Information on EC 3.4.21.48 - cerevisin

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.48
-
RECOMMENDED NAME
GeneOntology No.
cerevisin
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt Ac-Tyr-OEt. Does not hydrolyse peptide amides
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37288-81-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Pbn1p, encoded by the PBN1 gene; BJ 5410
SwissProt
Manually annotated by BRENDA team
cerevisin precursor, vacuolar protease B, encoded by the PRB1 gene; strain MT8-1, after disruption of proteinase B termed MT8-1/delta-PrB
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
deletion of the rim101 gene involved in sporulation control results in upregulation of the PRB1 gene leading to higher levels of proteinase B activity. Increase in proteinase B activity results in severely compromised stability of some proteins such as Slt2p or Chs4p
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-Tyr ethyl ester + H2O
acetyl-Tyr + ethanol
show the reaction diagram
-
-
-
-
?
Acid-denatured hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
Azocoll + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Arg ethyl ester + H2O
benzoyl-Arg + ethanol
show the reaction diagram
-
-
-
-
?
benzoyl-Arg p-nitroanilide + H2O
benzoyl-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
benzoyl-Ile-Glu-Gly-Arg p-nitroanilide + H2O
benzoyl-Ile-Glu-Gly-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
benzoyl-Tyr p-nitroanilide + H2O
benzoyl-Tyr + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Ala-Phe-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Leu + H2O
?
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Gly-Phe-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Leu-Phe-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Leu-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
hide powder azure + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-Trp-Met-Arg-Phe-Ala + H2O
?
show the reaction diagram
-
preferential attack at Trp-Met
-
-
?
muscle sarcoplasmic protein + H2O
?
show the reaction diagram
-
-
-
-
?
N-succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
nitrated casein + H2O
?
show the reaction diagram
-
-
-
-
?
oxidized insulin B chain + H2O
?
show the reaction diagram
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initial rapid cleavage step at Leu15-Tyr16 and Phe24-Phe25, slower hydrolysis at Gln4-His5, Leu11-Val12, Tyr16-Leu17, Leu17-Val18 and Arg22-Gly23 and Phe25-Tyr26
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-
?
additional information
?
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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
?
-
-
the enzyme is able to maintain viability under starvation
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-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dichloroisocoumarin
-
-
antipain
Aprotinin
-
i.e. trasylol, weak
chymostatin
iodoacetamide
-
-
p-hydroxymercuribenzoate
-
-
proteinase B inhibitor
-
Trypsin inhibitor
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Urea
-
stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
Acetyl-Tyr ethyl ester
-
-
0.1
benzoyl-Tyr ethyl ester
-
-
1.79
N-succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.6
Acetyl-Tyr ethyl ester
Saccharomyces cerevisiae
-
-
2.1
benzoyl-Tyr ethyl ester
Saccharomyces cerevisiae
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.2
-
hydrolysis of benzyloxycarbonyl-Gly-Leu
6.5 - 7.5
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hydrolysis of nitrated casein, in presence of 4 M urea
6.5 - 9.8
-
hydrolysis of nitrated casein, in absence of urea
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
80% or more of the proteinase in the yeast cell is in the zymogen form and seems to be particle-bound
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
x * 30000, SDS-PAGE
30700
-
gel filtration
31000
-
equilibrium sedimentation
32000
-
1 * 32000, SDS-PAGE
33700
-
equilibroum sedimentation
34000
-
gel filtration
69619
-
x * 69619, calculation from nucleotide sequence
73000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
the proteinase B precursor is glycosylated and proteolytically processed at least three times before mature enzyme is formed. The precursor is autocatalytically cleaved to yield the NH2 terminus and the COOH terminus of the mature enzyme. The pro region plays an essential role in the proteolytic processing of the enzyme
side-chain modification
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
30 min, no loss of activity
37
-
15 min, 50% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.5% gelatin stabilizes
-
freezing and thawing has no effect
-
freezing and thawing in absence of glycerol results in total loss of activity
-
HgCl2, 10 mM, stabilizes during purification
-
mature proteinase yscB is not stable in absence of proteinase yscA. The wild-type like conformation of proteolytically inactive mutant proteinase yscA proteins stabilizes mature proteinase yscB and thus enables continuous maturation of pro-proteinase yscB by active proteinase yscB
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without glycerol, rapid loss of activity due to autolysis
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20% glycerol, 0.1 mM HgCl2, stable for 2 months
-
-20°C, stable for several months
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli DH5-alpha, generation and transformation of protease B-knockout strain of Saccaromyces termed MT8-1/delta-PrB described
generation of a yeast strain with PBN1 under control of the GAL promoter and of strains depleted of Pbn1p, transformation of Saccaromyces BJ 5410 with the PBN1 gene to generate the pGAL-HA-PBN1 strain BJ 10242, properties of strain BJ 10242 by processing activities of transient proteins of the endoplasmic reticulum indicated
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
mutation in the active site of the vacuolar serine proteinase yscB abolishes proteolytic maturation of its 73000 Da precursor to the 41500 Da pro-enzyme and a newly detected 41000 Da peptide
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis