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Information on EC 3.4.24.37 - saccharolysin
for references in articles please use BRENDA:EC3.4.24.37
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.24 Metalloendopeptidases
3.4.24.37 saccharolysin
IUBMB Comments
An 83 kDa cytoplasmic thiol-dependent metalloendopeptidase from Saccharomyces cerevisiae. In peptidase family M3 (thimet oligopeptidase family).
The enzyme appears in viruses and cellular organisms
- 3.4.24.37
-
thimet
-
metallo
- chymotrypsin
-
protease-mediated
- melon
- virgifera
-
instars
- pepsin
- inodorus
- honeydew
- rootworm
-
diabrotica
-
intermembrane
-
leconte
- degradation
- plasmin
- thuringiensis
- endopeptidases
-
midgut
- cucumisin
-
exopeptidase
-
3.4.21.25
-
cry3bb1
showSynonyms
proteinase yscd, protease d, saccharolysin, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 3.4.22.22
Oligopeptidase YSCD
-
-
-
-
PrD
protease D
Proteinase yscD
-
-
-
-
Proteinase, Saccharomyces cerevisiae, yscD
-
-
-
-
EC 3.4.22.22
-
-
formerly
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cleavage of Pro-/-Phe and Ala-/-Ala bonds
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
96779-48-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Acetyl-Ala-Ala-Pro-Ala 4-nitroanilide + H2O
Acetyl-Ala + Ala-Pro-Ala 4-nitroanilide
-
Substrates: -
Products: -
Products: -
?
Acetyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
Acetyl-Ala + Ala-Pro-Phe 4-nitroanilide
-
Substrates: -
Products: -
Products: -
?
acetyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
?
-
Substrates: -
Products: -
Products: -
?
Benzoyl-Pro-Phe-Arg 4-nitroanilide + H2O
Benzoyl-Pro + Phe-Arg 4-nitroanilide
-
Substrates: -
Products: -
Products: -
?
bradykinin + H2O
?
-
Substrates: cleaved at the Phe-Ser bond
Products: -
Products: -
?
Mcc-Pro-Leu-Gly-Pro-D-Lys(Dnp) + H2O
Mcc-Pro-Leu + Gly-Pro-D-Lys(Dnp)
-
Substrates: -
Products: -
Products: -
?
MeOSuc-Ala-Ala-Pro-Met-NHPhNO2 + H2O
?
-
Substrates: -
Products: -
Products: -
?
Methoxysuccinyl-Ala-Ala-Pro-Met 4-nitroanilide + H2O
Methoxysuccinyl-Ala + Ala-Pro-Met 4-nitroanilide
-
Substrates: -
Products: -
Products: -
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
Pz-Pro-Leu-Gly-Pro-D-Arg + H2O
Pz-Pro-Leu + Gly-Pro-D-Arg
-
Substrates: -
Products: -
Products: -
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: methylcasein
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is not involved in any vital event in mitochondrial biogenesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: no cleavage of peptides with a free N-terminus, azocasein and (3H)methylcasein
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: enzyme is not involved in any vital event in mitochondrial biogenesis
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
metalloprotease, not affeted by Cu2+, Co2+, Mn2+, and Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
inhibits 50% at 1 mM and 90% at 10 mM, can be efficiently reactivated by the addition of Zn2+, Co2+ and Mn2+
additional information
-
not inhibited by DTT, N-ethylmaleimide, iodoacetic acid or iodoacetamide
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from the natural microflora of fermented sausages and selected as possible starter culture on the basis of its physiological and biochemical properties and its ability to compete during sausage manufacturing processes
-
-
brenda
isolated from the natural microflora of fermented sausages and selected as possible starter culture on the basis of its physiological and biochemical properties and its ability to compete during sausage manufacturing processes
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-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
midgut juice (pH 5.75) from third instars larvae
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PRTD_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
712
0
81934
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
deletion of Prd1, in deltayme1 cells increase of large peptides in the mitochondrial supernatant, in delta mop112 cells no effect on growth
additional information
-
prd1-6 mutants with thermolabile saccharolysin activity, prd1::URA3 mutants devoid of the cytoplasmic and mitochondrial activities
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 2560fold by fractionation with protamine sulfate, anion exchange chromatography on a weak followed by a strong anion exchange resin, and gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
degradation
-
Prd1 together with Mop112 is involved in the complete degradation of a large number of mitochondrial proteins to amino acids and therefore broadly influences the peptide efflux from mitochondria
degradation
-
most likely major intracellular oligopeptidase responsible for the degradation of peptides resulting from nonvacuolar proteolysis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Achstetter, T.; Ehmann, C.; Wolf, D.H.
Proteinase yscD. Purification and characterization of a new yeast peptidase
J. Biol. Chem.
260
4585-4590
1985
Saccharomyces cerevisiae
brenda
Garcia-Alvarez, N.; Teichert, U.; Wolf, D.H.
Proteinase yscD mutants of yeast. Isolation and characterization
Eur. J. Biochem.
163
339-346
1987
Saccharomyces cerevisiae
brenda
dEnfert, C.; Ibrahim-Granet, O.
Saccharolysin
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
1
360-361
2004
Saccharomyces cerevisiae
-
brenda
Kambacheld, M.; Augustin, S.; Tatsuta, T.; Mueller, S.; Langer, T.
Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria
J. Biol. Chem.
280
20132-20139
2005
Saccharomyces cerevisiae
brenda
Bolumar, T.; Sanz, Y.; Aristoy, M.C.; Toldra, F.
Purification and characterisation of proteases A and D from Debaryomyces hansenii
Int. J. Food Microbiol.
124
135-141
2008
Debaryomyces hansenii, Debaryomyces hansenii CECT 12487
brenda
Kaiser-Alexnat, R.
Protease activities in the midgut of Western corn rootworm (Diabrotica virgifera virgifera LeConte)
J. Invertebr. Pathol.
100
169-174
2009
Diabrotica virgifera virgifera
brenda
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