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Information on EC 3.4.21.103 - physarolisin and Organism(s) Physarum polycephalum and UniProt Accession Q8MZS4

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.103 physarolisin
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This record set is specific for:
Physarum polycephalum
UNIPROT: Q8MZS4 not found.
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Word Map
The taxonomic range for the selected organisms is: Physarum polycephalum
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Milk clotting activity. Preferential cleavage of Gly8-/-Ser in B chain of insulin most rapidly, followed by Leu11!Val, Cys(SO3H)19-/-Gly and Phe24-/-Phe. No action on Ac-Phe-Tyr(I)2.
Synonyms
physarolisin, physarolisin i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physarolisin I
-
formerly called physaropepsin
physarolysin II
-
-
Physarum aspartic proteinase
-
-
-
-
proteinase, Dictyostelium discoideum aspartic
-
-
-
-
proteinase, Dictyostelium discoideum aspartic, E
-
-
-
-
proteinase, Physarum flavicomum aspartic
-
-
-
-
proteinase, Physarum polycephalum acid
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
94949-28-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
?
insulin B chain + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitrophenyl)Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitrophenyl)Arg-Leu
show the reaction diagram
-
-
-
?
Glucagon + H2O
?
show the reaction diagram
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
show the reaction diagram
-
-
-
-
?
KPIEFF(NO2)RL + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
show the reaction diagram
-
-
-
?
oxidized insulin B + H2O
?
show the reaction diagram
-
-
-
?
oxidized insulin B chain + H2O
?
show the reaction diagram
-
the major cleavage sites are Gly8-Ser9, Leu11-Val12, Cys19-Gly20, Gly20-Glu21, and Phe24-Phe25
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
show the reaction diagram
-
major cleavage sites: Gly8-Ser9 (most susceptible), Leu11-Val12, Cysteic acid19-Gly20 and Phe24-Phe25
-
-
?
Substance P + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DAN
in the presence of cupric ions
Diazoacetyl-D,L-norleucine methyl ester
-
in presence of Cu2+
Diazoacetyl-DL-norleucine methyl ester
diisopropyl fluorophosphate
-
23% inhibition by 0.5 mM, 76% inhibition by 10 mM
pepstatin
-
not
PMSF
-
10 mM, 21% inhibition
tosyl-L-Leu-chloromethylketone
-
10 mM, 18% inhibition
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2
-
hydrolysis of oxidized insulin B chain
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.3 - 3
-
pH 1.3: about 25% of activity maximum, pH 3.0: about 35% of activity maximum
3.7 - 5.3
-
pH 3.7: about 40% of maximal actuvity, pH 5.3: about 35% of maximal activity, hydrolysis of oxidized insulin B chain
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 30
-
3°C: about 50% of maximal activity, 30°C: about 60% of maximal activity, hydrolysis of oxidized insulin B chain
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PHYSA_PHYPO
575
0
62709
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23000
1 * 31000 + 1 * 23000, SDS-PAGE, gel filtration
31000
1 * 31000 + 1 * 23000, SDS-PAGE, gel filtration
23000
31000
68000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
1 * 31000 + 1 * 23000, SDS-PAGE, gel filtration
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 6
-
-
647477
8
-
37°C, 15 min, 30% loss of activity
647477
9
-
37°C, 15 min, 45% loss of activity
647477
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18
-
pH 4.2, t1/2: 5 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the active enzyme is markedly unstable due to rapid autolysis, t1/2: 5 min at 18°C, pH 4.2
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Murakami-Murofushi, K.; Takahashi, T.; Minowa, Y.; Lino, S.; Takeuchi, T.; Kitagaki-Ogawa, H.; Murofushi, H.; Takahshi, K.
Purification and characterization of a novel intracellular acid proteinase from the plasmodia of a true slime mold, Physarum polycephalum
J. Biol. Chem.
32
19898-19903
1990
Physarum polycephalum
-
Manually annotated by BRENDA team
Murakami-Murofushi, K.; Takahashi, T.; Murofushi, H.; Takahashi, K.
A novel intracellular acid proteinase from the plasmodia of a true slime mold, Physarum polycephalum
Adv. Exp. Med. Biol.
362
565-568
1995
Physarum polycephalum
Manually annotated by BRENDA team
Nishii, W.; Ueki, T.; Miyashita, R.; Kojima, M.; Kim, Y.T.; Sasaki, N.; Murakami-Murofushi, K.; Takahashi, K.
Structural and enzymatic characterization of physarolisin (formerly physaropepsin) proves that it is a unique serine-carboxyl proteinase
Biochem. Biophys. Res. Commun.
301
1023-1029
2003
Physarum polycephalum
Manually annotated by BRENDA team
Nishii, W.; Kuriyama, H.; Takahashi, K.
The Physarum polycephalum php gene encodes a unique cold-adapted serine-carboxyl peptidase, physarolisin II
FEBS Lett.
546
340-344
2003
Physarum polycephalum
Manually annotated by BRENDA team
Murakami-Murofushi, K.; Nishii, W.; Takahashi, K.
Physarolisin
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
2
1891-1893
2004
Physarum polycephalum (Q8MZS4)
-
Manually annotated by BRENDA team
Nishii, W.; Kubota, K.; Takahashi, K.
The P1 and P1 residue specificities of physarolisin I, a serine-carboxyl peptidase from the true slime mold Physarum polycephalum
Biosci. Biotechnol. Biochem.
73
1168-1171
2009
Physarum polycephalum
Manually annotated by BRENDA team