3.4.21.B12: prostase
This is an abbreviated version!
For detailed information about prostase, go to the full flat file.
Word Map on EC 3.4.21.B12
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3.4.21.B12
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klk4
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kallikreins
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amelogenins
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amelogenesis
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ameloblastin
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enamelysin
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incisor
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imperfecta
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maturation-stage
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amelx
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amelotin
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medicine
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secretory-stage
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hypomineralized
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masp-1
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hypomaturation
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crystallite
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metalloproteinase-20
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analysis
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diagnostics
- 3.4.21.B12
- klk4
- kallikreins
- amelogenins
-
amelogenesis
- ameloblastin
- enamelysin
- incisor
- imperfecta
-
maturation-stage
-
amelx
-
amelotin
- medicine
-
secretory-stage
-
hypomineralized
- masp-1
-
hypomaturation
-
crystallite
-
metalloproteinase-20
- analysis
- diagnostics
Reaction
proteolysis of polypeptides =
Synonyms
EM serine proteinase 1, EMSP1, enamel matrix serine protease 1, HK4, K4, kallikrein 1-related peptidase 4, kallikrein 4, kallikrein-4, kallikrein-4 proteinase, kallikrein-like protein 1, kallikrein-related peptidase, kallikrein-related peptidase 4, kallikrein-related peptidase-4, KLK, KLK-4 proteinase, KLK-L1, KLK4, More, peptidase S01.251, prostase, prostate cancer serine protease, PRSS17, S01.251, serine protease 1, serine protease 17, tissue kallikrein-related peptidase 4
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 3.4.21.B12 - prostase
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glycoprotein
proteolytic modification
glycoprotein
3 potential N-linked glycosylation sites: N134, N169, and N214 of the nucleotide sequence
glycoprotein
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3 potential N-linked glycosylation sites: N134, N169, and N214 of the nucleotide sequence
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recombinant chimeric enzyme with exchange of the pro-piece of the zymogen for that of prostate-specific antigen PSA to create an activation site suceptible for trypsin-type proteases proteolytically activates itself
proteolytic modification
KLK4 is secreted as an inactive zymogen, pro-KLK4
proteolytic modification
no activation of recombinant zymogen by native KLK4 enzyme in vitro
proteolytic modification
recombinant zymogen can be activated in vitro by thermolysin and by recombinant pig enamelysin