3.4.21.94: proprotein convertase 2
This is an abbreviated version!
For detailed information about proprotein convertase 2, go to the full flat file.
Word Map on EC 3.4.21.94
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3.4.21.94
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neuropeptides
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proopiomelanocortin
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medicine
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secretogranin
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prodynorphin
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peptidomic
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convertase-1
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molecular biology
- 3.4.21.94
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neuropeptides
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proopiomelanocortin
- medicine
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secretogranin
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prodynorphin
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peptidomic
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convertase-1
- molecular biology
Reaction
release of protein hormones and neuropeptides from their precursors, generally by hydrolysis of -Lys-Arg-/- bonds =
Synonyms
EGL-3/KPC2, More, Neuroendocrine convertase 2, PC2, PC2-like enzyme, PCSK2, pro-protein convertase-2, pro-protein convertase-2/carboxypeptidase-E, prohormone convertase, prohormone convertase 2, prohormone convertase-2, proneuropeptide convertase 2, proprotein convertase 2, proprotein convertase subtilisin/kexin-type 2
ECTree
3.4.21.94 proprotein convertase 2Advanced search results
results (
results (Engineering
Engineering on EC 3.4.21.94 - proprotein convertase 2
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A322T/S323N
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site-directed mutagenesis, the mutant shows unaltered activity, but slightly decreased sensitivity for inhibitor 7B2 CT peptide compared to the wild-type enzyme
D278E
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site-directed mutagenesis of the S4/S5 subsite residue, the mutant shows altered substrate preferences, increased activity and reduced sensitivity to inhibitor 7B2 CT peptide compared to the wild-type enzyme
L341W
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site-directed mutagenesis of the residue from the far edge of subsite S2', the mutant shows increased activity, and slightly decreased sensitivity for inhibitor 7B2 CT peptide compared to the wild-type enzyme
N356S
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site-directed mutagenesis of the distant prime site residue, the mutant shows altered substrate preferences compared to the wild-type enzyme
R281G/E282R
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site-directed mutagenesis of the S6 edge residue R281, the mutant shows largely altered substrate preferences and reduced activity compared to the wild-type enzyme
S380T
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S383A
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active site mutant, seems to be folded correctly. Is efficiently secreted as the intact zymogen in CHO-K1 cells. Its propeptide can productively insert into the mutated binding pocket without causing misfolding. In AtT-20 cells, mutant S383A is cleaved at the secondary cleavage site within the propeptide. The mutant can not be cleaved by active PC2, so that other proprotein convertases, but not PC2, may be responsible for secondary site processing. This cleavage event is pH-dependent and is inhibited by the proprotein convertase inhibitor decanoyl-Arg-Val-Lys-Arg-chloromethylketone
T271E
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site-directed mutagenesis of the residue separating the subsites S3 and S5, the mutant shows increased activity compared to the wild-type enzyme
T271N
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site-directed mutagenesis of the residue separating the subsites S3 and S5, the mutant shows unaltered activity, but slightly decreased sensitivity for inhibitor 7B2 CT peptide compared to the wild-type enzyme
additional information
additional information
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EGL-3/KPC2 mutants, malprocessing of both FMRFamide-like peptide precursors and neuropeptide-like protein precursors
additional information
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EGL-3/KPC2 mutants, malprocessing of both FMRFamide-like peptide precursors and neuropeptide-like protein precursors
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additional information
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PC2-deficient cells do not show alterations in glucose-dependent insulinotropic polypeptide precursor processing activity
additional information
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approximately one third of peptides found in wild-type mice are not detectable in PC2 knock-out mice, and another third are present at levels ranging from 25 to 75% of wild-type levels
additional information
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in PC2-null mice, basal responses and responses after a cold swim are similar to wild-type mice. After a short forced swim in warm water, PC2-null mice are significantly less responsive to the stimuli than wild-type mice, an indication of increased opioid-mediated stress-induced analgesia. Enhanced analgesia in PC2-null mice may be caused by an accumulation of opioid precursor processing intermediates with potent analgesic effects, or by loss of anti-opioid peptides
additional information
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islets from mice lacking PC2 and with beta-cell expression of human proIAPP develop amyloid associated with beta-cell death during 2-week culture. Rescue of PC2 expression by ex vivo transduction with Ad-PC2 restores NH(2)-terminal processing to mature IAPP and decreases both the extent of amyloid formation and the number of TUNEL-positive cells, and enhances cell survival
additional information
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PC2-/- mice, brain levels of neuromedin N are reduced by more than 50% with a compensatory increase in the levels of large neuromedin N. Processing at site 2 is impaired. 20% reduction in neurotensin levels
