Information on EC 3.4.24.30 - coccolysin

for references in articles please use BRENDA:EC3.4.24.30
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.24.30
-
RECOMMENDED NAME
GeneOntology No.
coccolysin
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage: -/-Leu, -/-Phe, -/-Tyr, -/-Ala
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
156859-08-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Enterobacter faecalis
OG1-10
-
-
Manually annotated by BRENDA team
Enterobacter faecalis OG1-10
OG1-10
-
-
Manually annotated by BRENDA team
no activity in Enterococcus faecalis
-
-
-
Manually annotated by BRENDA team
no activity in Enterococcus faecalis Symbioflor 1
-
-
-
Manually annotated by BRENDA team
CNRZ 385
Q9F8Q4
SwissProt
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
3-methoxysuccinyl-Arg-Pro-Tyr-p-nitroanilide + H2O
?
show the reaction diagram
acetyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
show the reaction diagram
Ala-Leu-Ile-Leu-Thr-Leu-Val-Ser + H2O
Ala-Leu-Ile-Leu-Thr + Leu-Val-Ser
show the reaction diagram
-
i.e. iPDI, competitive inhibitor of Streptococcus faecalis sex pheromones
-
-
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin I + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro + Phe-His-Leu
show the reaction diagram
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
-
-
Angiotensin II + H2O
?
show the reaction diagram
-
only cleaved at Tyr-Ile
-
-
?
Angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
show the reaction diagram
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
-
-
Azoalbumin + H2O
?
show the reaction diagram
-
bovine albumin, fraction V
-
-
-
azocasein + H2O
?
show the reaction diagram
-
-
-
-
-
Azocoll + H2O
?
show the reaction diagram
beta-casein + H2O
?
show the reaction diagram
beta-Lipotropin
?
show the reaction diagram
-
cleavage site: Gly63-Phe64, poor substrate
-
-
-
Big endothelin-1 + H2O
?
show the reaction diagram
Big endothelin-1 fragment(22-38) + H2O
Hydrolyzed fragment of big endothelin fragment
show the reaction diagram
Bovine casein-yellow + H2O
?
show the reaction diagram
-
-
-
-
-
Bovine fibrinogen + H2O
?
show the reaction diagram
Bovine hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
-
Bovine pancreas insulin + H2O
?
show the reaction diagram
-
poor substrate
-
-
-
Bradykinin + H2O
?
show the reaction diagram
casein + H2O
?
show the reaction diagram
Cholecystokinin + H2O
?
show the reaction diagram
-
cleavage site: Gly29-Trp30
-
-
-
clots milk + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
high or low viscose polypetides from collagen
-
-
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Endothelin 1 + H2O
?
show the reaction diagram
Gelatin + H2O
?
show the reaction diagram
Glucagon + H2O
?
show the reaction diagram
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
human endothelin 1 + H2O
?
show the reaction diagram
-
-
-
-
?
Human endothelin-1 + H2O
?
show the reaction diagram
Insulin A-chain + H2O
Fragments of insulin A-chain
show the reaction diagram
-
cleavage at Gln15-Leu16 and Tyr14-Gln15, to a much lesser extent than B-chain
peptides (Gln1-Gln15) and (Leu16-Asn21), another product formed: peptide (Gln1-Trp14)
-
insulin B chain + H2O
?
show the reaction diagram
-
rapidly hydrolyzed at Phe24-Phe25, followed by the cleavage of the His5-Leu6 and other bonds
-
-
?
Insulin B-chain + H2O
?
show the reaction diagram
Leu-Phe-Ser-Leu-Val-Leu-Ala-Gly + H2O
Leu-Phe-Ser + Leu-Val-Leu-Ala-Gly
show the reaction diagram
-
i.e. cADI, Streptococcus faecalis sex pheromone, poor substrate
-
-
Leu-Phe-Val-Val-Thr-Leu-Val-Gly + H2O
Leu-Phe-Val-Val-Thr + Leu-Val-Gly
show the reaction diagram
-
i.e. iADI, competitive inhibitor of Streptococcus faecalis sex pheromones
-
-
Leucine-enkephalin + H2O
?
show the reaction diagram
-
cleavage site: Gly3-Phe4, poor substrate
-
-
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Lys-Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
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N-3-(2-Furyl)acryloyl tripeptides derivatives + H2O
?
show the reaction diagram
-
chromogenic substrates, e.g. -L-Ala-L-Ala-L-Ala, -Gly-L-Phe-L-Phe, -L-Phe-L-Phe-L-Phe, -Gly-L-Leu-L-Tyr, -Gly-L-Met-L-Leu, -L-Leu-L-Leu-L-Leu
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N-3-(2-Furyl)acryloyl-Gly-L-Leu amide + H2O
?
show the reaction diagram
N-3-(2-Furyl)acryloyl-Gly-L-Phe + H2O
?
show the reaction diagram
-
chromogenic substrate
-
-
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neurotensin + H2O
fragments of neurotensin
show the reaction diagram
-
cleavage site: Tyr11-Ile12, poor substrate
peptides (Arg1-Gly9) and (Leu10-Met11) are the first occuring products
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Phe-Leu-Val-Met-Phe-Leu-Ser-Gly + H2O
Phe-Leu-Val-Met-Phe + Leu-Ser-Gly
show the reaction diagram
-
i.e. cPDI, Streptococcus faecalis sex pheromone, poor substrate
-
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pheromone related peptide + H2O
?
show the reaction diagram
-
-
-
-
?
Substance P + H2O
?
show the reaction diagram
-
-
-
-
?
Substance P + H2O
Arg-Pro-Lys-Pro-Gln-Gln + Phe + Phe-Gly + Leu-Met-NH2
show the reaction diagram
-
i.e. Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2
-
-
succinyl-Ala-Glu-Pro-Phe-p-nitroanilide + H2O
?
show the reaction diagram
Q9F8Q4
-
-
?
succinyl-Val-Pro-Phe-p-nitroanilide + H2O
?
show the reaction diagram
Q9F8Q4
-
-
?
[Lys1]Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
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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
beta-casein + H2O
?
show the reaction diagram
casein + H2O
?
show the reaction diagram
Endothelin 1 + H2O
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
Q9F8Q4
highly activated by Ca2+ ions
NaBr
-
activation, 1-5 M, inhibits above
Zinc
-
requirement, metalloendopeptidase
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
3,4,5,6-Tetrachloro-1,2-benzoquinone
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i.e. o-chloranil, 0.003 mM, most potent inactivator
chymostatin
Q9F8Q4
75% inhibition
Diethylpyrocarbonate
-
partially reversed by hydroxylamine (not)
high molecular mass inflammatory factor
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-
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High MW factor of rat inflammatory exudate
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strong, MW: 720000-750000
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iodoacetic acid
Q9F8Q4
83% inhibition
L-cysteine
-
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L-Leucine hydroxamate
-
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metal chelator
-
inactivates
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methanol
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about 15% as effective as n-butanol
N-Ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline
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5 mM
NaBr
-
above 5 M, activates at 1-5 M
o-Chloranil
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is a near-stoichiometric inhibitor of the enzyme
p-chloromercuribenzoate
phenylmethylsulfonyl fluoride
Q9F8Q4
strongly inhibited, 100% inhibition
phosphoramidon
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i.e. N-(alpha-L-rhamnopyranosyloxy-hydroxyphosphinyl)-L-Leu-L-Trp
Tetranitromethane
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5 mM, pH-dependent
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0725
Insulin B-chain
-
scissile bond Phe24-Phe25
5
N-3-(2-furyl)acryloylglycyl-L-leucinamide
-
-
0.12
Substance P
-
scissile bond Gly9-Leu10
0.02 - 0.049
substrate P
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
broad, azocoll as substrate
7.2
-
cleavage of Ser3-Leu4 in pheromone cAD1
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7.5
-
about half-maximal activity at pH 5 and 7.5, N-3-(2-furyl)acryloyl-Gly-L-Leu amide as substrate
5.5 - 8.5
Q9F8Q4
about 70% activity remaining at pH 7.0 and pH 8.0
6 - 8
-
with azocoll as substrate
7 - 7.2
-
with shorter peptides as substrates
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
spectrophotometric assay at
30
Enterobacter faecalis
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29500
-
Streptococcus faecalis, FPLC gel filtration
30000
-
x * 30000, Streptococcus faecalis, SDS-PAGE
32000
-
Streptococcus faecalis, gel filtration
33000
-
1 * 33000, Streptococcus faecalis, SDS-PAGE
39000
-
Steptococcus thermophilus, gel filtration
153000
Q9F8Q4
purified enzyme
169000
Q9F8Q4
deduced from nucleotide sequence of prtS
additional information
-
amino acid composition shows similarity to Staphylococcus aureus metalloendopeptidase
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 30000, Streptococcus faecalis, SDS-PAGE
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6
-
above, 17 h stable in 50 mM 2-[N-morpholino]ethanesulfonic acid buffer
31192
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
rapid inactivation above
additional information
-
Ca2+ reduces thermal stability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Rapid autolysis, Zn2+ as protease inhibitor protects, Ca2+ does not stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
At very low temperatures stored in the presence of Zn2+ as protease inhibitor to prevent autolysis of purified enzyme
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
prtS gene sequenced by performing PCR
Q9F8Q4
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
coccolysin is a virulence factor
nutrition