Information on EC 3.4.24.30 - coccolysin

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The expected taxonomic range for this enzyme is: Lactobacillales

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
-
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
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
-
-
-
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
-
-
-
Lys-Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
-
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-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
?
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
-
-
?
succinyl-Val-Pro-Phe-p-nitroanilide + H2O
?
show the reaction diagram
-
-
?
[Lys1]Bradykinin + H2O
?
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
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+
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
-
i.e. o-chloranil, 0.003 mM, most potent inactivator
chymostatin
75% inhibition
Diethylpyrocarbonate
-
partially reversed by hydroxylamine (not)
high molecular mass inflammatory factor
-
-
-
High MW factor of rat inflammatory exudate
-
strong, MW: 720000-750000
-
iodoacetic acid
83% inhibition
L-cysteine
-
-
L-Leucine hydroxamate
-
-
metal chelator
-
inactivates
-
methanol
-
about 15% as effective as n-butanol
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
phenylmethylsulfonyl fluoride
strongly inhibited, 100% inhibition
phosphoramidon
-
i.e. N-(alpha-L-rhamnopyranosyloxy-hydroxyphosphinyl)-L-Leu-L-Trp
Tetranitromethane
-
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
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
32000
-
Streptococcus faecalis, gel filtration
39000
-
Steptococcus thermophilus, gel filtration
153000
purified enzyme
169000
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
coccolysin is a virulence factor
nutrition