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Information on EC 3.4.21.48 - cerevisin and Organism(s) Saccharomyces cerevisiae and UniProt Accession P09232
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3.4.21.48 cerevisinSpecify your search results
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt Ac-Tyr-OEt. Does not hydrolyse peptide amides
Synonyms
proteinase yscb, yeast proteinase b, cerevisin, yeast proteinase yscb, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
baker's yeast proteinase
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baker's yeast proteinase B
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brewer's yeast proteinase
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Proteinase B
Proteinase YSCB
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proteinase, yeast B
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yeast proteinase B
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yeast proteinase yscB
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CAS REGISTRY NUMBER
COMMENTARY
37288-81-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzoyl-Arg p-nitroanilide + H2O
benzoyl-Arg + 4-nitroaniline
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-
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?
benzoyl-Ile-Glu-Gly-Arg p-nitroanilide + H2O
benzoyl-Ile-Glu-Gly-Arg + p-nitroaniline
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-
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?
benzoyl-Tyr p-nitroanilide + H2O
benzoyl-Tyr + 4-nitroaniline
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?
Leu-Trp-Met-Arg-Phe-Ala + H2O
?
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preferential attack at Trp-Met
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?
oxidized insulin B chain + H2O
?
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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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the enzyme inactivates leucyl tRNA synthetase in extracts of Sacchacromyces cerevisiae
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?
additional information
?
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the enzyme inactivates 6-phosphogluconate dehydrogenase and uricase
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?
additional information
?
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the enzyme inactivates 6-phosphogluconate dehydrogenase and uricase
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?
additional information
?
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the enzyme is able to maintain viability under starvation
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?
additional information
?
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Pbn1p shown as an essential chaperone-like protein in the endoplasmic reticulum of yeast, essential function of the Pbn1 protein for protein processing in the membrane of the endoplasmic reticulum described, requirement for proper folding and stability of a subset of proteins in the endoplasmic reticulum indicated
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?
additional information
?
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protease-knockout strains constructed, processing of vacuolar proteases using a novel cell-surface engineering technique described
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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the enzyme is able to maintain viability under starvation
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
proteinase B inhibitor
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proteinase B inhibitor 1 and 2 are polypeptides of 8500 Da
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additional information
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inhibition by turkey egg white fraction II-T
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additional information
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proteinase B is difficult to detect unless the firmly bound inhibitor is previously inactivated. Procedure to unmask proteinase B activity by trypsin treatment
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
processing activities of transient proteins of the endoplasmic reticulum indicated, depletion of Pbn1p abrogates processing of precursor proteins of the endoplasmic reticulum but not global exit from the endoplasmic reticulum, significant increase in the unfolded protein response pathway observed indicating defects in protein folding in the endoplasmic reticulum
additional information
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processing of different vacuolar proteases by using protease B-knockout strains indicated
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
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80% or more of the proteinase in the yeast cell is in the zymogen form and seems to be particle-bound
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
43000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
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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
side-chain modification
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contains 8-9% neutral sugars and 1.5% amino sugars
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing in absence of glycerol results in total loss of activity
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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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration
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
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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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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high-level production of human mechano-growth factor in Saccharomyces cerevisiae is interfered by proteinase B. Expression of mechano-growth factor in a proteinase B deletion mutant results in a fivefold increase of yield
synthesis
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much stricter experimental protocols than those routinely used are necessary to prevent the artefactual interpretation of protein levels in strains or conditions that increase proteinase B activity. Stability of some proteins, such as Slt2p or Chs4p, but not others, is severely compromised in the rim101 mutant due to the upregulation of the PRB1 gene. Proteolytic degradation during protein processing can be almost completely prevented by an overdose of subtilisin-like protease inhibitors, such as PMSF, or by avoiding cell freezing
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nowak, J.; Tsai, H.
Purification and properties of three endopeptidases from baker's yeast
Can. J. Microbiol.
35
295-303
1989
Saccharomyces cerevisiae
Kominami, E.; Hoffschulte, H.; Holzer, H.
Purification and properties of proteinase B from yeast
Biochim. Biophys. Acta
661
124-135
1981
Saccharomyces cerevisiae
Kominami, E.; Hoffschulte, H.; Leuschel, L.; Maier, K.; Holzer, H.
The substrate specificity of proteinase B from baker's yeast
Biochim. Biophys. Acta
661
136-141
1981
Saccharomyces cerevisiae
Fujishiro, K.; Sanada, Y.; Tanaka, H.; Katunuma, N.
Purification and characterization of yeast protease B
J. Biochem.
87
1321-1326
1980
Saccharomyces cerevisiae
Maier, K.; Muller, H.; Holzer, H.
Purification and molecular characterization of two inhibitors of yeast proteinase B
J. Biol. Chem.
254
8491-8497
1979
Saccharomyces cerevisiae
Looze, Y.; Gillet, L.; Deconinck, M.; Couteaux, B.; Polastro, E.; Leonis, J.
Protease B from Saccharomyces cerevisiae. Purification and characterization
Int. J. Pept. Protein Res.
13
253-259
1979
Saccharomyces cerevisiae
Sanada, Y.; Fujishiro, K.; Tanaka, H.; Katunuma, N.
Isolation and characterization of yeast protease B
Biochem. Biophys. Res. Commun.
86
815-821
1979
Saccharomyces cerevisiae
Holzer, H.
Chemistry and biology of macromolecular inhibitors from yeast acting on proteinases A and B, and carboxypeptidase Y
Adv. Enzyme Regul.
13
125-134
1975
Saccharomyces cerevisiae
Felix, F.; Brouillet, N.
Purification et proprietes de deux peptidases de levure de brasserie
Biochim. Biophys. Acta
122
127-144
1966
Saccharomyces cerevisiae
Schwencke, J.
Measurement of proteinase B activity in crude yeast extracts: a novel procedure of activation using pepsin
Anal. Biochem.
118
315-321
1981
Saccharomyces cerevisiae
Lenney, J.F.; Dalbec, J.M.
Purification and properties of two proteinases from Saccharomyces cerevisiae
Arch. Biochem. Biophys.
120
42-48
1967
Saccharomyces cerevisiae
Hirsch.H.H.; Schiffer, H.H.; Muller, H.; Wolf, D.H.
Biogenesis of the yeast vacuole (lysosome). Mutation in the active site of the vacuolar serine proteinase yscB abolishes proteolytic maturation of its 73-kDa precursor to the 41-5-kDa pro-enzyme and a newly detected 41-kDa peptide
Eur. J. Biochem.
203
641-653
1992
Saccharomyces cerevisiae
Rupp, S.; Wolf, D.H.
Biogenesis of the yeast vacuole (lysosome). The use of active-site mutants of proteinase yscA to determine the necessity of the enzyme for vacuolar proteinase maturation and proteinase yscB stability
Eur. J. Biochem.
231
115-125
1995
Saccharomyces cerevisiae
Larrinoa, I.F.; Heredia, C.F.
Yeast proteinase yscb inactivates the leucyl tRNA synthetase in extracts of Saccharomyces cerevisiae
Biochim. Biophys. Acta
1073
502-508
1991
Saccharomyces cerevisiae
Campbell, A.A.; Slaughter, J.C.; Sturgeon, R.J.
Inhibition of proteinase B and stabilisation of malate dehydrogenase in extracts of the yeast Saccharomyces cerevisiae by turkey egg white fraction II-T
J. Gen. Appl. Microbiol.
41
449-453
1995
Saccharomyces cerevisiae
-
Moehle, C.M.; Tizard, R.; Lemmon, S.K.; Smart, J.; Jones, E.W.
Protease B of the lysosomelike vacuole of the yeast Saccharomyces cerevisiae is homologous to the subtilisin family of serine proteases
Mol. Cell. Biol.
7
4390-4399
1987
Saccharomyces cerevisiae
Nebes, V.L.; Jones, E.W.
Activation of the proteinase B precursor of the yeast Saccharomyces cerevisiae by autocatalysis and by an internal sequence
J. Biol. Chem.
266
22851-22857
1991
Saccharomyces cerevisiae
Subramanian, S.; Woolford, C.A.; Drill, E.; Lu, M.; Jones, E.W.
Pbn1p: an essential endoplasmic reticulum membrane protein required for protein processing in the endoplasmic reticulum of budding yeast
Proc. Natl. Acad. Sci. USA
103
939-944
2006
Saccharomyces cerevisiae (P25580), Saccharomyces cerevisiae BJ 5410 (P25580)
Kato, M.; Kuzuhara, Y.; Maeda, H.; Shiraga, S.; Ueda, M.
Analysis of a processing system for proteases using yeast cell surface engineering: conversion of precursor of proteinase A to active proteinase A
Appl. Microbiol. Biotechnol.
72
1229-1237
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae MT8-1
Morozkina, E.V.; Marchenko, A.N.; Keruchenko, J.S.; Keruchenko, I.D.; Khotchenkov, V.P.; Popov, V.O.; Benevolensky, S.V.
Proteinase B disruption is required for high level production of human mechano-growth factor in Saccharomyces cerevisiae
J. Mol. Microbiol. Biotechnol.
18
188-194
2010
Saccharomyces cerevisiae
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