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Information on EC 3.2.1.87 - capsular-polysaccharide endo-1,3-alpha-galactosidase
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EC Tree
3.2.1.87 capsular-polysaccharide endo-1,3-alpha-galactosidaseIUBMB Comments
Hydrolyses the galactosyl-alpha-1,3-D-galactose linkages only in the complex substrate, bringing about depolymerization.
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Word Map
- 3.2.1.87
- bacteriophage
-
o-antigens
-
beta-helix
-
endorhamnosidase
- octasaccharide
-
homotrimeric
-
carbapenem-resistant
-
t7-like
-
antivirulence
- endosialidase
- siphoviridae
- podoviridae
-
beta-helices
-
phage-encoded
The enzyme appears in viruses and cellular organisms
Synonyms
tailspike protein, tail fiber protein, polysaccharide depolymerase, capsule depolymerase, dpo48, kp32gp38, depokp36, kp32gp37, k1h depolymerase, k30 depolymerase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
capsule depolymerase
galactohydrolase, capsular polysaccharide
-
-
-
-
K30/K69 depolymerase
K30/K69dep
K5 depolymerase
K5dep
K8 depolymerase
K8dep
phage capsule depolymerase
polysaccharide depolymerase
tail fiber protein
tailspike protein
polysaccharide depolymerase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[Galalpha(1-3)(GlcAbeta(1-2))Manalpha(1-3)Galalpha(1-3)]n + H2O = [Galalpha(1-3)(GlcAbeta(1-2))Manalpha(1-3)Galalpha(1-3]n-1 + Galalpha(1-3)(GlcAbeta(1-2))Manalpha(1-3)Galalpha
hydrolyzes the galactosyl-alpha-1,3-D-galactose linkages only in the complex substrate, bringing about depolymerization
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
Aerobacter-capsular-polysaccharide galactohydrolase
Hydrolyses the galactosyl-alpha-1,3-D-galactose linkages only in the complex substrate, bringing about depolymerization.
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CAS REGISTRY NUMBER
COMMENTARY
62213-16-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Klebsiella pneumoniae capsule exopolysaccharides + H2O
?
-
-
-
?
[D-Gal-(1-3)(D-GlcUA-(1-2))-alpha-D-Man-(1-3)-alpha-D-Gal]n + H2O
D-Gal-(1-3)(D-GlcUA-(1-2))-alpha-D-Man-(1-3)-alpha-D-Gal
Klebsiella capsular polysaccharide + H2O
Klebsiella capsular monosaccharides
-
-
-
?
Klebsiella capsular polysaccharide + H2O
Klebsiella capsular monosaccharides
-
-
-
?
[D-Gal-(1-3)(D-GlcUA-(1-2))-alpha-D-Man-(1-3)-alpha-D-Gal]n + H2O
D-Gal-(1-3)(D-GlcUA-(1-2))-alpha-D-Man-(1-3)-alpha-D-Gal
-
capsular, polysaccharide produced by Aerobacter aerogenes, hydrolyzes the galactosyl-alpha-1,3-D-galactose linkages only in the complex substrate, bringing about depolymerization
-
?
[D-Gal-(1-3)(D-GlcUA-(1-2))-alpha-D-Man-(1-3)-alpha-D-Gal]n + H2O
D-Gal-(1-3)(D-GlcUA-(1-2))-alpha-D-Man-(1-3)-alpha-D-Gal
-
capsular, polysaccharide produced by Aerobacter aerogenes, hydrolyzes the galactosyl-alpha-1,3-D-galactose linkages only in the complex substrate, bringing about depolymerization
-
?
[D-Gal-(1-3)(D-GlcUA-(1-2))-alpha-D-Man-(1-3)-alpha-D-Gal]n + H2O
D-Gal-(1-3)(D-GlcUA-(1-2))-alpha-D-Man-(1-3)-alpha-D-Gal
-
capsular, polysaccharide produced by Aerobacter aerogenes, hydrolyses the galactosyl-alpha-1,3-D-galactose linkages only in the complex substrate, bringing about depolymerization, the enzyme is phage-induced and serves to degrade the capsular polysaccharide of the host
-
?
[D-Gal-(1-3)(D-GlcUA-(1-2))-alpha-D-Man-(1-3)-alpha-D-Gal]n + H2O
D-Gal-(1-3)(D-GlcUA-(1-2))-alpha-D-Man-(1-3)-alpha-D-Gal
-
capsular, polysaccharide produced by Aerobacter aerogenes, hydrolyses the galactosyl-alpha-1,3-D-galactose linkages only in the complex substrate, bringing about depolymerization, the enzyme is phage-induced and serves to degrade the capsular polysaccharide of the host
-
?
additional information
?
-
-
the enzyme interacts specifically with capsular polysaccharides of Acinetobacter baumannii B05
-
-
?
additional information
?
-
the enzymes have high specificity for the capsular serotypes K3 and K21
-
-
?
additional information
?
-
the enzymes have high specificity for the capsular serotypes K3 and K21
-
-
?
additional information
?
-
-
the enzymes have high specificity for the capsular serotypes K3 and K21
-
-
?
additional information
?
-
Klebsiella pneumoniae capsular serotype K2
-
virus K2 hydrolyses capsule of Aerobacter aerogenesis using glucane hydrolase splitting alpha1,3-bond between galactose residues
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Klebsiella pneumoniae capsule exopolysaccharides + H2O
?
-
-
-
?
[D-Gal-(1-3)(D-GlcUA-(1-2))-alpha-D-Man-(1-3)-alpha-D-Gal]n + H2O
D-Gal-(1-3)(D-GlcUA-(1-2))-alpha-D-Man-(1-3)-alpha-D-Gal
[D-Gal-(1-3)(D-GlcUA-(1-2))-alpha-D-Man-(1-3)-alpha-D-Gal]n + H2O
D-Gal-(1-3)(D-GlcUA-(1-2))-alpha-D-Man-(1-3)-alpha-D-Gal
-
capsular, polysaccharide produced by Aerobacter aerogenes, hydrolyses the galactosyl-alpha-1,3-D-galactose linkages only in the complex substrate, bringing about depolymerization, the enzyme is phage-induced and serves to degrade the capsular polysaccharide of the host
-
?
[D-Gal-(1-3)(D-GlcUA-(1-2))-alpha-D-Man-(1-3)-alpha-D-Gal]n + H2O
D-Gal-(1-3)(D-GlcUA-(1-2))-alpha-D-Man-(1-3)-alpha-D-Gal
-
capsular, polysaccharide produced by Aerobacter aerogenes, hydrolyses the galactosyl-alpha-1,3-D-galactose linkages only in the complex substrate, bringing about depolymerization, the enzyme is phage-induced and serves to degrade the capsular polysaccharide of the host
-
?
additional information
?
-
-
the enzyme interacts specifically with capsular polysaccharides of Acinetobacter baumannii B05
-
-
?
additional information
?
-
the enzymes have high specificity for the capsular serotypes K3 and K21
-
-
?
additional information
?
-
the enzymes have high specificity for the capsular serotypes K3 and K21
-
-
?
additional information
?
-
-
the enzymes have high specificity for the capsular serotypes K3 and K21
-
-
?
additional information
?
-
Klebsiella pneumoniae capsular serotype K2
-
virus K2 hydrolyses capsule of Aerobacter aerogenesis using glucane hydrolase splitting alpha1,3-bond between galactose residues
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Anthrax
Parenteral Administration of Capsule Depolymerase EnvD Prevents Lethal Inhalation Anthrax Infection.
Bacterial Infections
Orally administered P22 phage tailspike protein reduces salmonella colonization in chickens: prospects of a novel therapy against bacterial infections.
Escherichia coli Infections
Treatment of experimental Escherichia coli infection with recombinant bacteriophage-derived capsule depolymerase.
Foot-and-Mouth Disease
Converging antigenic structure of a recombinant viral peptide displayed on different frameworks of carrier proteins.
Infections
A new sialidase mechanism: Bacteriophage K1F endosialidase is an inverting glycosidase.
Infections
A Novel Tail-Associated O91-Specific Polysaccharide Depolymerase from Podophage Reveals Lytic Efficacy of Shiga Toxin-Producing E. coli.
Infections
Administration of Capsule-Selective Endosialidase E Minimises Up-Regulation of Organ Gene Expression Induced by Experimental Systemic Infection with Escherichia coli K1.
Infections
Carbohydrate binding of Salmonella phage P22 tailspike protein and its role during host cell infection.
Infections
Characterization of bacteriophage P22 tailspike mutant proteins with altered endorhamnosidase and capsid assembly activities.
Infections
Corrigendum: The Capsule Depolymerase Dpo48 Rescues Galleria mellonella and Mice From Acinetobacter baumannii Systemic Infections.
Infections
Differential expression of the polysialyl capsule during blood-to-brain transit of neuropathogenic Escherichia coli K1.
Infections
Genomic Characterization of Intron-containing T7-like Phage phiL7 of Xanthomonas campestris.
Infections
Identification of Capsular Types in Carbapenem-Resistant Klebsiella pneumoniae Strains by wzc Sequencing and Implications for Capsule Depolymerase Treatment.
Infections
Parenteral Administration of Capsule Depolymerase EnvD Prevents Lethal Inhalation Anthrax Infection.
Infections
Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 A, fully refined structure of the endorhamnosidase at 1.56 A resolution, and the molecular basis of O-antigen recognition and cleavage.
Infections
Stimulation of clover root hair infection by lectin-binding oligosaccharides from the capsular and extracellular polysaccharides of Rhizobium trifolii.
Infections
The Capsule Depolymerase Dpo48 Rescues Galleria mellonella and Mice From Acinetobacter baumannii Systemic Infections.
Infections
Treatment of experimental Escherichia coli infection with recombinant bacteriophage-derived capsule depolymerase.
Infections
Unravelling the Links between Phage Adsorption and Successful Infection in Clostridium difficile.
Influenza, Human
Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors.
Pneumonia
Depolymerase improves gentamicin efficacy during Klebsiella pneumoniae induced murine infection.
Sepsis
Depolymerase improves gentamicin efficacy during Klebsiella pneumoniae induced murine infection.
Sepsis
K2 Capsule Depolymerase Is Highly Stable, Is Refractory to Resistance, and Protects Larvae and Mice from Acinetobacter baumannii Sepsis.
Sepsis
The Capsule Depolymerase Dpo48 Rescues Galleria mellonella and Mice From Acinetobacter baumannii Systemic Infections.
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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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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 7
about 50% activity at pH 3.0, highest activity (about 98%) between pH 4.0 and 7.0, about 10% activity at pH 8.0, completely inactive at pH 9.0
5 - 9
the enzyme maintains high activity at temperatures ranging from pH 5.0 to 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18 - 50
20 - 70
18 - 50
the enzyme maintains more than 95% of its activity between 18 and 45°C. At 50°C the enzyme activity drops to 16.7%
18 - 50
the enzyme maintains more than 95% of its activity between 18 and 45°C. At 50°C, the enzyme displays more than 90% of its activity
20 - 70
the enzyme maintains high activity at temperatures ranging from 20 to 70°C. The enzymatic activity diminishes at 80°C
20 - 70
highest activity between 20 and 37°C, 95% activity at 45°C, 70% activity at 56-62°C, less than 60% activity at 70°C, completely inactive at 80°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
Escherichia phage K1
-
the enzyme actively degrades K1 capsule polysaccharide in vitro and sensitizes K1 bacteria to serum killing
physiological function
the enzyme decreases Klebsiella pneumoniae resistance to innate defense mechanisms and strongly affects the virulence of Klebsiella pneumoniae with the corresponding K3 and K21 capsular serotypes. The enzyme considerably increases the lifespan of Galleria mellonella larvae infected with Klebsiella pneumoniae in a time- and strain-dependent manner
physiological function
the enzyme degrades the bacterial surface exopolysaccharides of Actinetobacter baumannii types 208, 238, 420 and 1106
physiological function
the enzyme is able to infect and grow on either capsular types K30/K69 and K5 or K8 and K5 of Klebsiella strains. Bacterial killing is observed when incubated Klebsiella strains with phages but not with purified enzymes
physiological function
the enzyme is able to infect and grow on either capsular types K30/K69 and K5 or K8 and K5 of Klebsiella strains. Bacterial killing is observed when incubated Klebsiella strains with phages but not with purified enzymes
physiological function
the enzyme significantly inhibits Klebsiella-induced mortality of Galleria mellonella larvae in a time-dependent manner. The enzyme does not affect the action of antibiotics against Klebsiella pneumoniae strains
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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). K9L8R4_9CAUD
988
0
106889
TrEMBL
Mitochondrion (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36400
63200
36400
-
octamer: 4 * 63200 + 4 * 36400 or heptamer: 4 * 63200 + 3 * 36400, SDS-PAGE
36400
-
heptamer: 4 * 63200 + 3 * 36400 or octamer: 4 * 63200 + 4 * 36400, SDS-PAGE
63200
-
octamer: 4 * 63200 + 4 * 36400 or heptamer: 4 * 63200 + 3 * 36400, SDS-PAGE
63200
-
heptamer: 4 * 63200 + 3 * 36400 or octamer: 4 * 63200 + 4 * 36400, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heptamer
-
heptamer: 4 * 63200 + 3 * 36400 or octamer: 4 * 63200 + 4 * 36400, SDS-PAGE
octamer
-
octamer: 4 * 63200 + 4 * 36400 or heptamer: 4 * 63200 + 3 * 36400, SDS-PAGE
trimer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 7
the enzyme remains active from pH 4.0-7.0 with relative activities ranging from 97.1-97.8% after a 30 min incubation. The activity diminishes substantially as the pH is lowered below 4.0 or raised above 7.0, to 54.6% and 14.0% of initial activity, respectively
752325
6
after an incubation for 1 h under acidic conditions (pH 6.0 and below), less than 30% of the original activity is preserved
750649
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 65
the enzyme shows 100% and 77.6% activity after 1 h at 37°C and 45°C, respectively. The enzyme is completely inactive after 30 and 10 min at 56°C and 65°C, respectively . The melting temperature is 65°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is not resistant against denaturation by SDS at room temperature and against digestion by trypsin
the enzyme is resistant against denaturation by SDS at room temperature and against digestion by trypsin
the enzyme is susceptible to SDS denaturation and proteolytic cleavage
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisPur Ni-NTA resin column chromatography
Ni-NTA column chromatography
Ni-NTA column chromatography and Superdex S200 gel filtration
Ni-NTA His-Bind resin column chromatography and Superdex S200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yurewicz, E.C.; Ghalambor, M.A.; Heath, E.C.
The structure of Aerobacter aerogenes capsular polysaccharide
J. Biol. Chem.
246
5596-5606
1971
Klebsiella aerogenes
brenda
Yurewicz, E.C.; Ghalambor, M.A.; Duckworth, D.H.; Heath, E.C.
Catalytic and molecular properties of a phage-induced capsular polysaccharide depolymerase
J. Biol. Chem.
246
5607-5616
1971
Klebsiella aerogenes
brenda
Hsu, C.R.; Lin, T.L.; Pan, Y.J.; Hsieh, P.F.; Wang, J.T.
Isolation of a bacteriophage specific for a new capsular type of Klebsiella pneumoniae and characterization of its polysaccharide depolymerase
PLoS ONE
8
e70092
2013
Klebsiella pneumoniae capsular serotype K2
brenda
Popova, A.V.; Shneider, M.M.; Myakinina, V.P.; Bannov, V.A.; Edelstein, M.V.; Rubalskii, E.O.; Aleshkin, A.V.; Fursova, N.K.; Volozhantsev, N.V.
Characterization of myophage AM24 infecting Acinetobacter baumannii of the K9 capsular type
Arch. Virol.
164
1493-1497
2019
Acinetobacter phage AM24
brenda
Lin, H.; Paff, M.L.; Molineux, I.J.; Bull, J.J.
Therapeutic application of phage capsule depolymerases against K1, K5, and K30 capsulated E. coli in mice
Front. Microbiol.
8
2257
2017
Escherichia phage K1, Escherichia phage K30
brenda
Majkowska-Skrobek, G.; Latka, A.; Berisio, R.; Squeglia, F.; Maciejewska, B.; Briers, Y.; Drulis-Kawa, Z.
Phage-borne depolymerases decrease Klebsiella pneumoniae resistance to innate defense mechanisms
Front. Microbiol.
9
2517
2018
Klebsiella phage KP32 (D1L2X0), Klebsiella phage KP32 (D1L2X1), Klebsiella phage KP32
brenda
Liu, Y.; Mi, Z.; Mi, L.; Huang, Y.; Li, P.; Liu, H.; Yuan, X.; Niu, W.; Jiang, N.; Bai, C.; Gao, Z.
Identification and characterization of capsule depolymerase Dpo48 from Acinetobacter baumannii phage IME200
PeerJ
7
e6173
2019
Acinetobacter phage IME-200 (A0A0P0IJ73)
brenda
Hsieh, P.F.; Lin, H.H.; Lin, T.L.; Chen, Y.Y.; Wang, J.T.
Two T7-like bacteriophages, K5-2 and K5-4, each encodes two capsule depolymerases isolation and functional characterization
Sci. Rep.
7
4624
2017
Klebsiella phage K5-2 (A0A219YHC0), Klebsiella phage K5-4 (A0A219YHG0)
brenda
Majkowska-Skrobek, G.; Latka, A.; Berisio, R.; Maciejewska, B.; Squeglia, F.; Romano, M.; Lavigne, R.; Struve, C.; Drulis-Kawa, Z.
Capsule-targeting depolymerase, derived from Klebsiella KP36 phage, as a tool for the development of anti-virulent strategy
Viruses
8
E324
2016
Klebsiella phage KP36 (K9L8R4), Klebsiella phage KP36
brenda
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Release 2023.1 (January 2023)
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