Information on EC 3.4.23.35 - Barrierpepsin

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The expected taxonomic range for this enzyme is: Saccharomyces cerevisiae

EC NUMBER
COMMENTARY hide
3.4.23.35
-
RECOMMENDED NAME
GeneOntology No.
Barrierpepsin
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Selective cleavage of -Leu6-/-Lys- bond in the pheromone alpha-mating factor
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
152060-38-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain X2180-1A, gene BAR1
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha Factor + H2O
?
show the reaction diagram
alpha Factor + H2O
Trp-His-Trp-Leu-Gln-Leu + Lys-Pro-Gly-Gln-Pro-Met-Tyr
show the reaction diagram
His-Trp-Leu-Gln-Leu-Arg-Pro-Gly-Gln-Pro-Met-Tyr + H2O
His-Trp-Leu-Gln-Leu + Arg-Pro-Gly-Gln-Pro-Met-Tyr
show the reaction diagram
-
cleavage site: Leu-Arg
-
-
-
His-Trp-Leu-Gln-Leu-Lys-Pro-Gly-Gln-Pro-Met-Tyr + H2O
His-Trp-Leu-Gln-Leu + Lys-Pro-Gly-Gln-Pro-Met-Tyr
show the reaction diagram
-
cleavage site: Leu-Lys
-
-
-
Trp-Leu-Gln-Leu-Lys-Pro-Gly-Gln-Pro-Met-Tyr + H2O
Trp-Leu-Gln-Leu + Lys-Pro-Gly-Gln-Pro-Met-Tyr
show the reaction diagram
-
cleavage site: Leu-Lys
-
-
-
WHWLQLKQGQPMY + H2O
WHWLQL + KQGQPMY
show the reaction diagram
additional information
?
-
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
alpha Factor + H2O
?
show the reaction diagram
WHWLQLKQGQPMY + H2O
WHWLQL + KQGQPMY
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tosyl-Arg methyl ester
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
alpha factor
-
pH 5.5, 0.1 M acetate buffer
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 5.3
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 6.5
-
about half-maximal activity at pH 2.5 and 6.5
2.6 - 6.8
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
-
x * 200000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Mutant enzyme undergoes extensive proteolysis during purification with little or no loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, enzyme precipitated by cold ethanol and resuspended in water
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from Saccharomyces cerevisiae XP635 cells transformed with pZV24; the heavy glycosylation allows enzyme precipitation with ethanol
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purification from wild-type cells has been hampered because of the heterogeneous hyperglycosylation of the protein; to near homogeneity
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recombinant enzyme 2000fold by two different steps of anion exchange chromatography and gle filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Saccharomyces cerevisiae, by in vivo complementation of a bar1 mutation in yeast strain XP635-10C
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