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Information on EC 3.4.24.B2 - oligoendopeptidase F
for references in articles please use BRENDA:EC3.4.24.B2
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preliminary BRENDA-supplied EC number
EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.24 Metalloendopeptidases
3.4.24.B2 oligoendopeptidase F
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 3.4.24.B2
-
pepfs
-
lactococcus
- aminopeptidase
- lactis
- proteinases
- carboxypeptidase
- swine
- amyloliquefaciens
- feather
- hyopneumoniae
-
sporulation
- metallopeptidase
-
mycoplasma
- endopeptidases
- methane
showSynonyms
pepf2, pepf1, gt-sm3b, alkaline endopeptidase, oligoendopeptidase f, pepfba, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GT-SM3B
M03.007
oligopeptidase F
PepF
PepFBa
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
proteolytic cleavage of proteins at Leu-Gly
cleavage of Gly-/-Xaa, enzyme often cleaves Phe-/-Xaa, with X being hydrophilic or basic, and with proline in position P'2 of the cleaved bond, no cleavage of bonds involving acidic residues
proteolytic cleavage of proteins at Leu-Gly
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
110639-28-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl) + H2O
?
-
Substrates: -
Products: -
Products: -
?
adrenocorticotropic hormone fragment 1-10 + H2O
SYSMEHF + RWG
Substrates: -
Products: -
Products: -
?
adrenocorticotropic hormone fragment 1-14 + H2O
SYSMEHF + RWG + KPVG
Substrates: -
Products: -
Products: -
?
adrenocorticotropic hormone fragment 1-17 + H2O
SYSMEHF + RWG + KPV + GKKR
Substrates: -
Products: -
Products: -
?
adrenocorticotropic hormone fragment 4-10 + H2O
MEHF + RWG
Substrates: -
Products: -
Products: -
?
bradykinin + H2O
?
-
Substrates: best substrate among peptides
Products: -
Products: -
?
bradykinin + H2O
RPPGF + SPR
Substrates: best substrate
Products: -
Products: -
?
insulin chain B fragment 22-30 + H2O
RGFF + Tyr + TPKA
Substrates: -
Products: -
Products: -
?
substance P fragment 2-11 + H2O
PKPQQ + Phe + Phe + GLM-NH2
Substrates: -
Products: -
Products: -
?
4-phenylazobenzyloxycarbonyl-L-Pro-Leu-Gly-L-Pro-D-Arg + H2O
?
Substrates: -
Products: -
Products: -
?
4-phenylazobenzyloxycarbonyl-L-Pro-Leu-Gly-L-Pro-D-Arg + H2O
?
Substrates: -
Products: -
Products: -
?
carbobenzoxy-Gly-Pro-Gly-Gly-Pro-Ala + H2O
?
Substrates: -
Products: -
Products: -
?
carbobenzoxy-Gly-Pro-Gly-Gly-Pro-Ala + H2O
?
Geobacillus thermoleovorans DSM 15325
Substrates: -
Products: -
Products: -
?
N-(3-(2-furyl)acryloyl)-Leu-Gly-Pro-Ala + H2O
?
Substrates: -
Products: -
Products: -
?
N-(3-(2-furyl)acryloyl)-Leu-Gly-Pro-Ala + H2O
?
Substrates: -
Products: -
Products: -
?
N-carboxylbenzoyl-Gly-Pro-Leu-Gly-Pro + H2O
?
Substrates: -
Products: -
Products: -
?
N-carboxylbenzoyl-Gly-Pro-Leu-Gly-Pro + H2O
?
Substrates: -
Products: -
Products: -
?
protein + H2O
peptides
-
Substrates: enzyme is not essential for growth or development
Products: -
Products: -
?
protein + H2O
peptides
-
Substrates: enzyme is not essential for growth or development
Products: -
Products: -
?
protein + H2O
peptides
Substrates: wide pH-dependent substrate specificity, cleaves peptides of length between 7 and 17 amino acids
Products: -
Products: -
?
additional information
?
-
Substrates: no hydrolytic activities on bradykinin residues 1 to 5
Products: -
Products: -
?
additional information
?
-
Substrates: no hydrolytic activities on bradykinin residues 1 to 5
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrolytic activities on bradykinin residues 1 to 5
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme shows hydrolytic activity against short-chain collagenous peptides, gelatin-derived oligopeptides, type I collagen-derived oligopeptides, and raw collagen extract oligopeptides
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows hydrolytic activity against short-chain collagenous peptides, gelatin-derived oligopeptides, type I collagen-derived oligopeptides, and raw collagen extract oligopeptides
Products: -
Products: -
?
additional information
?
-
Geobacillus thermoleovorans DSM 15325
Substrates: the enzyme shows hydrolytic activity against short-chain collagenous peptides, gelatin-derived oligopeptides, type I collagen-derived oligopeptides, and raw collagen extract oligopeptides
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with bradykinin fragment 2-10, Lys-p-nitroanilide, Gly-Pro-p-nitroanilide, adrenocorticotropic hormone fragment 1-4 SYSM and fragment 1-24, PQFY, Cbz-GPLGP, leucin enkephalin YGGFL, glucagon, full length insulin chain B, caseins
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
protein + H2O
peptides
-
Substrates: enzyme is not essential for growth or development
Products: -
Products: -
?
protein + H2O
peptides
-
Substrates: enzyme is not essential for growth or development
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Zn2+
additional information
Zn2+
zinc-binding motif, molar ratio of 1.87 Zn2+ to PepFBa
Zn2+
the enzyme contains a conservative zinc metallopeptidase motif, His400-Glu401-X-XHis404
additional information
no effect by 1 mM K+ and 1-5 mM Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
not inhibited by E-64, iodoacetamide, phosphoramidon and pehylmethylsulfonyl fluoride
-
EDTA
strongly inhibits at 10 mM, inhibition can by restored by Ca2+, Mg2+ and Co2+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00217
Carbobenzoxy-Gly-Pro-Gly-Gly-Pro-Ala
pH 7.3, 40°C, recombinant wild-type enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.99
Carbobenzoxy-Gly-Pro-Gly-Gly-Pro-Ala
pH 7.3, 40°C, recombinant wild-type enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20.7
with N-(3-(2-furyl)acryloyl)-Leu-Gly-Pro-Ala as substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
formerly Geobacillus lituanicus DSM 15325, gene GT-SM3B
UniProt
brenda
Geobacillus thermoleovorans DSM 15325
formerly Geobacillus lituanicus DSM 15325, gene GT-SM3B
UniProt
brenda
subsp. cremoris, i.e. Streptococcus cremoris, located on natural 55kb lactose-protease plasmid
SwissProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme sequence contains a 23-residue signal peptide
-
brenda
Geobacillus thermoleovorans DSM 15325
-
the enzyme sequence contains a 23-residue signal peptide
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
evolution
the enzyme belongs to the M3B subfamily of metallopeptidases and displays the highest amino acid sequence identity (40.3%) to the oligopeptidase PepFBa from mesophilic Bacillus amyloliquefaciens 23-7A among the characterized oligopeptidases
evolution
-
enzyme PepF is a metallopeptidase belonging to the M3 family
evolution
Geobacillus thermoleovorans DSM 15325
-
the enzyme belongs to the M3B subfamily of metallopeptidases and displays the highest amino acid sequence identity (40.3%) to the oligopeptidase PepFBa from mesophilic Bacillus amyloliquefaciens 23-7A among the characterized oligopeptidases
-
evolution
-
enzyme PepF is a metallopeptidase belonging to the M3 family
-
malfunction
-
the mutant strain TM90, in which gene pepF, encoding oligopeptidase F, is disturbed, shows significant upregulation of biofilm formation compared to the parental strain. The TM90 colony phenotype is smaller, more transparent, and splendent. The adhesive ability of TM90 to HEP-G2 cells is significantly increased compared with the parental strain. Fifty percent lethal dose (LD50) determinations in zebrafish demonstrats that the enhanced-biofilm mutant TM90 is highly attenuated relative to the wild-type strain
malfunction
-
the mutant strain TM90, in which gene pepF, encoding oligopeptidase F, is disturbed, shows significant upregulation of biofilm formation compared to the parental strain. The TM90 colony phenotype is smaller, more transparent, and splendent. The adhesive ability of TM90 to HEP-G2 cells is significantly increased compared with the parental strain. Fifty percent lethal dose (LD50) determinations in zebrafish demonstrats that the enhanced-biofilm mutant TM90 is highly attenuated relative to the wild-type strain
-
physiological function
-
Aeromonas hydrophila oligopeptidase F, encoded by gene pepF, is negatively involved in biofilm formation. Enzyme PepF might contribute to Aeromonas hydrophila virulence
physiological function
-
Aeromonas hydrophila oligopeptidase F, encoded by gene pepF, is negatively involved in biofilm formation. Enzyme PepF might contribute to Aeromonas hydrophila virulence
-
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
67700
2 * 67700, enzyme without signal peptide, SDS-PAGE, 2 * 70200, enzyme with signal peptide, SDS-PAGE
70000
70200
2 * 67700, enzyme without signal peptide, SDS-PAGE, 2 * 70200, enzyme with signal peptide, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
additional information
homodimer
2 * 67700, enzyme without signal peptide, SDS-PAGE, 2 * 70200, enzyme with signal peptide, SDS-PAGE
homodimer
Geobacillus thermoleovorans DSM 15325
-
2 * 67700, enzyme without signal peptide, SDS-PAGE, 2 * 70200, enzyme with signal peptide, SDS-PAGE
-
additional information
both the homodimer and monomer are catalytically active
additional information
-
both the homodimer and monomer are catalytically active
additional information
Geobacillus thermoleovorans DSM 15325
-
both the homodimer and monomer are catalytically active
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
identification of the TM90 mutant strain with defective pepF, phenotype, overview
additional information
-
identification of the TM90 mutant strain with defective pepF, phenotype, overview
-
additional information
-
disruption of the gene by insertion leads to 70% reduction of activity, but does not produce any growth defects
additional information
-
disruption of the gene by insertion leads to 70% reduction of activity, but does not produce any growth defects
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
recombinant enzyme, stable at with over 60% of maximal activity
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
stable for 1 h, thermally inactive at temperatures over 55°C
60
purified recombinant enzyme, 71% activity remaining after 1 h
70
purified recombinant enzyme, 30% activity remaining after 1 h
80
purified recombinant enzyme, no activity remaining after 1 h
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant secreted enzyme from Escherichia coli strain BL21 (DE3) culture medium by dialysis, anion exchange and cation exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene GT-SM3B, DNA and amino acid sequence determination and analysis, sequence comparisons, expression of the soluble enzyme with introduced N-terminal hexahistidine thrombin-cleavable tag in Escherichia coli strain BL21 (DE3) cytoplasm and secretion of the enzyme
gene pepF, DNA sequence determination and analysis, 2 putative promotor regions, operon expression is independent of the transcription regulator CtrA
-
screening of a EZ-Tn5 transposon random mutant library and cloning of gene pepF, DNA and amino acid sequence determination and analysis, real-time quantitative PCR expression analysis
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
PepFBa can facilitate sporulation by processing a pro-Phr into active pentapeptides
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
additional information
-
PepFBa can facilitate sporulation by processing a pro-Phr into active pentapeptides
-
additional information
-
overexpression in Bacillus subtilis inhibits sporulation initiation
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Braz, V.S.; Lang, E.A.S.; Marques, M.V.
Cloning and characterization of the gene encoding the PepF endopeptidase from the aquatic bacterium Caulobacter crescentus
Braz. J. Microbiol.
33
84-91
2002
Caulobacter vibrioides, Caulobacter vibrioides LS2195
-
brenda
Monnet, V.; Nardi, M.; Chopin, A.; Chopin, M.C.; Gripon, J.C.
Biochemical and genetic characterization of PepF, an oligopeptidase from Lactococcus lactis
J. Biol. Chem.
269
32070-32076
1994
Lactococcus lactis (P54124)
brenda
Chao, S.H.; Cheng, T.H.; Shaw, C.Y.; Lee, M.H.; Hsu, Y.H.; Tsai, Y.C.
Characterization of a novel PepF-like oligopeptidase secreted by Bacillus amyloliquefaciens 23-7A
Appl. Environ. Microbiol.
72
968-971
2006
Bacillus amyloliquefaciens (Q71E77), Bacillus amyloliquefaciens 23-7A (Q71E77), Bacillus amyloliquefaciens 23-7A
brenda
Monnet, V.
Oligopeptidase F
Handbook of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
369-370
2004
Chlamydia muridarum, Chlamydia pneumoniae, Chlamydia trachomatis, Clostridium perfringens, Deinococcus radiodurans, Fusobacterium nucleatum, Halobacterium sp., Listeria innocua, Listeria monocytogenes, Mycoplasma capricolum, Lactococcus lactis, Mycoplasmoides genitalium, Mycoplasmoides pneumoniae, Mycoplasmopsis pulmonis, Oceanobacillus iheyensis, Staphylococcus aureus, Staphylococcus epidermidis, Streptococcus agalactiae, Streptococcus mutans, Streptococcus pneumoniae, Streptococcus pyogenes, Streptococcus thermophilus, Caldanaerobacter subterraneus subsp. tengcongensis, Ureaplasma urealyticum, Bacillus anthracis, Halalkalibacterium halodurans, Bacillus licheniformis, Bacillus subtilis, Borreliella burgdorferi, Caldicellulosiruptor saccharolyticus, Halobacterium sp. NRC-1
-
brenda
Jasilionis, A.; Kuisiene, N.
Characterization of the novel thermostable oligopeptidase from Geobacillus thermoleovorans DSM 15325
J. Microbiol. Biotechnol.
25
1070-1083
2015
Geobacillus thermoleovorans (W5RWH8), Geobacillus thermoleovorans, Geobacillus thermoleovorans DSM 15325 (W5RWH8)
brenda
Du, H.; Pang, M.; Dong, Y.; Wu, Y.; Wang, N.; Liu, J.; Awan, F.; Lu, C.; Liu, Y.
Identification and characterization of an Aeromonas hydrophila oligopeptidase gene pepF negatively related to biofilm formation
Front. Microbiol.
7
1497
2016
Aeromonas hydrophila, Aeromonas hydrophila NJ-35
brenda
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