Information on EC 3.4.24.30 - coccolysin

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The expected taxonomic range for this enzyme is: Lactobacillales

EC NUMBER
COMMENTARY
3.4.24.30
-
RECOMMENDED NAME
GeneOntology No.
coccolysin
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Preferential cleavage: -/-Leu, -/-Phe, -/-Tyr, -/-Ala
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cell envelope protein
Q9F8Q4
-
cell envelope protein
Streptococcus thermophilus CNRZ 385
Q9F8Q4
-
-
cell wall-anchored proteinase
Q9F8Q4
-
cell wall-anchored proteinase
Streptococcus thermophilus CNRZ 385
Q9F8Q4
-
-
CEP
Streptococcus thermophilus CNRZ 385
Q9F8Q4
-
-
EC 3.4.24.4
-
-
formerly
-
EM 19000
-
-
-
-
metalloendopeptidase II
-
-
microbial proteinase
-
-
PrtS
Streptococcus thermophilus CNRZ 385
Q9F8Q4
-
-
streptococcal gelatinase
-
-
Streptococcus thermophilus intracellular proteinase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
156859-08-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Enterobacter faecalis
OG1-10
-
-
Manually annotated by BRENDA team
Enterobacter faecalis OG1-10
OG1-10
-
-
Manually annotated by BRENDA team
var. liquefaciens, strain OG1-10
-
-
Manually annotated by BRENDA team
var. liquefaciens, straom 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
Streptococcus thermophilus CNRZ 385
CNRZ 385
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-methoxysuccinyl-Arg-Pro-Tyr-p-nitroanilide + H2O
?
show the reaction diagram
Q9F8Q4, -
-
-
?
3-methoxysuccinyl-Arg-Pro-Tyr-p-nitroanilide + H2O
?
show the reaction diagram
Streptococcus thermophilus CNRZ 385
Q9F8Q4
-
-
?
acetyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
show the reaction diagram
Q9F8Q4, -
-
-
?
acetyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
show the reaction diagram
Streptococcus thermophilus CNRZ 385
Q9F8Q4
-
-
?
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
-
-
-
-
?
Azocoll + H2O
?
show the reaction diagram
-
general protease substrate
-
-
-
Azocoll + H2O
?
show the reaction diagram
Enterobacter faecalis, Enterobacter faecalis OG1-10
-
general protease substrate
-
-
-
beta-casein + H2O
?
show the reaction diagram
Q9F8Q4, -
-
-
?
beta-casein + H2O
?
show the reaction diagram
Streptococcus thermophilus CNRZ 385
Q9F8Q4
-
-
?
beta-Lipotropin
?
show the reaction diagram
-
cleavage site: Gly63-Phe64, poor substrate
-
-
-
Big endothelin-1 + H2O
?
show the reaction diagram
Enterobacter faecalis, Enterobacter faecalis OG1-10
-
human, cleavage sites: Ser5-Leu6 and His16-Leu17
-
-
-
Big endothelin-1 fragment(22-38) + H2O
Hydrolyzed fragment of big endothelin fragment
show the reaction diagram
Enterobacter faecalis, Enterobacter faecalis OG1-10
-
-
peptides (Val22-Val28) and (Val29-Gly32) and (Leu33-Ser38)
-
Bovine casein-yellow + H2O
?
show the reaction diagram
-
-
-
-
-
Bovine fibrinogen + H2O
?
show the reaction diagram
-
B-chain and to a lesser extent A-chain
-
-
-
Bovine fibrinogen + H2O
?
show the reaction diagram
-
plasminogen-free or fraction I
-
-
-
Bovine hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
-
Bovine pancreas insulin + H2O
?
show the reaction diagram
-
poor substrate
-
-
-
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
-
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
Q9F8Q4, -
-
-
?
casein + H2O
?
show the reaction diagram
Streptococcus thermophilus CNRZ 385
Q9F8Q4
-
-
?
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
-
-
-
Endothelin 1 + H2O
?
show the reaction diagram
Enterobacter faecalis, Enterobacter faecalis OG1-10
-
presumably involved in initiation and propagation of Enterobacter faecalis associated inflammations, destroys biological activity of endothelin 1
-
-
-
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
-
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Glucagon + H2O
?
show the reaction diagram
-
-
-
-
-
Glucagon + H2O
?
show the reaction diagram
-
cleavage site: Trp25-Leu26
-
-
-
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
human endothelin 1 + H2O
?
show the reaction diagram
-
-
-
-
?
Human endothelin-1 + H2O
?
show the reaction diagram
Enterobacter faecalis, Enterobacter faecalis OG1-10
-
primary cleavage at Ser5-Leu6, subsequent hydrolysis of His16-Leu17, degradation resembles processing by thermolysin, identification of products
-
-
-
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
-
-
-
-
-
Insulin B-chain + H2O
?
show the reaction diagram
-
oxidized, best substrate, preferred cleavage at Phe24-Phe25, followed by His5-Leu6, after prolonged incubation: Ala14-Leu15 and His10-Leu11
-
-
-
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
-
-
-
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
-
-
-
N-3-(2-Furyl)acryloyl-Gly-L-Leu amide + H2O
?
show the reaction diagram
-
-
-
-
-
N-3-(2-Furyl)acryloyl-Gly-L-Leu amide + H2O
?
show the reaction diagram
-
chromogenic substrate, cleavage site: Gly-Leu, poor substrate
-
-
-
N-3-(2-Furyl)acryloyl-Gly-L-Phe + H2O
?
show the reaction diagram
-
chromogenic substrate
-
-
-
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
-
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
-
-
pheromone related peptide + 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
-
-
Substance P + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
-
Lys-Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
strict specificity for hydrophobic amino acid at position P1', exhibits endopeptidase and thermolysin-like specificity, very poor substrates are elastin-orcein or hide powder azure, No substrates are Ala-Ile-Phe-Ile-Ala-Ser (i.e. Streptococcus faecalis sex pheromone cAM373), aminoacyl-2-naphthylamides, Nalpha-benzoyl-DL-Arg 4-nitroanilide, phenylazobenzyloxycarbonyl-L-Pro-L-Leu-Gly-L-Pro-D-Arg, 2-furylacryloyl-L-Leu-Gly-L-Pro-L-Ala
-
-
-
additional information
?
-
-
No substrates are N-3-(2-furyl)acryloyl-Gly-Gly-Gly, N-3-(2-furyl)acryloyl-Gly-L-Leu or N-3-(2-furyl)acryloyl-Gly-L-Ala, neutral metalloendopeptidase, no aminopeptidase or esterase activity
-
-
-
additional information
?
-
Q9F8Q4, -
Bz-Phe-Val-Arg-p-nitroanilide, NZbz-Gly-Pro-Arg-p-nitroanilide, and Z-Phe-Arg-p-nitroanilide are no substrates
-
?
additional information
?
-
-
no cleavage of Pz-Pro-Leu-Gly-Pro-D-Arg and 2-FA-Leu-Gly-Pro-Ala
-
-
?
additional information
?
-
Streptococcus thermophilus CNRZ 385
Q9F8Q4
Bz-Phe-Val-Arg-p-nitroanilide, NZbz-Gly-Pro-Arg-p-nitroanilide, and Z-Phe-Arg-p-nitroanilide are no substrates
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-casein + H2O
?
show the reaction diagram
Q9F8Q4, -
-
-
?
beta-casein + H2O
?
show the reaction diagram
Streptococcus thermophilus CNRZ 385
Q9F8Q4
-
-
?
casein + H2O
?
show the reaction diagram
Q9F8Q4, -
-
-
?
casein + H2O
?
show the reaction diagram
Streptococcus thermophilus CNRZ 385
Q9F8Q4
-
-
?
Endothelin 1 + H2O
?
show the reaction diagram
Enterobacter faecalis, Enterobacter faecalis OG1-10
-
presumably involved in initiation and propagation of Enterobacter faecalis associated inflammations, destroys biological activity of endothelin 1
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
Q9F8Q4, -
highly activated by Ca2+ ions
NaBr
-
activation, 1-5 M, inhibits above
Zinc
-
requirement, metalloendopeptidase
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
3,4,5,6-Tetrachloro-1,2-benzoquinone
-
i.e. o-chloranil, 0.003 mM, most potent inactivator
chymostatin
Q9F8Q4, -
75% inhibition
Diethylpyrocarbonate
-
partially reversed by hydroxylamine (not)
EDTA
-
reversible by Co2+, Mn2+, Zn2+, Ca2+, Cu2+ or Mg2+ with decreasing order of efficiency, not by Cd2+, Ba2+, Ni2+ or Hg2+
EDTA
Q9F8Q4, -
30% inhibition
high molecular mass inflammatory factor
-
-
-
High MW factor of rat inflammatory exudate
-
strong, MW: 720000-750000
-
iodoacetic acid
Q9F8Q4, -
83% inhibition
L-Leucine hydroxamate
-
-
metal chelator
-
inactivates
-
N-Ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline
-
5 mM
NaBr
-
above 5 M, activates at 1-5 M
o-Chloranil
-
is a near-stoichiometric inhibitor of the enzyme
p-chloromercuribenzoate
-
not
p-chloromercuribenzoate
-
-
phenylmethylsulfonyl fluoride
Q9F8Q4, -
strongly inhibited, 100% inhibition
phosphoramidon
-
i.e. N-(alpha-L-rhamnopyranosyloxy-hydroxyphosphinyl)-L-Leu-L-Trp
Tetranitromethane
-
5 mM, pH-dependent
methanol
-
about 15% as effective as n-butanol
additional information
-
no inhibition by DTNB, carbodiimide/glycine ethyl ester; no inhibition by iodoacetate; no inhibition by PMSF, phenylglyoxal; no inhibition by tosyl-Leu chloromethyl ketone, tosyl-Phe chloromethyl ketone, trasylol (i.e. bovine lung trypsin inhibitor)
-
additional information
-
no inhibition by 2,3-butanedinone; no inhibition by PMSF, phenylglyoxal
-
additional information
-
diisopropyl fluorophosphate; no inhibition by iodoacetate
-
additional information
Q9F8Q4, -
no inhibition with bestatin or E64
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
substrate P
-
scissile bond Phe7-Phe8
-
0.049
-
substrate P
-
scissile bond Gln6-Phe7
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
-
broad, azocoll as substrate
6.5
-
-
N-3-(2-furyl)acryloyl-Gly-L-Leu amide as substrate
7.2
-
-
cleavage of Ser3-Leu4 in pheromone cAD1
additional information
-
-
pI: 5
additional information
-
-
pI: 4.6
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
spectrophotometric assay at
30
-
Enterobacter faecalis
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Enterobacter faecalis
-
-
-
Manually annotated by BRENDA team
Enterobacter faecalis OG1-10
-
-
-
-
Manually annotated by BRENDA team
Enterobacter faecalis
-
-
-
Manually annotated by BRENDA team
Enterobacter faecalis OG1-10
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
29500
-
-
Streptococcus faecalis, FPLC gel filtration
32000
-
-
Streptococcus faecalis, gel filtration
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 ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 30000, Streptococcus faecalis, SDS-PAGE
monomer
-
1 * 33000, Streptococcus faecalis, SDS-PAGE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.6
-
-
above, 17 h stable in 50 mM 2-[N-morpholino]ethanesulfonic acid buffer
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
55
-
-
rapid inactivation above
additional information
-
-
Ca2+ reduces thermal stability
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Rapid autolysis, Zn2+ as protease inhibitor protects, Ca2+ does not stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
At very low temperatures stored in the presence of Zn2+ as protease inhibitor to prevent autolysis of purified enzyme
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
prtS gene sequenced by performing PCR
Q9F8Q4, -
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
coccolysin is a virulence factor
nutrition
Q9F8Q4, -
wide utilization in the production of dairy products like yoghurt, hard cooked cheese, and soft cheese
nutrition
Streptococcus thermophilus CNRZ 385
-
wide utilization in the production of dairy products like yoghurt, hard cooked cheese, and soft cheese
-