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Information on EC 3.4.21.89 - Signal peptidase I
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3.4.21.89 Signal peptidase ISpecify your search results
Word Map
- 3.4.21.89
- polyproteins
- lipoprotein
- preproteins
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cleavable
- foot-and-mouth
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unprocessed
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dyad
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membrane-spanning
- prolipoproteins
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translocons
- pilins
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uncleaved
- beta-lactamase
- drug development
- flavivirus
- ompa
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nonstructural
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cotranslationally
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co-translational
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sec-dependent
- globomycin
- presequence
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papain-like
- prepeptide
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polytopic
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oligonucleotide-directed
- ns2b
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signal-anchored
- pharmacology
- medicine
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
signal peptidase, leader peptidase, spase, protease iv, signal peptidase i, spase i, type i signal peptidase, leader proteinase, plsp1, sec11, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Bacterial leader peptidase 1
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EC 3.4.99.36
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formerly
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Escherichia coli leader peptidase
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Eukaryotic signal peptidase
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Eukaryotic signal proteinase
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HOSP
Leader peptidase
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Leader peptidase I
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Leader peptide hydrolase
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Leader proteinase
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LepB
Peptidase, signal
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Pilin leader peptidase
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plastidic type I signal peptidase 1
Plsp1
Prokaryotic leader peptidase
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Prokaryotic signal peptidase
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Prokaryotic signal proteinase
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Propeptidase
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protease IV
Proteinase, eukaryotic signal
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Proteinase, signal
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PuIO prepilin peptidase
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Rv2903c
SEC11
secretory protein 11
Signal peptidase
signal peptidase I
Signal peptidase IB
signal peptidase type I
Signal peptide hydrolase
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Signal peptide peptidase
Signalase
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SipS
SipT
SipU
SipV
SipY
SP I
SPase
Spase I
SPase IB
SPC
SPI
SpsB
type I signal peptidase
HOSP
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Signal peptidase
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Signal peptide peptidase
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SPC
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cleavage of hydrophobic, N-terminal signal or leader sequences
mechanism
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Cleavage of hydrophobic, N-terminal signal or leader sequences
mechanism
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Cleavage of hydrophobic, N-terminal signal or leader sequences
mechanism
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Cleavage of hydrophobic, N-terminal signal or leader sequences
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
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CAS REGISTRY NUMBER
COMMENTARY
65979-36-4
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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
(4-(4-dimethylaminophenylazo)benzoyl)-AGHDAHASET-(5-((2-aminoethyl)amino)-naphthalene-1-sulfonic acid) + H2O
(4-(4-dimethylaminophenylazo)benzoyl)-AGHDAHA + SET-(5-((2-aminoethyl)amino)-naphthalene-1-sulfonic acid)
(NO2)YFSASALA-KI-(2-aminobenzoyl)K-NH2 + H2O
(NO2)YFSASALA + KI-(2-aminobenzoyl)K-NH2
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-
-
?
Ac-AGPRPTRIAFGA-NH2 + H2O
N-acetyl-L-alanine + GPRPTRIAFGA-NH2
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-
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?
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
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-
-
?
Acetyl-Trp-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile-4-methylcoumarin 7-amide + H2O
?
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-
-
-
?
Ala-Ala-Phe-4-methylcoumaryl-7-amide + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
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-
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?
alkaline phosphatase signal peptide
?
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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
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amphipatic, chimeric cytochrome b5 precursor
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?
beta-lactam response sensor BlaR1 + H2O
?
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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
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signal peptidase Sec11a and Sec11b cleave differentially
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?
Dabcyl-AGHDAHASET(EDANS) + H2O
?
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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
?
signal peptide of elastase
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?
envelope protein Toc75 precursor + H2O
mature envelope protein Toc75 + signal peptide
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?
Eukaryotic initiation factor eIF-4gamma from rabbit reticulocytes + H2O
?
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cleavage site Gly479-Arg480
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?
hexanoyl-LTPTQAKAASKIDD-OH + H2O
hexanoyl-LTPTQAKA + ASKIDD
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?
KLTFGTVKPVQAIAGYEWL + H2O
?
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synthetic peptide substrate, based upon the signal peptide of prestreptokinase from Streptococcus pyogene
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?
mammalian cytochrome b(5) precursor + H2O
?
the processing can occur after almost complete exocytoplasmic translocation of the preprotein is accomplished
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?
mitochondrial inter membrane space protein IMS
?
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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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?
octanoyl-LTPTQAKAASKIDD-OH + H2O
octanoyl-LTPTQAKA + ASKIDD
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?
Phe-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile + H2O
Phe-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile + ?
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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
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?
pre-maltose binding protein + H2O
maltose binding protein + signal peptide
the maltose binding protein (MBP) is mutated to introduce aromatic amino acids (tryptophan, tyrosine and phenylalanine) at P2' of the signal peptidase I cleavage sequence. All mutants with aromatic amino acids at P2' are exported less efficiently as indicated by a slight increase in precursor protein in vivo. Binding of LepB to peptides that encompass the MBP cleavage site are analysed using surface plasmon resonance. The presence of phenylalanine and tyrosine at P2', but not tryptophan, increase to a small extent the amount of preMBP in the sample
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?
pre-SceD protein + H2O
SceD + presequence of pre-SceD
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substrate of Sip2 and Sip3
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?
Precursor of the 23kd photosystem II protein + H2O
23kd Photosystem II protein + ?
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?
Precursors of the exported proteins Skp of E. coli + H2O
Exported proteins Skp of E. coli + ?
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processed at the authentic site
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?
pro-rem + H2O
signal peptide + rem
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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
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?
PsbO precursor protein + H2O
mature PcpO + signal peptide
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
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self-cleavage, results in a truncated product
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?
Staphylococcus epidermidis SceD preprotein + H2O
Staphylococcus epidermidis SceD protein + SceD protein prepeptide fragment
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specific cleavage at a single cleavage site located at the A-S bond
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?
synaptobrevin + H2O
?
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tail-anchored integral membrane protein
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?
Thylakoid lumen protein precursors + H2O
Thylakoid lumen protein + ?
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?
tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
tosyl-Gly-Pro-Lys + p-nitroaniline
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chromozym PL
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?
Y-NO2-FSASALAKIK-2-aminobenzoyl-NH2 + H2O
Y-NO2-FSASALA + KIK-2-aminobenzoyl-NH2
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?
YFSASALA-4-methylcoumarin-7-amide + H2O
YFSASALA + 7-amino-4-methylcoumarin