Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.4.21.50 - lysyl endopeptidase and Organism(s) Achromobacter lyticus and UniProt Accession P15636

for references in articles please use BRENDA:EC3.4.21.50
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.50 lysyl endopeptidase
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Achromobacter lyticus
UNIPROT: P15636 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Achromobacter lyticus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
Preferential cleavage: Lys-/-, including -Lys-/-Pro-
Synonyms
lep, endoproteinase, lys-c, endoproteinase lys-c, lysyl endopeptidase, caseinase, achromobacter protease i, achromopeptidase, lysine-specific protease, endopeptidase lys-c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Achromobacter lysyl endopeptidase
-
Achrombacter protease I
-
-
-
-
Achromobacter protease I
-
-
Achromobacter proteinase I
-
-
-
-
achromopeptidase
-
-
-
-
endo-Lys-C protease
-
-
-
-
endopeptidase Lys-C
-
-
-
-
endoproteinase Lys-C
-
-
-
-
lysine specific proteinase
-
-
-
-
lysine-specific protease
-
-
-
-
lysyl bond specific proteinase
-
-
-
-
Lysyl endopeptidase
protease I
-
-
-
-
proteinase, Achromobacter lyticus alkaline I
-
-
-
-
proteinase, lysine specific
-
-
-
-
proteinase, Pseudomonas lyticus alkaline , I
-
-
-
-
Pseudomonas aeruginosa lysine -specific protease
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
78642-25-8
-
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
cleavage into 5 peptide fragments
-
-
?
6-phosphogluconate dehydrogenase + H2O
?
show the reaction diagram
cleavage into 7 peptide fragments
-
-
?
acyl carrier protein + H2O
?
show the reaction diagram
cleavage into 3 peptide fragments
-
-
?
chaperone protein DNA kinase + H2O
?
show the reaction diagram
cleavage into 10 peptide fragments
-
-
?
elongation factor G + H2O
?
show the reaction diagram
cleavage into 8 peptide fragments
-
-
?
elongation factor Tu + H2O
?
show the reaction diagram
cleavage into 7 peptide fragments
-
-
?
enolase + H2O
?
show the reaction diagram
cleavage into 4 peptide fragments
-
-
?
fructose-bisphosphate aldolase class 2 + H2O
?
show the reaction diagram
cleavage into 5 peptide fragments
-
-
?
glyceraldehyde-3-phosphate dehydrogenase A + H2O
?
show the reaction diagram
cleavage into 5 peptide fragments
-
-
?
phosphoglycerate kinase + H2O
?
show the reaction diagram
cleavage into 4 peptide fragments
-
-
?
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
-
-
?
albacore tuna pepsin-solubilised collagen + 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-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
-
-
-
-
?
bovine trypsinogen + H2O
trypsin + ?
show the reaction diagram
-
the enzyme activates the zymogens
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
chymotrypsinogen + H2O
chymotrypsin + ?
show the reaction diagram
-
-
-
-
?
Lys-p-nitroanilide + H2O
Lys + p-nitroaniline
show the reaction diagram
-
-
-
-
?
lysine vasopressin + H2O
?
show the reaction diagram
-
only the Lys8-Gly9 bond is hydrolyzed
-
-
?
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-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
-
-
-
-
?
pepsin soluble collagen + H2O
?
show the reaction diagram
-
from the cartilages of brownbanded bamboo shark Chiloscyllium punctatum and blacktip shark Carcharhinus limbatus
-
-
?
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
-
-
?
Substance P + H2O
?
show the reaction diagram
-
hydrolysis of the bond Lys3-Pro4
-
-
?
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
Trypsinogen + H2O
?
show the reaction diagram
-
-
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
from calf skin
-
-
?
yellowfin tuna pepsin-solubilised collagen + H2O
?
show the reaction diagram
-
undergoes hydrolysis to the highest extent
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-amino-1-hexanoic acid
-
-
acetonitrile
-
-
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
-
-
diisopropylfluorophosphate
-
-
ethylamine
-
-
Isobutylamine
-
-
methylamine
-
-
n-alkylamine
-
-
n-amylamine
-
-
n-butylamine
-
-
n-Hexylamine
-
-
n-Propylamine
-
-
Nalpha-p-tosyl-L-Lys-chloromethylketone
-
-
phenylmethanesulfonyl fluoride
-
-
additional information
-
acyllysinals, acylaminoacyllysinals and acylpeptidyllysinals function as a transition-state inhibitor
-
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
-
-
2.5 - 35.7
N-tosyl-L-Arg methyl ester
0.083 - 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
0.0019
Trypsinogen
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.41
benzoyl-Arg ethyl ester
-
-
225
benzoyl-Lys methyl ester
-
-
1.54
benzoyl-Lys-NH2
-
-
0.86
benzoyl-Lys-p-nitroanilide
-
-
0.14
Lys-p-nitroanilide
-
-
10.4
N-benzoyl-L-Orn methyl ester
-
-
49
N-tert-butyloxycarbonyl-Ala-Ala-Lys-4-methylcoumarin 7-amide
-
-
32.9
N-tert-butyloxycarbonyl-Ala-Lys-4-methylcoumarin 7-amide
-
-
3.02
N-tert-butyloxycarbonyl-Lys-4-methylcoumarin 7-amide
-
-
5.04
N-tosyl-L-Arg methyl ester
-
-
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
0.103
Trypsinogen
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
for amidase activity
8 - 9
-
mutant enzyme H210S, hydrolysis of tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
8.5 - 10.7
8.8
-
amidolytic activity
9 - 10
-
mutant enzyme W169V, hydrolysis of tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
9 - 9.5
9.5
-
wild-type enzyme, hydrolysis of tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
50
-
amidolytic activity, esterolytic activity and caseinolytic activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the family of serine proteases
physiological function
-
characterisation of pepsin-solubilised collagen from the skin of unicorn leatherjacket Aluterus monocerous by lysyl endopeptidase
additional information
the additional disulfide bond (Cys6-Cys216) in the structure of lysyl endopeptidases, compared to trypsin, is thought to be responsible for their optimum activity at basic pH-values, 8.5-10.7, and their high resistance to denaturants
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
API_ACHLY
653
0
68125
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
30000
additional information
-
primary structure
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 30000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
the cloned gene of prepro-API is expressed in E. coli, pro-API is secreted into the periplasm and activated autocatalytically
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H210S
crystallization data. Optimum pH value shifts from around pH 9 of wild-type to approximately pH 7, while retaining high activity
W169F
crystallization data. Optimum pH value shifts from around pH 9 of wild-type to approximately pH 7, while retaining high activity
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
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
H210S
W169A
W169F
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
W169H
W169L
W169V
W169Y
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
stable
36618
4 - 11
-
4°C, 24 h, stable
36608
5 - 11
-
4°C, 24 h, stable
36604
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
pH 9.0, 30 min, stable up to
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
7 M urea, pH 8.0, 30°C, 20 min, 30% loss of activity
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-propanol
-
20%, 37°C, enzyme retains most of its activity
Ethanol
-
20%, 37°C, enzyme retains most of its activity
Methanol
-
20%, 37°C, enzyme retains most of its activity
SDS
-
0.1% w/v, in 40 mM Tris-HCl, pH 8, 20 min, 30°C, stable
urea
-
4 M, stable
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.001-0.1 M Tris-HCl buffer, pH 6.0-10.9, at enzyme concentration higher than 0.1 mg/ml
-
4°C, pH 5.0-11.0, 24 h, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overproduction and secretion into the periplasm of Escherichia coli
-
the cloned gene of prepro-API is expressed in Escherichia coli, pro-API is secreted into the periplasm and activated autocatalytically
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
the enzyme is attractive for the proteolytic generation of peptides to be analyzed by mass spectrometry, usage in quantitative mass spectrometry, overview. It can be used in the presence of protein denaturants which allow better access to cleavage sites and hence better proteolysis. The enzyme has advantages over trypsin, namely, reduced missed cleavage (because KR and RK are cleaved specifically), tolerance to denaturants and requirement for only a single labelled amino acid in experiments using isotopic labelling
analysis
biotechnology
-
Lys C is used to incorporate two 18O atoms into the carboxyl termini of peptides for proteomics
synthesis
-
use of the immobilized enzyme in the enzyme-assisted semisynthesis of human insulin
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Masaki, T.; Suzuki, H.; Soejima, M.
Purification and some properties of Achromobacter protease Ia from Achromobacter lyticus M497-1
Agric. Biol. Chem.
50
3087-3091
1986
Achromobacter lyticus, Achromobacter lyticus M497-1
-
Manually annotated by BRENDA team
Morihara, K.; Muneyuki, R.; Oka, T.
Use of immobilized Achromobacter protease I for semisynthesis of human insulin
Methods Enzymol.
136
162-170
1987
Achromobacter lyticus
Manually annotated by BRENDA team
Masaki, T.; Soejima, M.
Actions of Achromobacter protease I on some zymogens and dimethylcasein
Agric. Biol. Chem.
49
1867-1868
1985
Achromobacter lyticus
-
Manually annotated by BRENDA team
Masaki, T.; Fujihashi, T.; Nakamura, K.; Soejima, M.
Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. II. specificity and inhibition studies of Achromobacter protease I
Biochim. Biophys. Acta
660
51-55
1981
Achromobacter lyticus, Achromobacter lyticus M497-1
Manually annotated by BRENDA team
Masaki, T.; Tanabe, M.; Nakamura, K.; Soejima, M.
Studies on a new proteolytic enzyme from A chromobacter lyticus M497-1. I. Purification and some enzymatic properties
Biochim. Biophys. Acta
660
44-50
1981
Achromobacter lyticus, Achromobacter lyticus M497-1
Manually annotated by BRENDA team
Masaki, T.; Nakamura, T.; Isono, M.; Soejima, M.
A new proteolytic enzyme from Achromobacter lyticus M497-1
Agric. Biol. Chem.
42
1443-1445
1978
Achromobacter lyticus, Achromobacter lyticus M497-1
-
Manually annotated by BRENDA team
Oda, Y.; Kitagawa, Y.; Yamaguchi, H.; Matsuura, Y.; Katsube, Y.; Masaki, T.; Tanaka, T.; Matsuura, S.; Norioka, S.
Crystallization and preliminary X-ray diffraction analysis of two lysinal derivatives of Achromobacter protease I
Acta Crystallogr. Sect. D
52
1027-1029
1996
Achromobacter lyticus, Achromobacter lyticus M497-1
Manually annotated by BRENDA team
Leonard, R.B.; Carroll, K.C.
Rapid lysis of gram-positive cocci for pulsed-field gel electrophoresis using achromopeptidase
Diagn. Mol. Pathol.
6
288-291
1997
Achromobacter lyticus
Manually annotated by BRENDA team
Masaki, T.; Tanaka, T.; Tsunasawa, S.; Sakiyama, F.; Soejima, S.
Inhibition of Achromobacter protease I by lysinal derivatives
Biosci. Biotechnol. Biochem.
56
1604-1607
1992
Achromobacter lyticus
Manually annotated by BRENDA team
Ohara, T.; Makino, K.; Shinagawa, H.; Nakata, A.; Norioka, S.; Sakiyama, F.
Cloning, nucleotide sequence, and expression of Achromobacter protease I gene
J. Biol. Chem.
264
20625-20631
1989
Achromobacter lyticus
Manually annotated by BRENDA team
Tsunasawa, S.; Masaki, T.; Hirose, M.; Soejima, M.; Sakiyama, F.
The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease
J. Biol. Chem.
264
3832-3839
1989
Achromobacter lyticus
Manually annotated by BRENDA team
Sakiyama, F.; Masaki, T.
Lysyl endopeptidase of Achromobacter lyticus
Methods Enzymol.
244
126-137
1994
Achromobacter lyticus
Manually annotated by BRENDA team
Shiraki, K.; Norioka, S.; Li, S.; Yokota, K.; Sakiyama, F.
Electrostatic role of aromatic ring stacking in the pH-sensitive modulation of a chymotrypsin-type serine protease,Achromobacter protease I
Eur. J. Biochem.
269
4152-4158
2002
Achromobacter lyticus
Manually annotated by BRENDA team
Shiraki, K.; Norioka, S.; Li, S.; Sakiyama, F.
Contribution of an imidazole-indole stack to high catalytic potency of a lysine-specific serine protease, Achromobacter protease I
J. Biochem.
131
213-218
2002
Achromobacter lyticus
Manually annotated by BRENDA team
Kozhukh, G.V.; Hagihara, Y.; Kawakami, T.; Hasegawa, K.; Naiki, H.; Goto, Y.
Investigation of a peptide responsible for amyloid fibril formation of beta2-microglobulin by Achromobacter protease I
J. Biol. Chem.
277
1310-1315
2002
Achromobacter lyticus
Manually annotated by BRENDA team
Hajkova, D.; Rao, K.C.; Miyagi, M.
pH dependency of the carboxyl oxygen exchange reaction catalyzed by lysyl endopeptidase and trypsin
J. Proteome Res.
5
1667-1673
2006
Achromobacter lyticus
Manually annotated by BRENDA team
Ahmad, M.; Benjakul, S.
Extraction and characterisation of pepsin-solubilised collagen from the skin of unicorn leatherjacket (Aluterus monocerous)
Food Chem.
120
817-824
2010
Achromobacter lyticus
Manually annotated by BRENDA team
Kittiphattanabawon, P.; Benjakul, S.; Visessanguan, W.; Shahidi, F.
Isolation and characterization of collagen from the cartilages of brownbanded bamboo shark (Chiloscyllium punctatum) and blacktip shark (Carcharhinus limbatus)
LWT-Food Sci. Technol.
43
792-800
2010
Achromobacter lyticus
Manually annotated by BRENDA team
Ito, L.; Shiraki, K.; Uchida, T.; Okumura, M.; Yamaguchi, H.
Crystallization and preliminary crystallographic analysis of Achromobacter protease I mutants
Acta Crystallogr. Sect. F
66
1531-1532
2010
Achromobacter lyticus (P15636)
Manually annotated by BRENDA team
Patel, P.A.; Ledeboer, N.A.; Ginocchio, C.C.; Condon, S.; Bouchard, S.; Qin, P.; Karchmer, T.; Peterson, L.R.
Performance of the BD GeneOhm MRSA achromopeptidase assay for real-time PCR detection of methicillin-resistant Staphylococcus aureus in nasal specimens
J. Clin. Microbiol.
49
2266-2268
2011
Achromobacter lyticus
Manually annotated by BRENDA team
Ohnishi, Y.; Masaki, T.; Yamada, T.; Kurihara, K.; Tanaka, I.; Niimura, N.
A preliminary neutron diffraction analysis of Achromobacter protease I
J. Phys. Conf. Ser.
251
012032
2010
Achromobacter lyticus, Achromobacter lyticus M497-1
-
Manually annotated by BRENDA team
Kishimoto, T.; Kondo, J.; Takai-Igarashi, T.; Tanaka, H.
Accurate mass comparison coupled with two endopeptidases enables identification of protein termini
Proteomics
11
485-489
2011
Achromobacter lyticus
Manually annotated by BRENDA team
Achour, B.; Barber, J.
The activities of Achromobacter lysyl endopeptidase and Lysobacter lysyl endoproteinase as digestive enzymes for quantitative proteomics
Rapid Commun. Mass Spectrom.
27
1669-1672
2013
Achromobacter lyticus (P15636), Lysobacter enzymogenes (Q7M135)
Manually annotated by BRENDA team