Information on EC 3.4.24.37 - saccharolysin

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The expected taxonomic range for this enzyme is: Opisthokonta

EC NUMBER
COMMENTARY
3.4.24.37
-
RECOMMENDED NAME
GeneOntology No.
saccharolysin
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cleavage of Pro-/-Phe and Ala-/-Ala bonds
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
EC 3.4.22.22
-
-
formerly
-
EC 3.4.22.22
-
formerly
Oligopeptidase YSCD
-
-
-
-
PrD
Debaryomyces hansenii CECT 12487, Debaryomyces hansenii CECT12487
-
-
-
protease D
-
-
protease D
Debaryomyces hansenii CECT 12487, Debaryomyces hansenii CECT12487
-
-
-
Proteinase yscD
-
-
-
-
Proteinase, Saccharomyces cerevisiae, yscD
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
96779-48-5
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain CECT 12487, 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
-
-
Manually annotated by BRENDA team
Debaryomyces hansenii CECT 12487
strain CECT 12487, 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
-
-
Manually annotated by BRENDA team
Western corn rootworm
-
-
Manually annotated by BRENDA team
mutants devoid of proteinase yscD
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ac-Ala-Ala-Pro-Met-NHPhNO2 + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-Ala-Ala-Pro-Phe-NHPhNO2 + H2O
?
show the reaction diagram
-
-
-
-
?
Acetyl-Ala-Ala-Pro-Ala 4-nitroanilide + H2O
Acetyl-Ala + Ala-Pro-Ala 4-nitroanilide
show the reaction diagram
-
-
-
-
Acetyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
Acetyl-Ala + Ala-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
acetyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Benzoyl-Pro-Phe-Arg 4-nitroanilide + H2O
Benzoyl-Pro + Phe-Arg 4-nitroanilide
show the reaction diagram
-
-
-
-
Bradykinin + H2O
?
show the reaction diagram
-
cleaved at the Phe-Ser bond
-
-
?
Bz-Pro-Phe-Arg-NHPhNO2 + H2O
?
show the reaction diagram
-
-
-
-
?
Dnp-Pro-Leu-Gly-Pro-Trp-D-Lys + H2O
?
show the reaction diagram
-
-
-
-
?
MeOSuc-Ala-Ala-Pro-Met-NHPhNO2 + H2O
?
show the reaction diagram
-
-
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
Debaryomyces hansenii, Debaryomyces hansenii CECT 12487, Debaryomyces hansenii CECT12487
-
-
-
-
?
Pz-Pro-Leu-Gly-Pro-D-Arg,Mcc-Pro-Leu-Gly-Pro-D-Lys(Dnp) + H2O
?
show the reaction diagram
-
-
-
-
?
Methoxysuccinyl-Ala-Ala-Pro-Met 4-nitroanilide + H2O
Methoxysuccinyl-Ala + Ala-Pro-Met 4-nitroanilide
show the reaction diagram
-
-
-
-
additional information
?
-
-
not: methylcasein
-
-
-
additional information
?
-
-
enzyme is not involved in any vital event in mitochondrial biogenesis
-
-
-
additional information
?
-
-
no cleavage of peptides with a free N-terminus, azocasein and (3H)methylcasein
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme is not involved in any vital event in mitochondrial biogenesis
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
metalloprotease, not affeted by Cu2+, Co2+, Mn2+, and Ca2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
complete inhibition at 0.1 mM
2-mercaptoethanol
-
19% inhibition at 5 mM
3,4-Dichloroisocoumarin
-
71% inhibition at 1 mM
4-chloromercuribenzoate
-
complete inhibition at 0.1 mM
4-hydroxymercuribenzoate
-
100% inhibition with 0.1 mM
Cd2+
-
33% inhibition at 0.5 mM
Cpp-Ala-Ala-Phe-p-aminobenzoic acid
-
strongly inhibits
DTT
-
19% inhibition at 1 mM
EDTA
-
inhibits 50% at 1 mM and 90% at 10 mM, can be efficiently reactivated by the addition of Zn2+, Co2+ and Mn2+
EGTA
-
35% inhibition at 5 mM
Hg2+
-
complete inhibition at 0.05 mM
HgCl2
-
100% inhibition with 0.01 mM
Mercurials
-
-
-
Pepstatin
-
weak
pepstatin A
-
15% inhibition at 1 mM
PMSF
-
50% inhibition at 1 mM
Zn2+
-
73% inhibition at 0.5 mM
Mg2+
-
21% inhibition at 0.5 mM
additional information
-
not inhibited by DTT, N-ethylmaleimide, iodoacetic acid or iodoacetamide
-
additional information
-
no inhibition by EDTA at 5 mM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iodoacetate
-
11% activation at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.19
Ac-Ala-Ala-Pro-Met-NHPhNO2
-
-
0.085
Ac-Ala-Ala-Pro-Phe-NHPhNO2
-
-
0.19
Acetyl-Ala-Ala-Pro-Ala 4-nitroanilide
-
-
0.085
Acetyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
-
0.06
benzoyl-Pro-Phe-Arg 4-nitroanilide
-
-
0.06
Bz-Pro-Phe-Arg-NHPhNO2
-
-
0.029
Dnp-Pro-Leu-Gly-Pro-Trp-D-Lys
-
-
0.035
MeOSuc-Ala-Ala-Pro-Met-NHPhNO2
-
-
0.035
Methoxysuccinyl-Ala-Ala-Pro-Met 4-nitroanilide
-
-
0.006
Pz-Pro-Leu-Gly-Pro-D-Arg
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6000
Acetyl-Ala-Ala-Pro-Ala 4-nitroanilide
-
-
38000
Acetyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
-
1500
benzoyl-Pro-Phe-Arg 4-nitroanilide
-
-
38000
Methoxysuccinyl-Ala-Ala-Pro-Met 4-nitroanilide
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
-
methoxy-succinyl-Ala-Ala-Pro-Met 4-nitroanilide
5.8 - 6
-
acetyl-Ala-Ala-Pro-Ala 4-nitroanilide
6.5 - 7
-
benzoyl-Pro-Phe-Arg 4-nitroanilide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
-
with MeOSuc-Ala-Ala-Pro-Met-NHPhNO2
5.9
-
with Ac-Ala-Ala-Pro-Met-NHPhNO2
7.9
-
with Bz-Pro-Phe-Arg-NHPhNO2
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
midgut juice (pH 5.75) from third instars larvae
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
68000
-
gel filtration
683560
81800
-
-
668761
86000
-
Saccharomyces cerevisiae, gel filtration
31230
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 65000, SDS-PAGE
monomer
-
1 * 83000, Saccharomyces cerevisiae, SDS-PAGE
monomer
Debaryomyces hansenii CECT 12487, Debaryomyces hansenii CECT12487
-
1 * 65000, SDS-PAGE
-
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
-
250fold by chromatographies
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
-
most likely major intracellular oligopeptidase responsible for the degradation of peptides resulting from nonvacuolar proteolysis
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