3.4.21.72: IgA-specific serine endopeptidase
This is an abbreviated version!
For detailed information about IgA-specific serine endopeptidase, go to the full flat file.
Word Map on EC 3.4.21.72
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3.4.21.72
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neisseria
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haemophilus
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streptococcus
-
influenzae
-
gonorrhoeae
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hinge
-
meningitidis
-
sanguis
-
autotransporter
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pneumococcal
-
gonococcal
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serogroups
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meningococci
-
oralis
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medicine
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protease-producing
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lactamica
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nontypeable
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paraproteins
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ramosum
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enzyme-neutralizing
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urealyticum
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pharmacology
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agriculture
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drug development
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analysis
- 3.4.21.72
- neisseria
- haemophilus
- streptococcus
- influenzae
- gonorrhoeae
- hinge
- meningitidis
- sanguis
-
autotransporter
- pneumococcal
-
gonococcal
-
serogroups
-
meningococci
- oralis
- medicine
-
protease-producing
- lactamica
-
nontypeable
-
paraproteins
- ramosum
-
enzyme-neutralizing
- urealyticum
- pharmacology
- agriculture
- drug development
- analysis
Reaction
Cleavage of immunoglobulin A molecules at certain Pro-/- bonds in the hinge region. No small molecule substrates are known =
Synonyms
Iga, IgA protease, IgA protease A1, IgA protease B2, IgA proteinase, IgA-specific proteinase, IgA1 protease, IgA1-protease, IgA1-specific protease, IgA1?P, IgA1P, IgA1pr, IgaA1, IgaA2, IgaB2, IgAP, Immunoglobulin A protease, Immunoglobulin A proteinase, immunoglobulin A1 protease, NMB IgA1 protease, Proteinase, immunoglobulin A, serine-type IgA1 protease, serine-type immunoglobulin A1 protease, ST-11 IgA protease, type 2 IgA1 protease
ECTree
3.4.21.72 IgA-specific serine endopeptidaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.21.72 - IgA-specific serine endopeptidase
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NATURAL SUBSTRATE 
NATURAL 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
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fab
-
cleavage of the hinge region
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
IgA proteases only cleave the proline, serine and threonine rich hinge peptide unique to immunoglobulin A1
-
-
?
NF-kappaB p65/RelA component + H2O
?
-
specific cleavage at the C-terminal region of NF-kappaB p65/RelA component within the nucleus of infected cells
-
-
?
human IgA1 + H2O
?
culture supernatants from all strains tested cause degradation of human IgA1
-
-
?
human IgA1 + H2O
?
-
IgA1 protease is a proteolytic enzyme with strict substrate specificity for human IgA1
-
-
?
human IgA1 + H2O
?
the enzyme specifically cleaves the hinge region of human IgA1, the predominant class of immunoglobulin present on mucosal membranes
-
-
?
human IgA1 + H2O
?
unique cleavage specificity of the NTHI IgA1 protease
-
-
?
human IgA1 + H2O
?
-
IgA1 protease is a proteolytic enzyme with strict substrate specificity for human IgA1
-
-
?
human IgA1 + H2O
?
-
IgA1 protease is a proteolytic enzyme with strict substrate specificity for human IgA1
-
-
?
human IgA1 + H2O
?
-
the enzyme possesses a unique substrate specificity to immunoglobulin A1
-
-
?
human immunoglobulin A1 + H2O
?
bacterial isolates show wide variability in IgA1 protease activity, and those isolated from patients with clinical infection possess the highest levels of activity, overview
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
human IgA1, cleavage at the hinge region
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Haemophilus influenzae ATCC 10211
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Haemophilus influenzae ATCC 49247
-
human IgA1, cleavage at the hinge region
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Haemophilus influenzae ATCC 49247
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
cleavage of the hinge region
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Neisseria gonorrhoeae ATCC 49226
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Neisseria meningitidis ATCC 13090
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
IgA1 from human serum
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
IgA1 from human serum
-
-
?
immunoglobulin A + H2O
?
-
IgA 1 proteases are a family of bacterial enzymes specifically cleaving human IgA, the immunoglobulin for antibody defense of mucosal surfaces
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
immunoglobulin A + H2O
?
-
IgA 1 proteases are a family of bacterial enzymes specifically cleaving human IgA, the immunoglobulin for antibody defense of mucosal surfaces
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
immunoglobulin A + H2O
?
-
IgA 1 proteases are a family of bacterial enzymes specifically cleaving human IgA, the immunoglobulin for antibody defense of mucosal surfaces
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
immunoglobulin A + H2O
?
-
IgA 1 proteases are a family of bacterial enzymes specifically cleaving human IgA, the immunoglobulin for antibody defense of mucosal surfaces
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
additional information
?
-
-
the type 2 IgA1 protease is a potential virulence factor in Haemophilus influenzae, the igaB encoded enzyme is the primary mediator of IgA1 protease activity in strain 11P6H, not the type 1 IgA1 protease encoded by igaA, IgA1 proteases are classified as type 1 or type 2 based on the specific site of enzymatic cleavage in the hinge region of the IgA1 molecule
-
-
?
additional information
?
-
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
-
immunglobulin A1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agimmunglobulin A1 also exists as circulating immunglobulin A1-immunglobulin G immune complexes in patients with IgAN
-
-
?
additional information
?
-
-
the IgA protease from Haemophilus influenzae strain ATCC 49247 has a high activity and the ability to degrade human in vivo deposited aberrantly glycosylated IgA1-containing immune complex
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 10211
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 10211
-
immunglobulin A1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agimmunglobulin A1 also exists as circulating immunglobulin A1-immunglobulin G immune complexes in patients with IgAN
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 49247
-
the IgA protease from Haemophilus influenzae strain ATCC 49247 has a high activity and the ability to degrade human in vivo deposited aberrantly glycosylated IgA1-containing immune complex
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 49247
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 49247
-
immunglobulin A1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agimmunglobulin A1 also exists as circulating immunglobulin A1-immunglobulin G immune complexes in patients with IgAN
-
-
?
additional information
?
-
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
Neisseria gonorrhoeae ATCC 49226
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
the enzyme performs autoproteolysis at the SD domain
-
-
?
additional information
?
-
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
Neisseria meningitidis ATCC 13090
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
-
cleavage of p65/RelA occurs at the C-terminal region which contains the transactivation domain (TAD). Removal of the TAD from the rest of the protein may therefore disable the activation capacity of the native p65/RelA molecule
-
-
?
