Information on EC 3.4.23.52 - preflagellin peptidase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
3.4.23.52
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RECOMMENDED NAME
GeneOntology No.
preflagellin peptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleaves the signal peptide of 3 to 12 amino acids from the N-terminal of preflagellin, usually at Arg-Gly-/- or Lys-Gly-/-, to release flagellin.
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no activity in Methanococcus igneus
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Manually annotated by BRENDA team
no activity in Methanoculleus marisnigri
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Manually annotated by BRENDA team
no activity in Methanogenium cariaci
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
DUF361-containing proteins + H2O
?
show the reaction diagram
EppA specifically cleaves proteins with DUF361-like domains
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?
FlaB2 + H2O
?
show the reaction diagram
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cosynthesis of of FlaK with its full-length substrate, FlaB2, leads to complete cleavage of the substrate signal peptides
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?
FlaB2 protein + H2O
?
show the reaction diagram
MEFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MEFMSNKKG + ASGIGTLIVFIAMVLVAAV
show the reaction diagram
MFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MFMSNKKG + ASGIGTLIVFIAMVLVAAV
show the reaction diagram
MKEFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MKEFMSNKKG + ASGIGTLIVFIAMVLVAAV
show the reaction diagram
MKGASGIGTLIVFIAMVLVAAV + H2O
MKG + ASGIGTLIVFIAMVLVAAV
show the reaction diagram
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-
-
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?
MKKGASGIGTLIVFIAMVLVAAV + H2O
MKKG + ASGIGTLIVFIAMVLVAAV
show the reaction diagram
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-
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?
MMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MMSNKKG + ASGIGTLIVFIAMVLVAAV
show the reaction diagram
MNKKGASGIGTLIVFIAMVLVAAV + H2O
MNKKG + ASGIGTLIVFIAMVLVAAV
show the reaction diagram
MSNKKGASGIGTLIVFIAMVLVAAV + H2O
MSNKKG + ASGIGTLIVFIAMVLVAAV
show the reaction diagram
pre-glucose-binding protein + H2O
glucose-binding protein + ?
show the reaction diagram
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?
precursor of flagellin + H2O
flagellin + ?
show the reaction diagram
precursor of glucose-binding protein + H2O
glucose-binding protein + ?
show the reaction diagram
preflagellin + H2O
flagellin + ?
show the reaction diagram
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most efficient substrate
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?
preflagellin FlaB1 + H2O
flagellin FlaB1 + ?
show the reaction diagram
preflagellin FlaB2 + H2O
flagellin + ?
show the reaction diagram
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?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
show the reaction diagram
preflagellin FlaB2 + H2O
MKIKEFMSNKKG + flagellin
show the reaction diagram
prepilin AapA + H2O
?
show the reaction diagram
additional information
?
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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
FlaB2 + H2O
?
show the reaction diagram
Q8NKW5
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cosynthesis of of FlaK with its full-length substrate, FlaB2, leads to complete cleavage of the substrate signal peptides
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?
FlaB2 protein + H2O
?
show the reaction diagram
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?
precursor of flagellin + H2O
flagellin + ?
show the reaction diagram
Q6IFS8
the enzyme is responsible for processing of precursor of flagellin
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?
precursor of glucose-binding protein + H2O
glucose-binding protein + ?
show the reaction diagram
Q6IFS8
the enzyme is responsible for the processing of precursor of glucose-binding protein
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
PilD is a zinc-binding protein. Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
wild type enzyme is not affected by 1,2-ethanedithiol dimethanesulfonate and dithiothreitol
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25900
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x * 25900, calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 30% (w/v) PEG 300, 50 mM glycine (pH 9.5) and 100 mM NaCl
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Triton X-100
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crude membrane fraction
metal-affinity column chromatography and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a His-tagged version expressed in Escherichia coli; expressed in an Methanococcus maripaludis DELTAflaK strain and in Escherichia coli
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expressed in an Methanococcus maripaludis DELTAflaK strain
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expressed in BL21(DE3)/pLysS membranes
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expressed in Escherichia coli K113 cell membranes
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expressed in Escherichia coli Rosetta 2 (DE3) cells
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E25C/I206C
the mutant is proteolytically active
D186A
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the mutation does not affect the activity towards preflagellin FlaB2
D18A
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inactive
D18E
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the mutation results in an apparently unstable protein
D18N
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inactive
D190A
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the mutation does not affect the activity towards preflagellin FlaB2
D224A
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the mutation does not affect the activity towards preflagellin FlaB2
D79A
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inactive
D79E
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the mutant restores preflagellin peptidase activity (despite a reduced amount of peptidase produced)
D79N
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inactive
D186A
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the mutation does not affect the activity towards preflagellin FlaB2
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D18A
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inactive
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D190A
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the mutation does not affect the activity towards preflagellin FlaB2
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D79A
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inactive
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D79N
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inactive
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A77E
mutant enzyme shows no processing of prepillin AapA
A77G
activity level is comparable to that of the wild type enzyme under standard assay conditions
A77P
activity level is comparable to that of the wild type enzyme under standard assay conditions; cleavage activity is reduced
D185A
activity of the mutant enzyme is lower than activity of wild-type enzyme
D186A
activity level is comparable to that of the wild type enzyme under standard assay conditions
D21A
mutant enzyme shows no processing of prepillin AapA
D78A
mutant enzyme shows no processing of prepillin AapA
G75E
mutant enzyme shows no processing of prepillin AapA
I22E
activity level is comparable to that of the wild type enzyme under standard assay conditions
K23A
activity level is comparable to that of the wild type enzyme under standard assay conditions
K24A
activity level is comparable to that of the wild type enzyme under standard assay conditions
L81A
activity level is comparable to that of the wild type enzyme under standard assay conditions
R25A
single mutant displays Aap pili even though no preopillin AapA-processing is observed
W32A
mutation results in reduced activity
D186A
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activity level is comparable to that of the wild type enzyme under standard assay conditions
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D21A
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mutant enzyme shows no processing of prepillin AapA
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D78A
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mutant enzyme shows no processing of prepillin AapA
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L81A
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activity level is comparable to that of the wild type enzyme under standard assay conditions
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R25A
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single mutant displays Aap pili even though no preopillin AapA-processing is observed
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D157A
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the activity level of the mutant is comparable to that of the wild type enzyme
D173A
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the activity level of the mutant is comparable to that of the wild type enzyme
D180A
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the activity level of the mutant is comparable to that of the wild type enzyme
D187A
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the mutant shows an apparent reduction in activity
D187A/D188A
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the mutant does not cleave preflagellin
D188A
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the mutant shows about wild type activity
D207N
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the activity level of the mutant is comparable to that of the wild type enzyme
D23A
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the mutant does not cleave preflagellin
D30A
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the activity level of the mutant is comparable to that of the wild type enzyme
D80A
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the mutant does not cleave preflagellin
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
scaled-up synthesis of PilD, followed by solubilization in dodecyl-beta-D-maltoside and chromatography, leads to a pure enzyme that retains its known biochemical activities