Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr + H2O
Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys + Ser-Gln-Thr-Pro-Leu-Val-Thr
show the reaction diagram
-
i.e. alpha-endorphin
-
?
Val-Leu-Lys-p-nitroanilide + H2O
Val-Leu-Lys + p-nitroaniline
show the reaction diagram
-
-
-
-
?
yellowfin tuna pepsin-solubilised collagen + H2O
?
show the reaction diagram
-
undergoes hydrolysis to the highest extent
-
-
?
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
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
enhances the enzyme production in strain PA103
additional information
-
no effects by Cl-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-amino-1-hexanoic acid
-
-
acetonitrile
-
-
antipain
benzamidine
-
; 0.1 mM, 21% inhibition
benzoyl-DL-lysinal
-
-
Benzoyl-Lys
-
-
benzyloxycarbonyl-Leu-Leu-lysinal
benzyloxycarbonyl-Leu-Pro-lysinal
-
-
benzyloxycarbonyl-Pro-lysinal
-
-
benzyloxycarbonyl-Val-lysinal
-
benzyloxycarbonyl-Val-lysinol
-
poor competitive inhibitor
-
Cyclohexylamine
-
-
diisopropyl fluorophosphate
diisopropylfluorophosphate
ethylamine
-
-
Guanidine-HCl
0.1 M, 20 min, 72% loss of activity
Isobutylamine
-
-
methylamine
-
-
n-alkylamine
-
-
n-amylamine
-
-
n-butylamine
-
-
n-Hexylamine
-
-
n-Propylamine
-
-
N-tosyl-L-Lys chloromethyl ketone
N-tosyl-L-Lys chloromethylketone
-
Nalpha-p-tosyl-L-Lys-chloromethylketone
Nalpha-p-tosyl-L-lysine chloromethyl ketone
-
1 mM, complete inhibition
phenylmethanesulfonyl fluoride
sodium dodecylsulfate
0.1%, 20 min, 70% loss of activity
tosyl-L-lysine chloromethylketone
-
i.e. TLCK
Urea
4 M, 20 min, 80% loss of activity
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EGTA
-
activates
Pepstatin
slight activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
benzoyl-Arg ethyl ester
-
-
0.091
benzoyl-Lys methyl ester
-
-
0.32
benzoyl-Lys-NH2
-
-
0.08 - 0.11
Lys-p-nitroanilide
1.59
N-acetyl-L-lysine
-
pH 9, rate of carboxyl oxygen exchange reaction by Lys-C is accelerated at acidic pH conditions.
0.07 - 0.09
N-benzoyl-L-Lys p-nitroanilide
0.63 - 1
N-benzoyl-L-Orn methyl ester
3.09
N-tert-butyloxycarbonyl-Ala-Ala-Lys-4-methylcoumarin 7-amide
-
-
3.11
N-tert-butyloxycarbonyl-Ala-Lys-4-methylcoumarin 7-amide
-
-
41
N-tert-butyloxycarbonyl-Lys-4-methylcoumarin 7-amide
-
-
0.034
N-tosyl-Gly-Pro-Lys-p-nitroanilide
-
-
2.5 - 35.7
N-tosyl-L-Arg methyl ester
0.053 - 0.1
N-tosyl-L-Lys methyl ester
0.0028 - 0.024
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
0.0037 - 0.042
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
0.029 - 0.081
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
0.0007 - 0.032
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
0.034 - 0.25
tosyl-Gly-Pro-Lys-p-nitroanilide
0.053
Tosyl-Lys methyl ester
-
pH 8.0
0.0019
Trypsinogen
-
-
0.33
Val-Leu-Lys-p-nitroanilide
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.41
benzoyl-Arg ethyl ester
Achromobacter lyticus
-
-
225
benzoyl-Lys methyl ester
Achromobacter lyticus
-
-
1.54
benzoyl-Lys-NH2
Achromobacter lyticus
-
-
0.86
benzoyl-Lys-p-nitroanilide
Achromobacter lyticus
-
-
0.14
Lys-p-nitroanilide
Achromobacter lyticus
-
-
10.4
N-benzoyl-L-Orn methyl ester
Achromobacter lyticus
-
-
49
N-tert-butyloxycarbonyl-Ala-Ala-Lys-4-methylcoumarin 7-amide
Achromobacter lyticus
-
-
32.9
N-tert-butyloxycarbonyl-Ala-Lys-4-methylcoumarin 7-amide
Achromobacter lyticus
-
-
3.02
N-tert-butyloxycarbonyl-Lys-4-methylcoumarin 7-amide
Achromobacter lyticus
-
-
59
N-tosyl-Gly-Pro-Lys-p-nitroanilide
Pseudomonas aeruginosa
-
-
5.04
N-tosyl-L-Arg methyl ester
Achromobacter lyticus
-
-
282 - 570
N-tosyl-L-Lys methyl ester
2.6 - 98
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
1.1 - 46
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
0.4 - 8.4
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
0.8 - 96
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
59
tosyl-Gly-Pro-Lys-p-nitroanilide
Pseudomonas aeruginosa
-
pH 9.0
282
Tosyl-Lys methyl ester
Pseudomonas aeruginosa
-
pH 8.0
0.103
Trypsinogen
Achromobacter lyticus
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3
pH 9.2, 30C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
for carboxyl oxygen exchange activity
7.5 - 8.2
-
esterolytic activity
7.8 - 8.2
8 - 9
-
mutant enzyme H210S, hydrolysis of tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
8 - 8.5
esterolytic activity
8
-
activity with tosyl-Lys methyl ester; tosyl-Lys-methyl ester
8.5 - 10.7
8.5 - 10.5
caseinolytic activity
8.8
-
amidolytic activity
9 - 10
-
mutant enzyme W169V, hydrolysis of tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
9 - 9.5
9 - 9.6
amidolytic activity
9
-
activity with tosyl-Gly-Pro-p-nitroanilide
9.5
-
wild-type enzyme, hydrolysis of tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
more than 50% of maximum activty in this range
7 - 8.5
-
pH 7.0: about 50% of maximal activity, pH 8.5. about 70% of maximal activity, activity with tosyl-Lys methyl ester; pH 7.0: about 50% of maximal activity, pH: 8.5: about 70% of maximal activity, tosyl-Lys-methyl ester
8 - 10
-
pH 8.0: about 40% of maximal activity, pH 10.0: about 95% of maximal activity, wild-type enzyme, hydrolysis of tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
-
pH 6: about 50% of maximal activity, pH 10: about 55% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
blockage of the type IX secretion system, T9SS, leads to localization of the enzyme in the outer membrane, subcellular localization study overview
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27850
ion-spray mass spectrometry
31000
1 * 31000, SDS-PAGE
32000
x * 32000, SDS-PAGE
48000
-
x * 48000, SDS-PAGE
additional information
-
primary structure
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutants H210S and W169F, to 2.0 and 2.3 A resolution, respectively
neutron structure analysis of catalytic triad with Trp169 and His210. His57 is double protonated and forms hydrogen bonds to Ser194Ogamma and Asp113Odelta1, Odelta2. Resolution of data 2.0 A
-
purified recombinant enzyme, sitting drop vapor diffusion method, mixing of equal volumes of 0.001 ml of protein with reservoir solution containing 27% PEG 4000, 100 mM sodium acetate, pH 5.0, and 0.2 M ammonium sulfate, equilibration over 0.5 ml of reservoir solution, one week, X-ray diffraction structure determination and analysis at 1.6 A resolution, molecular replacement/heavy atom derivatization
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
stable
36618
4 - 11
5 - 11
-
4C, 24 h, stable
36604
5
-
pH 7.5, 20 min, about 60% loss of activity
36614
6.5 - 8.5
-
pH 7.5, 20 min, stable
36614
10
-
40% loss of activity
36614
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
moderately stable up to
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
7 M urea, pH 8.0, 30C, 20 min, 30% loss of activity
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-propanol
-
20%, 37C, enzyme retains most of its activity
Ethanol
-
20%, 37C, enzyme retains most of its activity
Methanol
-
20%, 37C, enzyme retains most of its activity
SDS
-
0.1% w/v, in 40 mM Tris-HCl, pH 8, 20 min, 30C, stable
urea
-
4 M, stable
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 0.001-0.1 M Tris-HCl buffer, pH 6.0-10.9, at enzyme concentration higher than 0.1 mg/ml
-
4C, pH 5.0-11.0, 24 h, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from strain PA103-29 by ion exchange chromatography and gel filtration, or from strain PAO1-B1 supernatants by ultrafiltration, anion exchange and hydrophobic interaction chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene PGN_1416, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression in Escherichia coli strain BL21(DE3)
overproduction and secretion into the periplasm of Escherichia coli
-
recombinant expression of Gly681-Ala710 deletion mutant in Porphyromonas gingivalis strain ECR368, release of enzyme Kgp catalytic domain in soluble form into the culture supernatant
-
the cloned gene of prepro-API is expressed in Escherichia coli, pro-API is secreted into the periplasm and activated autocatalytically
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H210/W169F
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 8.6% of the wild-type ratio
H210A/W169A
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 0.25% of the wild-type ratio
H210F
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin is 14% of the wild-type value, the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin is 29.5% of the wild-type value
H210K
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 0.02% of the wild-type ratio
W169G
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin is 0.06% of the wild-type value
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
biotechnology
medicine
synthesis
-
use of the immobilized enzyme in the enzyme-assisted semisynthesis of human insulin
Show AA Sequence (108 entries)
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