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Information on EC 3.4.21.89 - Signal peptidase I and Organism(s) Homo sapiens

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.89 Signal peptidase I
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Cleavage of hydrophobic, N-terminal signal or leader sequences
Synonyms
signal peptidase, leader peptidase, spase, protease iv, signal peptidase i, spase i, type i signal peptidase, leader proteinase, plsp1, sec11, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Bacterial leader peptidase 1
-
-
-
-
Escherichia coli leader peptidase
-
-
-
-
Eukaryotic signal peptidase
-
-
-
-
Eukaryotic signal proteinase
-
-
-
-
HOSP
-
-
-
-
Leader peptidase
-
-
-
-
Leader peptidase I
-
-
-
-
Leader peptide hydrolase
-
-
-
-
Leader proteinase
-
-
-
-
Peptidase, signal
-
-
-
-
Pilin leader peptidase
-
-
-
-
Prokaryotic leader peptidase
-
-
-
-
Prokaryotic signal peptidase
-
-
-
-
Prokaryotic signal proteinase
-
-
-
-
Propeptidase
-
-
-
-
Proteinase, eukaryotic signal
-
-
-
-
Proteinase, signal
-
-
-
-
PuIO prepilin peptidase
-
-
-
-
Signal peptidase
Signal peptide hydrolase
-
-
-
-
Signal peptide peptidase
Signalase
-
-
-
-
SPC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
65979-36-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
p23 + H2O
p21 + ?
show the reaction diagram
-
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
show the reaction diagram
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
signal peptides from preproteins + H2O
mature proteins
show the reaction diagram
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(Z-LL)2-ketone
-
completely abolishes signal peptide peptidase-catalysed maturation of p23 to p21 in the case of wild-type
L685,458
-
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
Huh-7.5.1 cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
membrane topology of the 12000 and the 25000 MW subunit
Manually annotated by BRENDA team
additional information
-
human signal peptide peptidase promotes the formation of hepatitis C virus non-enveloped particles and is captured on the viral membrane during assembly
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SC11A_HUMAN
179
1
20625
Swiss-Prot
other Location (Reliability: 5)
SC11B_HUMAN
166
1
19160
Swiss-Prot
Secretory Pathway (Reliability: 1)
SC11C_HUMAN
192
1
21542
Swiss-Prot
other Location (Reliability: 4)
A0A024RC78_HUMAN
179
1
20625
TrEMBL
other Location (Reliability: 5)
K7EJQ7_HUMAN
161
1
18095
TrEMBL
other Location (Reliability: 4)
B4DI03_HUMAN
156
1
17404
TrEMBL
other Location (Reliability: 4)
H0YNX5_HUMAN
106
0
11986
TrEMBL
Secretory Pathway (Reliability: 2)
Q6IAM7_HUMAN
179
1
20611
TrEMBL
other Location (Reliability: 5)
H0YNA5_HUMAN
135
1
15649
TrEMBL
Secretory Pathway (Reliability: 5)
Q7Z4Z6_HUMAN
188
1
21612
TrEMBL
Mitochondrion (Reliability: 3)
H0YNG3_HUMAN
163
1
18651
TrEMBL
other Location (Reliability: 5)
SPCS2_HUMAN
226
0
25003
Swiss-Prot
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kalies, K.U.; Hartmann, E.
Membrane topology of the 12- and the 25-kDa subunits of the mammalian signal peptidase complex
J. Biol. Chem.
271
3925-3929
1996
Canis lupus familiaris, Homo sapiens
Manually annotated by BRENDA team
Dalbey, R.E.; Lively, M.O.; Bron,S.; Van Diijl, J.M.
The chemistry and enzymology of the type I signal peptidases
Protein Sci.
6
1129-1138
1997
Bacillus amyloliquefaciens, [Bacillus] caldolyticus, Bacillus subtilis, Bacillus licheniformis, Bradyrhizobium japonicum, Saccharomyces cerevisiae, Canis lupus familiaris, Gallus gallus, Escherichia coli, Haemophilus influenzae, Methanocaldococcus jannaschii, Staphylococcus aureus, Mycobacterium tuberculosis, no activity in Mycoplasma genitalium, Phormidium laminosum, Pseudomonas fluorescens, Rana sp., Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium, Caenorhabditis elegans (P34525), Schizosaccharomyces pombe (Q10259), Homo sapiens (Q15005), Rhodobacter capsulatus (Q52697)
Manually annotated by BRENDA team
Majeau, N.; Gagne, V.; Bolduc, M.; Leclerc, D.
Signal peptide peptidase promotes the formation of hepatitis C virus non-enveloped particles and is captured on the viral membrane during assembly
J. Gen. Virol.
86
3055-3064
2005
Homo sapiens
Manually annotated by BRENDA team
Loureiro, J.; Lilley, B.N.; Spooner, E.; Noriega, V.; Tortorella, D.; Ploegh, H.L.
Signal peptide peptidase is required for dislocation from the endoplasmic reticulum
Nature
441
894-897
2006
Homo sapiens
Manually annotated by BRENDA team
Pene, V.; Hernandez, C.; Vauloup-Fellous, C.; Garaud-Aunis, J.; Rosenberg, A.R.
Sequential processing of hepatitis C virus core protein by host cell signal peptidase and signal peptide peptidase: a reassessment
J. Viral Hepat.
16
705-715
2009
Homo sapiens
Manually annotated by BRENDA team