Information on EC 3.4.23.36 - Signal peptidase II

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.23.36
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RECOMMENDED NAME
GeneOntology No.
Signal peptidase II
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Release of signal peptides from bacterial membrane prolipoproteins including murein prolipoprotein. Hydrolyses -Xaa-Yaa-Zaa-/-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral sidechains
show the reaction diagram
Xaa is hydrophobic (preferably Leu) and Xbb (Ala or Ser) and Xcc (Gly or Ala) have small, neutral side chains, release of signal peptides from bacterial membrane prolipoproteins including murein prolipoprotein
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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aspartic endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY hide
171715-14-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain SK36
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-
Manually annotated by BRENDA team
strain SK36
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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
bacterial lipoprotein + H2O
?
show the reaction diagram
Braun's polylipoprotein + H2O
?
show the reaction diagram
Glyceride-containing precursor of new lipoprotein + H2O
?
show the reaction diagram
-
-
-
-
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Glyceride-containing precursor of the major outer membrane lipoprotein + H2O
?
show the reaction diagram
-
-
-
-
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Glyceride-containing precursor of the peptidoglycan-associated lipoprotein + H2O
?
show the reaction diagram
-
-
-
-
-
Murein prolipoprotein + H2O
?
show the reaction diagram
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cleavage of Gly-diacylglyceryl-cysteine bond, also cleavage of this bond in the majority of other lipoprotein precursors, some prolipoproteins contain Ala-diacylglyceryl-cysteine, or Ser-diacylglyceryl-cysteine cleavage sites
-
-
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pre-PrsA + H2O
PrsA protein + ?
show the reaction diagram
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-
-
?
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
bacterial lipoprotein + H2O
?
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
chymostatin
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Globomycin
lauroyl sarcoside
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Myxobacteria antibiotic TA
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TA inhibits pro-lipoprotein processing in whole cells, similar to globomycin, thus preventing outer membrane localization of lipoproteins LpoA and LpoB and blocking their essential interactions with PBP1A and PBP1B
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octylglucoside
Pepstatin
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Phenylethyl alcohol
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phenylmethylsulfonyl fluoride
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tosyl arginyl methyl ester
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tosyl-Arg methyl ester
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Detergent
-
additional information
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no requirement for phospholipid
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
prolipoprotein
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000036
Globomycin
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.9
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crude enzyme
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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37C: activity maximum, active even at 80C
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17400
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calculated from amino acid sequence
18000
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x * 18144, amino acid sequence calculation, x * 18000, SDS-PAGE
18140
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E. coli, calculation from nucleotide sequence
18144
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x * 18144, amino acid sequence calculation, x * 18000, SDS-PAGE
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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N-terminal Cys modification with diacylglyceryl before cleavage of the signal peptide to the mature enzyme
additional information
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N-terminal Cys modification with diacylglyceryl before cleavage of the signal peptide to the mature enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
in presence of 2% Triton X-100 enzyme can withstand brief exposure up to
80
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purified enzyme, stable for a short time
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Unstable during purification unless 10% glycerol, 1% Triton X-100, and 1 mM DTT are included in the buffers
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C or -20C, 10% glycerol, 1% Triton X-100, and 1 mM DTT, stable for at least 1 month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from inner membrane to homogeneity by solubilization from membrane with Triton X-100, heat treatmemt at 65C and pH 4.0, anion exchange chromatography, and chromatofocusing, 35000fold, recombinant enzyme by ammonium sulfate fractionation, anion exchange chromatography in presence of EDTA, and gel filtration to homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
enzyme overexpression in Escherichia coli confers high resistance to globomycin
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expressed in Escherichia coli DH5alpha cells
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expression of Sp0928 protects Escherichia coli against the Lsp antagonist globomycin
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gene lsp, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli under control of the trp promoter
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ORF Rv1539, gene lspA, from strain H37Rv, DNA and amino acid sequence determination and analysis
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overexpression of Rickettsia typhi lspA in Escherichia coli confers increased globomycin resistance. Recombinant lspA from significantly restores the growth of temperature-sensitive Escherichia coli Y815 at the nonpermissive temperature, supporting its biological activity as SPase II in prolipoprotein processing
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wild-type lsp gene amplified by PCR, cloned into pGDL48 and used to transform Bacillus subtilis 8G5lsp, lacking the lsp gene
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A128V
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site-directed mutagenesis
D102A
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site-directed mutagenesis
D111A
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site-directed mutagenesis
D129A
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site-directed mutagenesis
D14A
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site-directed mutagenesis
F125A
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site-directed mutagenesis
F50A
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site-directed mutagenesis
G47A
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site-directed mutagenesis
G95A
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site-directed mutagenesis
K18A
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site-directed mutagenesis
N126A
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site-directed mutagenesis
N45A
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site-directed mutagenesis
N99A
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site-directed mutagenesis
R103A
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site-directed mutagenesis
V109A
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site-directed mutagenesis
W50A
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site-directed mutagenesis
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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important role of the enzyme in the pathogenicity of Legionella pneumophila, making it a promising target for therapeutic intervention
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