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Information on EC 3.4.24.39 - deuterolysin and Organism(s) Aspergillus oryzae and UniProt Accession P46076

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.39 deuterolysin
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This record set is specific for:
Aspergillus oryzae
UNIPROT: P46076 not found.
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The taxonomic range for the selected organisms is: Aspergillus oryzae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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Preferential cleavage of bonds with hydrophobic residues in P1'; also Asn3-/-Gln and Gly8-/-Ser bonds in insulin B chain
Synonyms
asap1, deuterolysin, acid metalloproteinase, aspzincin, mep2-like, neutral proteinase ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid metalloproteinase
-
-
-
-
aspzincin
-
-
Deuterolysin
-
-
-
-
Microbial neutral proteinase II
-
-
-
-
Neutral proteinase II
NPII
-
-
-
-
Penicillium roqueforti metalloproteinase
-
-
-
-
Penicillium roqueforti protease II
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-
-
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Proteinase, Penicillium roqueforti metallo-
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
247028-11-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-casein + H2O
?
show the reaction diagram
degradation with low specific activity
-
-
?
beta-lactoglobulin + H2O
?
show the reaction diagram
degradation with low specific activity
-
-
?
Boc-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
degradation with low specific activity
-
-
?
casein + H2O
?
show the reaction diagram
degradation with low specific activity
-
-
?
clupeine + H2O
?
show the reaction diagram
degradation with high specific activity
-
-
?
Fibrin + H2O
?
show the reaction diagram
degradation with low specific activity
-
-
?
Glt-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
degradation with low specific activity
-
-
?
histone + H2O
?
show the reaction diagram
degradation with high specific activity
-
-
?
ovalbumin + H2O
?
show the reaction diagram
degradation with low specific activity
-
-
?
salmine + H2O
?
show the reaction diagram
degradation with high specific activity
-
-
?
Suc-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
degradation with low specific activity
-
-
?
alpha-casein + H2O
?
show the reaction diagram
degradation with low specific activity
-
-
?
benzyloxycarbonyl-Val-Lys-Met-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
second-best substrate
-
-
?
beta-lactoglobulin + H2O
?
show the reaction diagram
degradation with low specific activity
-
-
?
Boc-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
most favorable substrate
-
-
?
Boc-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
calf thymus histone 4 + H2O
?
show the reaction diagram
-
-
-
?
carboxybenzyl-Gly-Phe amide + H2O
carboxybenzyl-Gly + Phe amide
show the reaction diagram
-
-
-
?
casein + H2O
?
show the reaction diagram
degradation with low specific activity
-
-
?
casein + H2O
hydrolyzed casein
show the reaction diagram
-
-
-
-
?
clupeine + H2O
?
show the reaction diagram
degradation with high specific activity
-
-
?
Elastin + H2O
?
show the reaction diagram
-
-
-
?
Fibrin + H2O
?
show the reaction diagram
degradation with low specific activity
-
-
?
Glt-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
histone + H2O
?
show the reaction diagram
degradation with high specific activity
-
-
?
N-butoxycarbonyl-arginyl-valyl-arginyl-arginyl-4-methylcoumarin-7-amide + H2O
?
show the reaction diagram
-
-
-
?
N-butoxycarbonyl-Leu-Arg-Arg-4-methylcoumarin-7-amide + H2O
?
show the reaction diagram
-
-
-
?
N-butoxycarbonyl-Leu-Lys-Arg-4-methylcoumarin-7-amide + H2O
?
show the reaction diagram
-
-
-
?
ovalbumin + H2O
?
show the reaction diagram
degradation with low specific activity
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin-7-amide + H2O
?
show the reaction diagram
-
-
-
?
salmine + H2O
?
show the reaction diagram
degradation with high specific activity
-
-
?
salmon protamine sulfate + H2O
?
show the reaction diagram
-
-
-
?
Suc-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
Z-Arg-Arg-4-methylcoumarin-7-amide + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0264 - 0.0275
N-butoxycarbonyl-arginyl-valyl-arginyl-arginyl-4-methylcoumarin-7-amide
0.0638 - 0.07
N-butoxycarbonyl-Leu-Arg-Arg-4-methylcoumarin-7-amide
0.146 - 0.1573
N-butoxycarbonyl-Leu-Lys-Arg-4-methylcoumarin-7-amide
0.0119 - 0.0237
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin-7-amide
0.0473 - 0.0522
Z-Arg-Arg-4-methylcoumarin-7-amide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017 - 0.022
N-butoxycarbonyl-arginyl-valyl-arginyl-arginyl-4-methylcoumarin-7-amide
0.0017 - 0.0045
N-butoxycarbonyl-Leu-Arg-Arg-4-methylcoumarin-7-amide
0.0035 - 0.009
N-butoxycarbonyl-Leu-Lys-Arg-4-methylcoumarin-7-amide
0.00082 - 0.0022
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin-7-amide
0.00065 - 0.0009
Z-Arg-Arg-4-methylcoumarin-7-amide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6
-
casein
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19020
-
amino acid sequence
19300
-
Aspergillus oryzae, gel filtration
19800
-
recombinant enzyme, gel filtration
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D104N
-
site-directed mutagenesis
D121N
-
site-directed mutagenesis
D143E
-
site-directed mutagenesis
D143N
-
site-directed mutagenesis
D164N
-
site-directed mutagenesis
D80N
-
site-directed mutagenesis
E129D
-
site-directed mutagenesis
E129Q
-
site-directed mutagenesis
E142Q
-
site-directed mutagenesis
E42Q
-
site-directed mutagenesis
E65Q
-
site-directed mutagenesis
E86Q
-
site-directed mutagenesis
H118A
-
site-directed mutagenesis
H128R
-
site-directed mutagenesis
H132R
-
site-directed mutagenesis
R58Q
-
site-directed mutagenesis
Y106F
-
site-directed mutagenesis
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 11
stable
753029
3 - 11
stable
753029
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
pH 7.0, 10 min, 15% loss of activity
30
pH 7.0, 10 min, no loss of activity
40
pH 7.0, 10 min, 10% loss of activity
50
pH 7.0, 10 min, 5% loss of activity
60
pH 7.0, 10 min, 10% loss of activity
70
pH 7.0, 10 min, 30% loss of activity
80
pH 7.0, 10 min, 35% loss of activity
90
pH 7.0, 10 min, 30% loss of activity
30
pH 7.0, 10 min, 15% loss of activity
30 - 100
-
extremely stable at 100°C, but unstable near 75°C because of self-digestion
40
pH 7.0, 10 min, no loss of activity
50
pH 7.0, 10 min, 50% loss of activity
60
pH 7.0, 10 min, 50% loss of activity
70
pH 7.0, 10 min, 85% loss of activity
80
pH 7.0, 10 min, DeuB completely loses its activity
90
-
10 min, less than 30% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant prodeuterolysin
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressing in Aspergillus oryzae niaD300
overexpressing in Aspergillus oryzae niaD300
recombinant enzyme expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
proteinous nitrogen sources such as skimmed milk and gelatin instead of NaNO3 upregulate the transcription level of deuB. Addition of NaNO3 inhibits the upregulation of deuB transcription
transcription of deuB is observed at an early stage of CDN liquid culture (24 h) and the prolonged cultivation reduces the transcription of deuB. Addition of NaNO3 inhibits the upregulation of deuB transcription
proteinous nitrogen sources such as skimmed milk and gelatin instead of NaNO3 upregulate the transcription level of deuB. Addition of NaNO3 inhibits the upregulation of deuB transcription
transcription of deuB is observed at an early stage of CDN liquid culture (24 h) and the prolonged cultivation reduces the transcription of deuB. Addition of NaNO3 inhibits the upregulation of deuB transcription
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakadai, T.; Nasuno, S.; Iguchi, N.
Purification and properties of neutral proteinase II from Aspergillus oryzae
Agric. Biol. Chem.
37
2703-2708
1973
Aspergillus oryzae
-
Manually annotated by BRENDA team
Doi, Y.; Lee, B.R.; Ikeguchi, M.; Ohoba, Y.; Ikoma, T.; Tero-Kubota, S.; Yamauchi, S.; Takahashi, K.; Ichishima, E.
Substrate specificities of deuterolysin from Aspergillus oryzae and electron paramagnetic resonance measurement of cobalt-substituted deuterolysin
Biosci. Biotechnol. Biochem.
67
264-270
2003
Aspergillus oryzae
Manually annotated by BRENDA team
Fushimi, N.; Ee, C.E.; Nakajima, T.; Ichishima, E.
Aspzincin, a family of metalloendopeptidases with a new zinc-binding motif. Identification of new zinc-binding sites (His(128), His(132), and Asp(164)) and three catalytically crucial residues (Glu(129), Asp(143), and Tyr(106)) of deuterolysin from Aspergillus oryzae by site-directed mutagenesis
J. Biol. Chem.
274
24195-24201
1999
Aspergillus oryzae
Manually annotated by BRENDA team
Maeda, H.; Katase, T.; Sakai, D.; Takeuchi, M.; Kusumoto, K.; Amano, H.; Ishida, H.; Abe, K.; Yamagata, Y.
A novel non-thermostable deuterolysin from Aspergillus oryzae
Biosci. Biotechnol. Biochem.
80
1813-1819
2016
Aspergillus oryzae (P46076), Aspergillus oryzae (Q2UP30), Aspergillus oryzae, Aspergillus oryzae ATCC 42149 (P46076), Aspergillus oryzae ATCC 42149 (Q2UP30)
Manually annotated by BRENDA team