Information on EC 3.4.21.110 - C5a peptidase

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The expected taxonomic range for this enzyme is: Streptococcus

EC NUMBER
COMMENTARY hide
3.4.21.110
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RECOMMENDED NAME
GeneOntology No.
C5a peptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
the primary cleavage site is at His67-/-Lys68 in human C5a with a minor secondary cleavage site at Ala58-/-Ser59
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY hide
100179-39-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Streptococcus zooepidemicus, gene scpZ
UniProt
Manually annotated by BRENDA team
Streptococcus zooepidemicus, gene scpZ
UniProt
Manually annotated by BRENDA team
strain SSI-9
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Manually annotated by BRENDA team
strain COH1, group B streptococci
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ac-SQLRANISH-4-nitroanilide + H2O
?
show the reaction diagram
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weak chromogenic substrate
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?
Ac-SQLRANISH-p-nitroanilide + H2O
?
show the reaction diagram
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?
chemotaxin C5a
?
show the reaction diagram
chemotaxin C5a + H2O
?
show the reaction diagram
Cys-Val-Val-Ala-Ser-Gln-Leu-Arg-Ala-Asn-Ile-His-Gln-Asp-Met-Gln-Leu-Gly-Arg
?
show the reaction diagram
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substrate is cleaved into 2 fragments
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?
Cys-Val-Val-Ala-Ser-Gln-Leu-Arg-Ala-Asn-Ile-Ser-His-Lys-Asp-Met-Gln-Leu-Gly-Arg
?
show the reaction diagram
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?
glutathione S-transferase-chemotaxin C5a-GFP + H2O
?
show the reaction diagram
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fusion protein
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?
N-terminal His-tagged C5a fusion protein + H2O
?
show the reaction diagram
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Matrix-assisted laser desorption ionization time-of-flight mass spectrometry analysis of cleaved HT-C5a indicate a loss of 830 Da, consistent with the removal of seven residues from the C-terminus
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?
rGST-C5a-enhanced green fluorescent protein + H2O
?
show the reaction diagram
SQLRANISHKDMQLGR + H2O
?
show the reaction diagram
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good substrate
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?
VVASQLRANISH + H2O
VVA + SQLRANISH
show the reaction diagram
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?
VVASQLRANISHKDMQLGR + H2O
VVASQLRANISH + KDMQLGR
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
chemotaxin C5a
?
show the reaction diagram
chemotaxin C5a + H2O
?
show the reaction diagram
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?
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
anti-ScpA antibody
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anti-SCPB antibody
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also provides protection against group A streptococcal infection
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Ca2+
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inhibition at 10 mM
EDTA
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inhibition at 5 mM
Mn2+
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inhibition at 10 mM
Zn2+
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significant inhibition at 0.1-10 mM
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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at the lowest fibronectin coverages the probability of observing a ScpB-Fn binding event increases linearly with fibronectin surface coverage. As a fibronectin monolayer is reached the probability of a ScpB-fibronectin binding event occurring increases markedly (ca. 50fold), with a concomitant increase in the rupture force from 17 pN to 33 pN
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
Ac-SQLRANISH-4-nitroanilide
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pH 7.4, 25°C, Km above 2 mM
0.36
SQLRANISHKDMQLGR
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pH 7.4, 25°C
0.936
VVASQLRANISH
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pH 7.4, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
SQLRANISHKDMQLGR
Streptococcus pyogenes
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pH 7.4, 25°C
0.2
VVASQLRANISH
Streptococcus pyogenes
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pH 7.4, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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SQLRANISHKDMQLGR as substrate
8.6
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activity against chromogenic substrate Ac-SQLRANISH-4-nitroanilide is 60% higher than at pH 7.4
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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activity sharply declines below pH 7
8.6
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activity against chromogenic substrate Ac-SQLRANISH-4-nitroanilide is 60% higher than at pH 7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 43
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increase of temperature from 5°C to 43°C results in 10fold increase in enzyme activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
123300
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predicted from cDNA
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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propeptide is cleaved either via an autocatalytic intramolecular cleavage or by exogenous protease streotopain
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
SCP mutant, by hanging drop method, to 2 A resolution, SCPB composed of five distinct domains, N-terminal subtilisin-like protease domain with a 134-residue protease-associated domain inserted into a loop between two beta-strands, and with one of two Arg-Gly-Asp sequences found in SCPB, at the C-terminus are three fibronectin type III domains, second Arg-Gly-Asp sequence is located between fibronectin type III (1) and fibronectin type III (2)
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crystal structure of an active form of ScpA is solved to 1.9 A resolution. The ScpA structure reveals that access to the catalytic site is restricted by variable regions in the catalytic domain and by the presence of the inserted protease-associated domain and the second fibronectin type III domains (Fn2). Modeling of the ScpA-C5a complex indicates that the substrate binds with carboxyl-terminal residues (65-74) extended through the active site and core residues (1-64) forming exosite-type interactions with the Fn2 domain. Substrate binding is anticipated to be dominated by ionic interactions in two distinct regions of ScpA. On the prime side of the active site, salt bridges are predicted between P1', P2', and P7' residues, and residues in the catalytic and PA domains. Remote to the active site, a larger number of ionic interactions between residues in the C5a core and the Fn2 domain are observed in the model. Thus, both PA and Fn2 domains are expected to play significant roles in substrate recognition
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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complete inactivation
65
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85% activity after 30 min, 75% activity after 60 min
100
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30% activity after boiling for 10 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
as a GST fusion protein
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by ion-exchange chromatography
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nickel affinity column chromatography
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standard method
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amino acid residues 31-1032 of the C5a peptidase gene are fused to GST and expressed in Escherichia coli. In addition expression as an N-terminal His-tagged C5a fusion protein in Escherichia coli
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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female ICR mice immunized with encapsulated C5a peptidase or free C5a peptidase
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full length clone and ScpB-PDF fragment
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gene scpZ, quantitative real-time PCR expression analysis
in Escherichia coli B834(DE3)
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ScpB expressed as a fusion protein
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strain 90 226 SCPA-mutant expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
culture in the presence of 1 to 50% human serum results in a dose-dependent induction of reporter gene activity for C5a peptidase
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D130A/S512A
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SCP mutant with 949-residue fragment
D130A
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mutant with reduced proteolytic activity
D130A/S512A
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no hydrolysis of substrate
H193A
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mutant with reduced proteolytic activity
L512A
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mutant with reduced proteolytic activity
N295A
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mutant with reduced proteolytic activity
S512A
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no autocatalytic cleavage
D130A
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strain 90 226 SCPA-mutant, impaired capacity to infect nasal mucosa-associated lymphoid tissue
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
additional information