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3.4.21.76: Myeloblastin

This is an abbreviated version!
For detailed information about Myeloblastin, go to the full flat file.

Word Map on EC 3.4.21.76

Reaction

Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-/- > -Val-/- =

Synonyms

AGP7, C-ANCA antigen, hPR-3, human leukocyte proteinase 3, human PR3, human proteinase 3, Leukocyte proteinase 3, Leukocyte proteinase 4, membrane proteinase 3, membrane-associated proteinase 3, mP3, mPR3, myeloblastin, neutrophil protease PR3, neutrophil proteinase 3, neutrophil serine protease, neutrophilic serine protease proteinase 3, P29, p29b, PMNL proteinase, Pr 3, PR-3, PR3, protease 3, proteinase 3, Proteinase PR-3, Proteinase-3, proteinase3, PRTN3, SAP3, secreted aspartic proteinase 3, surface proteinase 3, Wegener autoantigen, Wegener's autoantigen, Wegener's granulomatosis autoantigen, Xenopus PR3, xPR-3

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.76 Myeloblastin

Engineering

Engineering on EC 3.4.21.76 - Myeloblastin

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F180A/F181A
-
mutant is still able to display membrane PR3 after degranulation, with similar fluorescence intensity as wild-type
F180A/F181A/L228A/F229A
-
contrary to wild-type, membrane anchorage is abrogated in mutant. Mutant is still able to cleave the synthetic substrate Boc-Ala-Pro-Val in cell lysates, but fails to cleave extracellular fibronectin, is not externalized after apoptosis and does not impair macrophage phagocytosis of apoptotic cells, does not promote myeloid cell proliferation and fails to cleave p21/waf1
F180A/L228A/F229A
-
mutant is still able to display membrane PR3 after degranulation, with similar fluorescence intensity as wild-type
H4A
site-directed mutagenesis
L228A
-
mutant is still able to display membrane PR3 after degranulation, with similar fluorescence intensity as wild-type
L228A/F229A
-
mutant is still able to display membrane PR3 after degranulation, with similar fluorescence intensity as wild-type
N102Q
-
glycosylation deficient recombinant PR3 mutant, hydrolytic activity like recombinant PR3-wild-type. N-terminal processing is delayed
N102Q/N147Q
-
glycosylation deficient recombinant PR3 mutant, reduction in hydrolytic activity in relation to recombinant PR3-wild-type. Reduction in hydrolytic activity is more pronounced than the reduction induced by deglycosylation of purified neutrophil PR3. N-terminal processing is delayed
N147Q
-
glycosylation deficient recombinant PR3 mutant, is processed like recombinant PR3-wild-type
R193A/R194A/K195A
-
mutant does not affect membrane expression
R193A/R194A/K195A/R227A
-
contrary to wild-type, membrane anchorage is abrogated in mutant
R194A/K195A/R227A
-
mutant does not affect membrane expression
S176A
substitution of the active centre
S195A
site-directed mutagenesis, cDNA construction of a catalytically inactive active site enzyme mutant lacking the codons for the N-terminal activation dipeptide, DELTAPR3ctp-S195A
S203A
S204A
site-directed mutagenesis
V35M/S38AN/I38BP/Q74R/N113K/N159K/119-122QVAS
-
results in the gibbon proteinase 3 variant 2. Is no longer able to interact with the mouse antibodies 4A5 and WGM2, but retains its binding to CLB12.8
V35M/S38AN/L39BP/Q74R
-
results in the gibbon proteinase 3 variant 1. The binding site for mouse antibody CLB12.8, but not that for MCPR3-2, is reconstituted. Binds also to mouse antibody 6A6. Like MCPR3-2, WGM3 binds neither to gibbon PR3 nor to the humanized gibbon proteinase 3 variant 1
additional information
-
catalytically inactive Ser195-substituted PR3 variant, eliminates quality check of the antigen preperation. Recombinant PR3 variants which only carry a single antigenic region on its surface may be used to neutralize or eliminate circulating anti-neutrophil cytoplasmic antibodies (ANCA) in patients without triggering immune complex-mediated type III reactions