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
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amelogenesis
- ameloblastin
- enamelysin
- incisor
- imperfecta
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maturation-stage
-
amelx
-
amelotin
- medicine
-
secretory-stage
-
hypomineralized
- masp-1
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hypomaturation
-
crystallite
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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
3.4.21.B12 prostaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.21.B12 - prostase
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SUBSTRATE 
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
(Abz)-SKGR-SLIGK(N-[2,4-dintrophenyl]ethylenediamine)-Asp-OH
?
-
fluorescence quenched peptide spanning the PAR-2 activation site, is rapidly cleaved by KLK4
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-
?
32 kDa enamelin + H2O
?
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five cleavage sites on the C-terminal sides of R180, Y205, H206, M219 and R262. Kallikrein 4 digestion of the 32 kDa enamelin generates nine major cleavage products. 12 h of digestion with KLK4, all of the 32 kDa enamelin has been cleaved. Some cleavage products persist after 48 h of digestion
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-
?
52 kDa prostatic acid phosphatase + H2O
33 kDa prostatic acid phosphatase + 19 kDa fragment
benzoyl-L-Ile-L-Glu-Gly-L-Arg-4-nitroanilide + H2O
benzoyl-L-Ile-L-Glu-Gly-L-Arg + 4-nitroaniline
benzyloxycarbonyl-FR-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-FR + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-LR-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-LR + 7-amino-4-methylcoumarin
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-
-
?
D-Val-Leu-Arg-7-amido-4-trifluoromethyl coumarin + H2O
D-Val-Leu-Arg + 7-amino-4-trifluoromethyl coumarin
-
-
-
?
EKK-7-amido-4-methylcoumarin + H2O
EKK + 7-amino-4-methylcoumarin
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9% of the activity with VPR-7-amido-4-methylcoumarin
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-
?
GPR-7-amido-4-methylcoumarin + H2O
GPR + 7-amino-4-methylcoumarin
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20% of the activity with VPR-7-amido-4-methylcoumarin
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-
?
human ephrin-B2 + H2O
?
low activity with recombinant human enzyme and human substrate
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-
?
murine ephrin-B2 + H2O
?
the substrate harbors N-glycosylation sites its extracellular domain sequence, R27-R178, good activity with recombinant human enzyme and murine substrate, the primary enzyme cleavage site in murine ephrin-B2 is verified as located between extracellular domain residues Arg178 and N179
cleavage fragments, overview
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?
pro-urokinase-type plasminogen activator + H2O
activated urokinase-type plasminogen activator
protease-activated receptor-1 + H2O
?
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KLK4 cleaves protease-activated receptor-1 at the activation site on intact cell surface
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-
?
QAR-7-amido-4-methylcoumarin + H2O
QAR + 7-amino-4-methylcoumarin
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38% of the activity with VPR-7-amido-4-methylcoumarin
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-
?
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
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-
-
-
?
urokinase-type plasminogen activator receptor + H2
?
-
cleavage occurs in D1-D2 linker sequence and, to a lesser extent, in D3 juxtamembrane domain
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-
?
urokinase-type plasminogen activator receptor + H2O
?
cleaves after Thr-Tyr-Ser-Arg as well as in the sequence Val-Gln-Tyr-Arg-/-Ser-Gly
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-
?
VLK-7-amido-4-methylcoumarin + H2O
VLK + 7-amino-4-methylcoumarin
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60% of the activity with VPR-7-amido-4-methylcoumarin
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-
?
52 kDa prostatic acid phosphatase + H2O
33 kDa prostatic acid phosphatase + 19 kDa fragment
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recombinant self-activated, chimeric enzyme
products contain 256 and 73 amino acid residues, respectively
?
52 kDa prostatic acid phosphatase + H2O
33 kDa prostatic acid phosphatase + 19 kDa fragment
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primary cleavage site is the Arg73-Ser74 bond
products contain 256 and 73 amino acid residues, respectively
?
52 kDa prostatic acid phosphatase + H2O
33 kDa prostatic acid phosphatase + 19 kDa fragment
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inactivation of substrate
products contain 256 and 73 amino acid residues, respectively
?
52 kDa prostatic acid phosphatase + H2O
33 kDa prostatic acid phosphatase + 19 kDa fragment
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enzyme may be involved in the physiological clearance of prostatic acid phosphatase
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?
amelogenin + H2O
?
the enzyme plays a pivotal role during dental enamel formation by degrading the major enamel protein, amelogenin, prior to the final steps of enamel hardening. KLK4 self-destructs once amelogenin is degraded. It progressively loses activity, becomes aggregated, and autofragmented when incubated without substrate in both the presence and absence of reducer. However, with non-ionic detergent present as proxy substrate, KLK4 remains active and intact throughout
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-
?
amelogenin + H2O
amelogenin fragments
recombinant substrate from pig expressed in Escherichia coli strain XL-1 blue as His-tagged protein
product identification by N-terminal sequencing and mass spectrometry
?
benzoyl-L-Ile-L-Glu-Gly-L-Arg-4-nitroanilide + H2O
benzoyl-L-Ile-L-Glu-Gly-L-Arg + 4-nitroaniline
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recombinant self-activated, chimeric enzyme
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-
?
benzoyl-L-Ile-L-Glu-Gly-L-Arg-4-nitroanilide + H2O
benzoyl-L-Ile-L-Glu-Gly-L-Arg + 4-nitroaniline
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fluorogenic substrate, i.e. S-2222
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-
?
D-Pro-L-Phe-L-Arg-4-nitroanilide + H2O
D-Pro-L-Phe-L-Arg + 4-nitroaniline
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recombinant self-activated, chimeric enzyme
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-
?
D-Pro-L-Phe-L-Arg-4-nitroanilide + H2O
D-Pro-L-Phe-L-Arg + 4-nitroaniline
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fluorogenic substrate, i.e. S-2302
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-
?
D-Val-L-Leu-L-Lys-4-nitroanilide + H2O
D-Val-L-Leu-L-Lys + 4-nitroaniline
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recombinant self-activated, chimeric enzyme
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-
?
D-Val-L-Leu-L-Lys-4-nitroanilide + H2O
D-Val-L-Leu-L-Lys + 4-nitroaniline
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fluorogenic substrate, i.e. S-2251
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-
?
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
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recombinant self-activated, chimeric enzyme
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-
?
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
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fluorogenic substrate, i.e. S-2266
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-
?
matrix metalloproteinase-1 + H2O
?
the enzyme activates matrix metalloproteinase-1, a protease that promotes prostate tumor growth and metastasis. Matrix metalloproteinase-1 is produced in the tumor compartment of prostate cancer bone metastases, highlighting its accessibility to KLK4 at this site
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-
?
plasma hepatocyte growth factor activator zymogen + H2O
mature HGF activator + ?
activation, hepatocyte growth factor is mainly secreted from fibroblasts as an inactive single-chain precursor, which lacks biological activity
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-
?
plasma hepatocyte growth factor activator zymogen + H2O
mature HGF activator + ?
conversion to an active two-chain form
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-
?
polypeptide + H2O
peptides
enzyme is involved in degradation of extracellular matrix and activation of prostate specific antigen PSA and other proteases
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?
polypeptide + H2O
peptides
enzyme is regulated by steroid hormones
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?
polypeptide + H2O
peptides
enzyme may be involved in the pathogenesis and/or progression of prostate, breast, and possibly other malgnancies
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?
polypeptide + H2O
peptides
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enzyme plays a role in the physiologic processing of seminal plasma proteins , e.g. pro-PSA, as well as in the pathogenesis of prostate cancer through the activation of pro-PSA
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?
pro-prostate-specific antigen + H2O
activated prostate-specific antigen
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activation of substrate
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?
pro-prostate-specific antigen + H2O
activated prostate-specific antigen
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recombinant self-activated, chimeric enzyme
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?
pro-prostate-specific antigen + H2O
activated prostate-specific antigen
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i.e. PSA
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?
pro-prostate-specific antigen + H2O
activated prostate-specific antigen
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activation of PSA
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?
pro-urokinase-type plasminogen activator + H2O
activated urokinase-type plasminogen activator
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activation of substrate
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?
pro-urokinase-type plasminogen activator + H2O
activated urokinase-type plasminogen activator
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recombinant self-activated, chimeric enzyme
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?
pro-urokinase-type plasminogen activator + H2O
activated urokinase-type plasminogen activator
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i.e. pro-uPA
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?
thrombospondin-1 + H2O
?
the enzyme liberates an N-terminal product, with purported angiogenic activity, from thrombospondin-1. It cleaves thrombospondin-1 in osteoblast-derived matrix
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-
?
urokinase-type plasminogen activator + H2O
?
cleaves after Pro-Arg-Phe-Lys
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-
?
additional information
?
-
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no activity with serum albumin from human seminal plasma
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?
additional information
?
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enzyme has a trypsin-type substrate specificty
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-
?
additional information
?
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no activity with pyroglu-Gly-Arg-4-nitroanilide, i.e. S-2444, and with 3-carbomethoxypropionyl-L-Arg-L-Pro-L-Tyr-4-nitroanilide, i.e. S-2586
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-
?
additional information
?
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enzyme is regulated by steroid hormones, contains androgen response elements in the proximal promotor region
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?
additional information
?
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enzyme is involved in tissue remodeling and cancer metastasis
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?
additional information
?
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enzyme modulates the tumor-associated urokinase-type plasminogen activator/urokinase-type plasminogen activator receptor system activity by either activating the pro-enzyme form of urokinase-type plasminogen activator or cleaving the cell surface-associated urokinase-type plasminogen activator receptor
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-
?
additional information
?
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enzyme cleaves more efficiently after Arg compared to Lys at the P1 position and exhibits modest specificity for amino acids at P2 and P3 positions
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?
additional information
?
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KLK4 initiates phosphorylation of ERK1/2 via PAR-2
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-
?
additional information
?
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kallikrein-4 is a serine protease expressed during enamel maturation, and proteolytic processing of the enamel matrix by KLK4 is critical for proper enamel formation. In vitro dipeptidyl peptidase I activates pro-KLK4 to cleave a fluorogenic peptide containing a KLK4 cleavage site
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-
?
additional information
?
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preference for Arg over Lys at position P1. KLK4 prefers as P2 residue the medium-sized polar Gln over the more hydrophobic Val, Leu, Thr, and Pro, whereas large aromatic and basic side chains are not accepted. Marked specificity for medium-sized to large hydrophobic P4 residues. Activation cleavage site: SCSQ-IING
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-
?
additional information
?
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two proteases are secreted into the enamel matrix of developing teeth. The early protease is enamelysin (MMP-20). The late protease is kallikrein 4. KLK4 aggressively degrades the retained organic matrix following the termination of enamel protein secretion. The principle functions of MMP-20 and KLK4 in dental enamel formation are to facilitate the orderly replacement of organic matrix with mineral, generating an enamel layer that is harder, less porous, and unstained by retained enamel proteins
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-
?
additional information
?
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the enzyme performs proteolytic autoactivation
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?
additional information
?
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the enzyme performs proteolytic autoactivation
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?
additional information
?
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position of predicted enzyme cleavage sites within the sequence and the folded protein, structure, overview
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?
additional information
?
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position of predicted enzyme cleavage sites within the sequence and the folded protein, structure, overview
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?
additional information
?
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recombinant zymogen can be activated by thermolysin
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?
additional information
?
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recombinant zymogen can be activated by thermolysin
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?
additional information
?
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enzyme participates in the degradation of enamel proteins in vivo
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?
additional information
?
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enzyme participates in the degradation of enamel proteins in vivo
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?
