Information on EC 3.4.21.89 - Signal peptidase I

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.89
-
RECOMMENDED NAME
GeneOntology No.
Signal peptidase I
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of hydrophobic, N-terminal signal or leader sequences
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
65979-36-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain DSM 319, gene sipM
SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
strain MC1061
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Manually annotated by BRENDA team
strain MC1061/pRD8
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Manually annotated by BRENDA team
overproducing strain
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Manually annotated by BRENDA team
strain MHOM/IL/81, isolated from footpad lesions of infected BALB/c mice
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Manually annotated by BRENDA team
strain MHOM/IL/81, isolated from footpad lesions of infected BALB/c mice
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Manually annotated by BRENDA team
catalytic subunit SEC11
UniProt
Manually annotated by BRENDA team
putative signal peptidase
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-
Manually annotated by BRENDA team
strain PS
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
no activity in Mycoplasma genitalium
smallest genome of all known self-replicating organisms, lacks a gene with any recognizable similarity to the type I peptidase family
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Manually annotated by BRENDA team
pea
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
strain PA103-29
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Manually annotated by BRENDA team
frog
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
-
proper maturation of lumenal proteins may be a key process for correct assembly of thylakoids
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(NO2)YFSASALA-KI-(2-aminobenzoyl)K-NH2 + H2O
(NO2)YFSASALA + KI-(2-aminobenzoyl)K-NH2
show the reaction diagram
-
-
-
?
Ac-AGLIARAVTSGA-NH2 + H2O
Ac-AGLIAR + AVTSGA-NH2
show the reaction diagram
-
-
-
?
Ac-AGPRPTRIAFGA-NH2 + H2O
N-acetyl-L-alanine + GPRPTRIAFGA-NH2
show the reaction diagram
-
-
-
?
Ac-AGPTARAVTSGA-NH2 + H2O
Ac-AGPTARA + VTSGA-NH2
show the reaction diagram
-
-
-
?
Ac-AGSASALAKIGA-NH2 + H2O
Ac-AGSASALA + KIGA-NH2
show the reaction diagram
-
-
-
?
Ac-AGVPPLFAMLGA-NH2 + H2O
Ac-AGVPPLF + AMLGA-NH2
show the reaction diagram
-
-
-
?
Acetyl-Trp-Leu-Val-Pro-norleucine-Leu-Ser-Phe-Ala-Ala-Glu-Gly-Asp-Asp-Pro-Ala-NH2 + H2O
Acetyl-Trp-Leu-Val-Pro-norleucine-Leu-Ser-Phe-Ala + Ala-Glu-Gly-Asp-Asp-Pro-Ala-NH2
show the reaction diagram
-
-
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Acetyl-Trp-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile + H2O
?
show the reaction diagram
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Acetyl-Trp-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
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Ala-Ala-Phe-4-methylcoumaryl-7-amide + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
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?
alkaline phosphatase signal peptide
?
show the reaction diagram
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clear evidence of a weak peptide-enzyme complex formation. The peptide adopts a U-turn shape originating from the proline residues within the primary sequence that is stabilized by its interaction with the peptidase and leaves key residues of the cleavage region exposed for proteolysis. In dodecylphosphocholine micelles the signal peptide also adopts a U-turn shape comparable with that observed in association with the enzyme. In both environments this conformation is stabilized by the signal peptide phenylalanine side chain-interaction with enzyme or lipid mimetic. In the presence of dodecylphosphocholine, the N-terminal core region residues of the peptide adopt a helical motif and are buried within the membrane. This is consistent with proteolysis of the preprotein occurring while the signal peptide remains in the bilayer and the enzyme active site functions at the membrane surface
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?
alkaline phosphatase signal peptide fused to full-length mammalian cytochrome b5
cytochrome b5
show the reaction diagram
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amphipatic, chimeric cytochrome b5 precursor
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?
beta-lactam response sensor BlaR1 + H2O
?
show the reaction diagram
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presence of extracellular domains of beta-lactam response sensor BlaR1 in the medium is dependent on SPase activity, suggesting that it is cleaved at noncanonical sites within the protein
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?
Clostridium thermocellum cellulose-binding domain containing a signal peptide + H2O
signal peptide + Clostridium thermocellum cellulose-binding domain
show the reaction diagram
-
signal peptidase Sec11a and Sec11b cleave differentially
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?
complement component C1q + H2O
?
show the reaction diagram
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partially degraded
-
?
core protein of classical swine fever virus + H2O
?
show the reaction diagram
Cytochrome c2 of Rhodobacter sphaeroides + H2O
?
show the reaction diagram
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Dabcyl-AGHDAHASET(EDANS) + H2O
?
show the reaction diagram
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a substrate constructed based on the C-terminal region of the Staphylococcus epidermidis pre-SceD protein and containing the native SPase I cleavage site
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?
Dabcyl-VSPAAFAADL(EDANS) + H2O
?
show the reaction diagram
signal peptide of elastase
-
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?
decanoyl-LTPTAKAASKIDD-OH + H2O
decanoyl-LTPTAKA + ASKIDD
show the reaction diagram
envelope protein Toc75 precursor + H2O
mature envelope protein Toc75 + signal peptide
show the reaction diagram
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?
Eukaryotic initiation factor eIF-4gamma from rabbit reticulocytes + H2O
?
show the reaction diagram
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cleavage site Gly479-Arg480
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Fibrinogen + H2O
?
show the reaction diagram
FSASALAKI + H2O
FSASALA + Lys-Ile
show the reaction diagram
hepatitis C virus core protein + H2O
?
show the reaction diagram
hexanoyl-LTPTQAKAASKIDD-OH + H2O
hexanoyl-LTPTQAKA + ASKIDD
show the reaction diagram
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-
-
?
Hybrid protein pro-OmpA-nuclease A + H2O
?
show the reaction diagram
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IgG + H2O
?
show the reaction diagram
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partially degraded
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?
Immunoglobulin + H2O
?
show the reaction diagram
intermediate of cytochrome c peroxidase + H2O
mature cytochrome c peroxidase + peptide
show the reaction diagram
KLTFGTVKPVQAIAGYEWL + H2O
?
show the reaction diagram
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synthetic peptide substrate, based upon the signal peptide of prestreptokinase from Streptococcus pyogene
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?
lipoteichoic acid synthase + H2O
?
show the reaction diagram
M13 phage procoat protein + H2O
Free signal peptide + coat protein
show the reaction diagram
mammalian cytochrome b(5) precursor + H2O
?
show the reaction diagram
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the processing can occur after almost complete exocytoplasmic translocation of the preprotein is accomplished
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?
Methanococcus voltae S-layer protein + H2O
?
show the reaction diagram
mitochondrial inter membrane space protein IMS
?
show the reaction diagram
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mitochondrial inner membrane peptidase, complex specificity requirement, cleaves initially synthesized with a bipartite signal sequence that contains a matrix-targeting signal and an IMS sorting signal, specificity of Imp1p and Imp2p is not identical, precursors of the cytochrome oxidase subunit II pre-COXII and cytochrome b2 are processed exclusively by Imp1p, in contrast, the precursor form of cytochrome c1 is exclusively processed by Imp2p
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?
O-acetyltransferase + H2O
?
show the reaction diagram
octanoyl-LTPTQAKAASKIDD-OH + H2O
octanoyl-LTPTQAKA + ASKIDD
show the reaction diagram
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-
-
?
OE33 + H2O
?
show the reaction diagram
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-
-
?
p23 + H2O
p21 + ?
show the reaction diagram
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?
Parathyroid hormone + H2O
?
show the reaction diagram
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-
-
?
Phe-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile + H2O
?
show the reaction diagram
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Phe-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile + H2O
Phe-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile + ?
show the reaction diagram
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Phe-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile-NH2 + H2O
Phe-Ser-Ala-Ser-Ala-Leu-Ala + Lys-Ile-NH2
show the reaction diagram
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plasmin + H2O
?
show the reaction diagram
plasminogen + H2O
?
show the reaction diagram
-
-
-
?
Pre-beta-lactamase + H2O
beta-Lactamase + ?
show the reaction diagram
Pre-lambda phage receptor + H2O
Lambda Phage receptor + ?
show the reaction diagram
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pre-SceD protein + H2O
SceD + presequence of pre-SceD
show the reaction diagram
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substrate of Sip2 and Sip3
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?
Precursor of pea cytochrome f + H2O
Pea cytochrome f + ?
show the reaction diagram
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Precursor of the 23kd photosystem II protein + H2O
23kd Photosystem II protein + ?
show the reaction diagram
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Precursor of the leucine-binding protein + H2O
Leucine-binding protein + ?
show the reaction diagram
Precursors of the exported proteins Skp of E. coli + H2O
Exported proteins Skp of E. coli + ?
show the reaction diagram
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processed at the authentic site
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Premaltose-binding protein + H2O
Maltose-binding protein + ?
show the reaction diagram
preprotein substrate PONA + H2O
protein substrate PONA + ?
show the reaction diagram
Pro-OmpA + H2O
OmpA + ?
show the reaction diagram
pro-ompA-nuclease + H2O
ompA-nuclease + ?
show the reaction diagram
pro-rem + H2O
signal peptide + rem
show the reaction diagram
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Rev-like export protein encoded by mouse mammary tumor virus. Mutations at both glycosylation positions eliminate detectable rem glycosylation without effect on SP cleavage. Rem protein expression constructs with mutations at position -1, relative to the predicted cleavage site, i.e. G98R or both positions -1 and -3, V96R/G98R are not cleaved by SP-I
-
-
?
propolylipoprotein signal peptide + H2O
?
show the reaction diagram
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?
PsbO precursor protein + H2O
mature PcpO + signal peptide
show the reaction diagram
-
Zea mays oxygen-evolving enhancer protein 3-1, chloroplastic. Activity is reduced below 10% in Pbs mutant A83L
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-
?
signal peptidase I + H2O
SPase37-204
show the reaction diagram
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self-cleavage, results in a truncated product
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?
signal peptides from preproteins + H2O
mature proteins
show the reaction diagram
SpsB + H2O
?
show the reaction diagram
-
self-cleavage
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-
?
Staphylococcus epidermidis SceD preprotein + H2O
Staphylococcus epidermidis SceD protein + SceD protein prepeptide fragment
show the reaction diagram
-
specific cleavage at a single cleavage site located at the A-S bond
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-
?
streptokinase precursor + H2O
streptokinase
show the reaction diagram
synaptobrevin + H2O
?
show the reaction diagram
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tail-anchored integral membrane protein
-
?
Thylakoid lumen protein precursors + H2O
Thylakoid lumen protein + ?
show the reaction diagram
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Toc75 + H2O
?
show the reaction diagram
-
-
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?
tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
tosyl-Gly-Pro-Lys + p-nitroaniline
show the reaction diagram
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chromozym PL
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?
Val-Leu-Lys-p-nitroanilide + H2O
Val-Leu-Lys + p-nitroaniline
show the reaction diagram
VsiSP-mTNFalpha + H2O
?
show the reaction diagram
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?
YFSASALA-4-methylcoumarin-7-amide + H2O
YFSASALA + 7-amino-4-methylcoumarin
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
core protein of classical swine fever virus + H2O
?
show the reaction diagram
-
the processing of core protein of classical swine fever virus is conducted by signal peptide peptidase. Inhibition of this enzyme results in a reduced virus yield
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?
hepatitis C virus core protein + H2O
?
show the reaction diagram
-
signal peptide peptidase-catalyzed cleavage of hepatitis C virus core protein is dispensable for virus budding, but destabilizes the viral capsid
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-
?
intermediate of cytochrome c peroxidase + H2O
mature cytochrome c peroxidase + peptide
show the reaction diagram
-
Pcp1 is involved in processing of the intermediate of cytochrome c peroxidase
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?
pre-SceD protein + H2O
SceD + presequence of pre-SceD
show the reaction diagram
-
substrate of Sip2 and Sip3
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?
signal peptides from preproteins + H2O
mature proteins
show the reaction diagram
streptokinase precursor + H2O
streptokinase
show the reaction diagram
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3S)-3-((1R)-1-[(N-decanoyl-L-prolyl-L-threonyl-L-alanyl-L-asparaginyl)amino]ethyl)azetidin-2-one
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beta-lactam lipopeptide, 57% inhibition at 0.1 mM
(3S)-3-((1S)-1-[(N-decanoyl-L-prolyl-L-threonyl-L-alanyl-L-asparaginyl)amino]ethyl)azetidin-2-one
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beta-lactam lipopeptide, 47% inhibition at 0.1 mM
(5S,6S) penem
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beta-lactam inhibitor
(5S,6S)-6-[(R)-acetoxyethyl]-penem-3-carboxylate
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(NO2)YFSASALA
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product inhibition
(Z-LL)2-ketone
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completely abolishes signal peptide peptidase-catalysed maturation of p23 to p21 in the case of wild-type
1,3-bis[(N-benzyloxycarbonyl-L-leucyl-leucyl)amino]acetone
-
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1-(2,5-dichlorophenyl)-3-(dimethylamino)propan-1-one
overexpression of lepB reduces the susceptibility of Mycobacterium tuberculosis to 1-(2,5-dichlorophenyl)-3-(dimethylamino)propan-1-one, and downregulation results in increased susceptibility. Treatment with 1-(2,5-dichlorophenyl)-3-(dimethylamino)propan-1-one leads to a rapid loss of viability and cell lysis. The compound has increased potency in nonreplicating cells, causing a reduction in viable cell numbers below the detection limit after 24 h
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
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23 residue synthetic signal peptide of the M13 coat protein
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4-nitrobenzyl (5S,6S)-6-(1-hydroxyethyl)-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
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4-nitrobenzyl (5S,6S)-6-[(1R)-1-(acetyloxy)ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
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4-nitrobenzyl (5S,6S)-6-[(1R)-1-(butanoyloxy)ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
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4-nitrobenzyl (5S,6S)-6-[(1R)-1-(ethoxymethoxy)ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
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4-nitrobenzyl (5S,6S)-6-[(1R)-1-(methoxymethoxy)ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
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4-nitrobenzyl (5S,6S)-6-[(1R)-1-[(2-methylbutanoyl)oxy]ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
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4-nitrobenzyl (5S,6S)-6-[(1R)-1-[(2-methylpropanoyl)oxy]ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
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4-nitrobenzyl (5S,6S)-6-[(1R)-1-[(acetyloxy)methoxy]ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
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4-nitrobenzyl (5S,6S)-6-[(1R)-1-[(ethylcarbamoyl)oxy]ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
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4-nitrobenzyl (5S,6S)-6-[(1R)-1-[(N-acetylalanyl)oxy]ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
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4-nitrobenzyl (5S,6S)-6-[(1R)-1-[(N-acetylglycyl)oxy]ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
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4-nitrobenzyl (5S,6S)-6-[(1R)-1-[(N-acetylisoleucyl)oxy]ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
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4-nitrobenzyl (5S,6S)-6-[(1R)-1-[(N-acetylvalyl)oxy]ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
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4-nitrobenzyl (5S,6S)-7-oxo-6-[(1R)-1-(propanoyloxy)ethyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
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4-nitrobenzyl (5S,6S)-7-oxo-6-[(1R)-1-[(propan-2-ylcarbamoyl)oxy]ethyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
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5S penem derivative
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best inhibitor
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antipain
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arylomycin A-C16
arylomycin A2
arylomycin C16
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BAL0019193
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a morpholino-beta-sultam derivative, inhibits SPase I by binding to non-overlapping subsites near the catalytic center in a noncovalent manner, binding mode, overview
benzyl (2S,5R,6S)-6-[(N-decanoyl-L-prolyl-L-threonyl-L-alanyl-L-asparaginyl)amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]-heptane-2-carboxylate
-
beta-lactam lipopeptide, 36% inhibition at 0.1 mM
beta-Lactams
-
-
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beta-mercaptoethanol
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Bromosuccinimide
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inactivation by modification of tryptophan residues 300 and 310
Carboxyphenanthroline
-
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cholate
-
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decanoyl-AKAPSKIDD
-
complete inhibition at 0.2 mM
decanoyl-L-prolyl-L-threonyl-L-alanyl-L-asparaginyl-carboxamide
-
beta-lactam lipopeptide, 60% inhibition at 100 mM, removal of the beta-lactam moiety results in a loss of activity
decanoyl-LTPTA
-
susceptible to classic protease inhibition, SpsB can be inhibited with a P1' proline
decanoyl-LTPTAKAPS
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7.1% inhibition at 0.2 mM
deoxycholate
-
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diethyldicarbonate
-
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diisopropyl fluorophosphate
-
partial inhibition
dinitrophenol
dithiothreitol
EDTA
-
mitochondrial Imp1p
L685,458
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exerts only a slight effect on signal peptide peptidase-catalysed maturation of p23 to p21 in the case of wild-type, but it almost completely abolishes this process in the case of the Con1/C3/VLV replicon
lactacystin
-
proteasome inhibitor, presence in cells infected with mouse mammary tumor virus results in accumulation of uncleaved Rem relative to SP, consistent with SP retrotranslocation and proteasome escape before nuclear entry
Leader peptide of bacteriophage procoat
-
inhibits cleavage of M13 procoat or pre-maltose-binding protein
-
LTPTAKAPSKIDD
-
21.6% inhibition at 0.2 mM
MG132
-
proteasome inhibitor, presence in cells infected with mouse mammary tumor virus results in accumulation of uncleaved Rem relative to SP, consistent with SP retrotranslocation and proteasome escape before nuclear entry
Mg2+
-
above 1 mM
N-hexadecanoyl-N-methylserylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
N-methyl-N-(12-methyltridecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
N-methyl-N-(12-methyltridecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
N-methyl-N-(13-methyltetradecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
N-methyl-N-(14-methylpentadecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
N-methyl-N-(14-methylpentadecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
N-methyl-N-pentadecanoylserylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
N-methyl-N-tetradecanoylserylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
N-[(1S)-1-(chloroacetyl)-3-methylbutyl]-4-methylbenzenesulfonamide
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total loss of enzyme activity
N-[(2S)-4-[(2S)-1-decanoylpyrrolidin-2-yl]-2-(1-hydroxyethyl)-4-oxobutanoyl]-L-alanyl-N1-[(2S)-1-oxopropan-2-yl]-L-aspartamide
-
i.e. decanoyl-PTANA-aldehyde, inhibition by the synthetic substrate-based peptide aldehyde, overview. The length of the core lipopeptide can be reduced by removing several amino acids from both termini. Conversion of this peptide to an aldehyde. The signal peptide consists of three domains, a positively charged N-terminal domain, n-region, a hydrophobic middle domain, which contains usually 7-15 amino acids forming an alpha-helix, h-region, and a C-terminal domain, c-region, which is responsible for substrate recognition
Phenylglyoxal
-
-
phenylmethyl sulfonyl fluoride
-
partial inhibition
pre-protein including a proline at the +1 position
-
not cleaved, act as competitive inhibitors
-
Signal peptides that include a Pro residue at position +1
-
-
-
sodium chloride
-
above 160 mM
Synthetic leader peptide
-
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dodecylphosphocholine
-
at 37°C, degradation occurs to a lesser extent in dodecylphosphocholine micelles than in Triton X-100 or n-octyl-beta-D-glucopyranoside
-
n-octyl-beta-D-glucopyranoside
-
-
phosphatidylethanolamine
-
is required to maintain activity of the membrane-incorporated signal-peptidase (full-length signal peptidase I incoporated into phospholipid vesicles). Maximal activity is achieved at about 55% phosphatidylethanolamine
Phospholipids
Triton X-100
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
alkaline phosphatase signal peptide fused to full-length mammalian cytochrome b5
-
pH 7.5, 37°C
-
0.988
decanoyl-LT-P-TAKA-A-SKIDD-OH
-
pH 8.5, 37°C
0.029
decanoyl-LTPTAKAASKIDD-OH
-
pH 8.5, 37°C
0.43 - 0.8
FSASALAKI
0.33 - 0.52
Phe-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile
1
Phe-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile-NH2
-
-
0.0166 - 0.044
preprotein substrate PONA
-
0.0165
pro-ompA-nuclease
-
pH 8.0
-
0.0165 - 0.032
pro-OmpA-nuclease A
-
0.319
tosyl-Gly-Pro-Lys-p-nitroanilide
-
pH 10.0, 25°C
0.727
Val-Leu-Lys-p-nitroanilide
-
pH 10.0, 25°C
0.0006 - 0.11
Y-NO2-FSASALAKIK-2-aminobenzoyl-NH2
0.0328 - 0.0354
YFSASALA-4-methylcoumarin 7-amide
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 110
Ala-Ala-Phe-4-methylcoumaryl-7-amide
11
alkaline phosphatase signal peptide fused to full-length mammalian cytochrome b5
Escherichia coli
-
pH 7.5, 37°C
-
67 - 418
decanoyl-LTPTAKAASKIDD-OH
0.03
FSASALA-KI
Escherichia coli
-
pH 8.1, 37°C
0.037 - 1.44
FSASALAKI
0.0212 - 0.024
Phe-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile
0.033
Phe-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile-NH2
Escherichia coli
-
-
0.014 - 44
preprotein substrate PONA
-
0.04 - 8.73
pro-ompA-nuclease
-
3 - 8.73
pro-OmpA-nuclease A
-
0.001 - 1.5
Y-NO2-FSASALAKIK-2-aminobenzoyl-NH2
0.00028 - 0.000528
YFSASALA-4-methylcoumarin 7-amide
additional information
additional information
Escherichia coli
-
effect of the length of the polypeptide chain of substrates on the turnover number
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.059 - 1.85
SpsB
160399
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000158
N-hexadecanoyl-N-methylserylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
-
0.00005
N-methyl-N-(12-methyltridecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
-
0.00011
N-methyl-N-(12-methyltridecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
-
0.000058
N-methyl-N-(14-methylpentadecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004 - 0.001
arylomycin A2
0.00019
N-hexadecanoyl-N-methylserylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
Escherichia coli
-
IC50: 190 nM
0.00011
N-methyl-N-(12-methyltridecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
Escherichia coli
-
IC50: 110 nM
0.00011
N-methyl-N-(12-methyltridecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
Escherichia coli
-
IC50: 110 nM
0.00013
N-methyl-N-(13-methyltetradecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
Escherichia coli
-
IC50: 130 nM
0.00013
N-methyl-N-(14-methylpentadecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
Escherichia coli
-
IC50: 130 nM
0.00017
N-methyl-N-(14-methylpentadecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
Escherichia coli
-
IC50: 170 nM
0.00013
N-methyl-N-pentadecanoylserylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
Escherichia coli
-
IC50: 130 nM
0.00011
N-methyl-N-tetradecanoylserylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
Escherichia coli
-
IC50: 110 nM
0.00009
N-[(2S)-4-[(2S)-1-decanoylpyrrolidin-2-yl]-2-(1-hydroxyethyl)-4-oxobutanoyl]-L-alanyl-N1-[(2S)-1-oxopropan-2-yl]-L-aspartamide
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
additional information
additional information
Staphylococcus aureus
-
conversion of a substrate based peptide to an aldehyde results in a molecule with an IC(50) value of 0.09 micromol
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 9
-
maximal processing rates at pH 8.5 and above, 90% activity at neutral pH
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 11
-
activity increases from pH 4.0-9.0, 85% of maximal activity at pH 11.0, no activity above pH 12.0
4.5 - 9
-
20% of maximal activity at pH 4.5, half-maximal activity at pH 6.5, 90% of maximal activity at pH 7.0
5 - 12
-
activity range, inactive at or below pH 4.0 and at or above pH 13.0, profile, overview
7.7 - 10
-
7.7: 57% of activity maximum, 10: maximum activity
additional information
-
pH-rate profile reveals apparent pKa values of 6.6 and 8.7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 40
-
signal peptidase I
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.7
-
isoelectric focusing
9.72
calculated from sequence
9.77
calculated from sequence
10.02
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
normal mouse mammary cell line
Manually annotated by BRENDA team
additional information
-
Huh-7.5.1 cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
Pcp1 is an integral part of the inner membrane
-
Manually annotated by BRENDA team
-
the location of Plsp1 may depend on the developmental stage of plastids and Plsp1 may have multiple functions. In premature chloroplasts where internal membranes are not fully developed yet, Plsp1 may catalyze complete maturation of Toc75 at envelope membranes. In mature chloroplasts, Plsp1 may be mainly located at the thylakoid membrane and process thylakoidal proteins
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12000
-
1 * 25000 + 1 * 22000-23000 (a glycoprotein) + 1 * 21000 + 1 * 18000 + 1 * 12000, dog, SDS-PAGE
20067
x * 20067, calculated
21500
-
his-tagged version, overexpressed in Escherichia coli, Western blotting
22000
-
deduced from DNA sequence
24600
-
deduced from DNA sequence
26380
-
mass spectrometry
27910
-
E. coli, detergent-free DELTA2-75 mutant protein lacking the two N-terminal transmembrane spanning and the cytoplasmic domains, calculation from amino acid sequence
30000
-
gel filtration, SDS-PAGE
32103
x * 32103, calculated
35000
-
SDS-PAGE
41000
x * 41000, calculated from sequence
42000
x * 42000, calculated from sequence
67000
-
SDS-PAGE
67240
-
hypothetical polypeptide sequence deduced from the DNA sequence
268000
-
protease IV, gel filtration
640000
-
protease IV, determined in presence of Triton X-100
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
pentamer
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dynamic conformational changes of soluble, catalytically active variant DELTA2-75
C6EK19
mutant delta2-75 in complex with beta-lactam inhibitor (5S,6S) penem, crystals belong to orthorhombic space group P2(1)2(1)2 with unit cell dimensions a : 110.7 A, b : 113.2 A, c : 99.2 A, crystal structure of apoenzyme in absence of substrate or inhibitor solved by molecular replacement, space group P4(1)2(1)2, unit cell dimensions a : b : 112.4 A, c : 198.7 A
-
presence of Triton X-100 is required to obtain crystals sufficiently large for X-ray analysis
-
soluble catalytic domain of SSPase I in ternary complex with inhibitors arylomycin A2 and BAL0019193, sitting drop vapor diffusion method at 18°C, mixing of 0.002 ml of protein solution and of reservoir solution, containing 0.2 M ammonium formate, 25% PEG 2000, 0.1 M sodium cacodylate pH 6.5, and 5% tertiary-amyl alcohol, equilibration over 1 ml reservoir solution, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement
-
cubic crystalsdifferent variants, Lbpro-C51A, space group P4(1)32, unit cell a : 275.5 A, sLbpro-C51A-C133S, space group P2(1), a : 46.0, b : 110.8, c : 57.0
-
to 2.05 A resolution, monoclinic space group P21
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10.5
-
37°C, 30 min, more than 70% of the activity is retained
29827
11
-
inactivated nearly completely at above pH 11.0
29827
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
incubation at 37°C results in self-cleavage and appearance of 2 products with molecular masses of 19 kDa and 8 kDa, signal peptidase I basically loses its activity after self-cleavage
50
-
1 h, pH 7, complete inactivation
60 - 80
-
90% of the enzyme activity is abolished by incubation at 60°C for 40 min or 80°C for 1 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Inter-autocatalytic degradation at 4°C and 37°C
-
Stable at low ionic strength in solutions of nonionic detergents at low temperature
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM sodium phosphate, 10% glycerol, 0.05% Emulphogen BC-720 (Sigma) and 1 mM beta-mercaptoethanol, pH 7.2, stable for more than 6 months
-
-20°C, stable for months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by centrifugation, gel filtration and on Ni-agarose resin
-
by sonication, centrifugation and gel filtration
-
doubly 13C, 15N- and singly 15N-isotopically labeled C-terminal SPase I DELTA2-75
-
for purification purposes, tagged versions of the protein products of type I signal peptidase Sec11a and SEc11b are expressed in transformed Haloferax volcanii, with Sec11a or Sec11b being fused to a cellulose-binding domain capable of interaction with cellulose in hypersaline surroundings
-
isoenzyme protease IV
-
Lbpro-C51A, Lbpro-C51A-C-133S, and sLbpro-C51A-C133S
-
Lep and mutant delta2-75
-
MBP-SipS fusion protein, SipS, SipS-P2
recombimant His-tagged wild-type and mutant SpsBs from Escherichia coli strain BL21(DE3) by ultracentrifugation and nickel affinity chromatography
-
recombinant His-tagged Sip2 and Sip3 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant protein
wild-type and mutant enzymes
-