3.4.21.B45: kallikrein 14
This is an abbreviated version!
For detailed information about kallikrein 14, go to the full flat file.
Word Map on EC 3.4.21.B45
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3.4.21.B45
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klk5
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stratum
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desquamation
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corneum
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netherton
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proteinase-activated
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trypsin-like
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kazal-type
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lekti
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corneodesmosomes
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medicine
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kazal
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granulosum
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endocrine-related
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spink6
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diagnostics
- 3.4.21.B45
- klk5
-
stratum
-
desquamation
- corneum
- netherton
-
proteinase-activated
-
trypsin-like
-
kazal-type
- lekti
-
corneodesmosomes
- medicine
-
kazal
-
granulosum
-
endocrine-related
- spink6
- diagnostics
Reaction
proteolytic cleavage of polypeptides =
Synonyms
hK 14, hK14, kallikrein 14, kallikrein-related peptidase 14, KLK14, S01.029, SCTE
ECTree
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Substrates Products
Substrates Products on EC 3.4.21.B45 - kallikrein 14
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REACTION DIAGRAM
Ala-Thr-Pro-Lys-Ile-Phe-Asn + H2O
Ala-Thr-Pro-Lys + Ile-Phe-Asn
19% cleavage after 1 h incubation
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?
collagen alpha1 (XII and XIX) chain precursor + H2O
?
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residues 1838-1841
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?
D-Ile-Pro-Arg-p-nitroanilide + H2O
D-Ile-Pro-Arg + p-nitroaniline
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?
D-Val-Leu-Lys-thiobenzyl ester + H2O
D-Val-Leu-Lys + thiobenzyl alcohol
low activity
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?
GDDSTPSILPAPRGYPGQV + H2O
GDDSTPSILPAPR + GYPGQV
the tethered ligand is GYPGQV
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?
GPNSKGRSLIGRLDTPYGGC + H2O
SLIGRLDTPYGGC + RLDTPYGGC + GPNSKGRSLIG
the tethered ligand is SLIGRL
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?
GTNRSSKGRSLIGKVDGTSHVTGKGVT + H2O
GTNRSSKGR + SLIGKVDGTSHVTGKGVT
the tethered ligand is SLIGKV
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?
HAI-1A + H2O
?
HAI-1A is extensively degraded when the protease:inhibitor stoichiometry is 1:1, or the enzyme is in excess. When the inhibitor is in excess, processing of HAI-1A generates fragments that likely mediate inhibition of pro-hepatocyte growth factor convertases
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?
human proteinase-activated receptor 2 zymogen + H2O
mature human proteinase-activated receptor 2 + ?
unmasking the PAR2 receptor-activating sequence from a peptide precursor
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?
L-Gln-Gly-Asp-Lys-Ile-Ile-Asp + H2O
L-Gln-Gly-Asp-Lys + Ile-Ile-Asp
41% cleavage after 1 h incubation
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?
L-Glu-Thr-Arg-Ile-Ile-Lys + H2O
L-Glu-Thr-Arg + Ile-Ile-Lys
55% cleavage after 1 h incubation
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?
L-Ile-Gln-Ser-Arg-Ile-Val-Gly + H2O
L-Ile-Gln-Ser-Arg + Ile-Val-Gly
97% cleavage after 1 h incubation
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?
L-Ile-Leu-Ser-Arg-Ile-Val-Gly + H2O
L-Ile-Leu-Ser-Arg + Ile-Val-Gly
87% cleavage after 1 h incubation
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?
L-Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
L-Pro-Phe-Arg + 7-amino-4-methylcoumarin
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?
L-Ser-Ser-Ser-Arg-Ile-Ile-Asn + H2O
L-Ser-Ser-Ser-Arg + Ile-Ile-Asn
57% cleavage after 1 h incubation
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?
methoxy-succinyl-Arg-Pro-Tyr-p-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + p-nitroaniline
very low activity
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?
NATLDPRSFLLRNPNDKYE + H2O
NATLDPR + SFLLRNPNDKYE
the tethered ligand is SFLLRN
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?
pro-hepatocyte growth factor + H2O
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the enzyme converts pro-hepatocyte growth factor to the two-chain heterodimer required for Met activation, while higher concentrations degrade the hepatocyte growth factor alpha-chain. When pro-hepatocyte growth factor is in vast excess it is activated by KLK14, and as the substrate concentration increases above a threshold level (protease:substrate ratio above 1:200), hepatocyte growth factor is inactivated
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?
pro-KLK3 + H2O
KLK3 + ?
KLK3 is activated by cleavage after arginine at position 7
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?
proprotein convertase subtilisin/kexin type 5 precursor + H2O
?
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residues 371-375
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?
proteinase-activated receptor 2 zymogen + H2O
mature proteinase-activated receptor 2 + ?
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?
rat proteinase-activated receptor 2 zymogen + H2O
mature rat proteinase-activated receptor 2 + ?
unmasking the PAR2 receptor-activating sequence from a peptide precursor
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?
serin protease inhibitor Kazal-type 5 precursor + H2O
?
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residues 1034-1037
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?
tosyl-Gly-L-Pro-L-Arg-4-nitroanilide + H2O
tosyl-Gly-L-Pro-L-Arg + 4-nitroaniline
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?
vascular endothelial growth factor receptor 3 precursor + H2O
?
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residues 1126-1130
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?
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does not cleave L-Glu-Ser-Ser-Lys-Val-Leu-Asn, L-Ser-Cys-Ser-Gln-Ile-Ile-Asn, L-Glu-Gln-Asn-Lys-Leu-Val-His, L-Gln-Glu-Asp-Lys-Val-Leu-Gly, L-Asp-Thr-Arg-Ala-Ile-Gly, L-Asn-Asp-Thr-Arg-Leu-Asp-Pro, L-Asp-Glu-Asn-Lys-Ile-Ile-Gly, and L-Asp-Gly-Asp-Lys-Leu-Leu-Glu
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?
additional information
?
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does not cleave L-Glu-Ser-Ser-Lys-Val-Leu-Asn, L-Ser-Cys-Ser-Gln-Ile-Ile-Asn, L-Glu-Gln-Asn-Lys-Leu-Val-His, L-Gln-Glu-Asp-Lys-Val-Leu-Gly, L-Asp-Thr-Arg-Ala-Ile-Gly, L-Asn-Asp-Thr-Arg-Leu-Asp-Pro, L-Asp-Glu-Asn-Lys-Ile-Ile-Gly, and L-Asp-Gly-Asp-Lys-Leu-Leu-Glu
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?
additional information
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crucial cascade-mediated function of KLK14 in regulating the coagulation and liquefaction of human semen
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?
additional information
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crucial cascade-mediated function of KLK14 in regulating the coagulation and liquefaction of human semen
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?
additional information
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the enzyme activates the proteinase-activated receptor 2 recombinnatly expressed in rat and in human cells
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?
additional information
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the enzyme activates the proteinase-activated receptor 2 recombinnatly expressed in rat and in human cells
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additional information
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determination of substrate and cleavage site specificities of the enzyme using peptide fused to 4-nitroanilide as substrates, molecular modeling of preferred KLK14 substrates. The enzyme KLK14 displays a preference for Tyr and Trp at the P4 site
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?
additional information
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KLK14 can cleave synthetic peptides representing the cleavage-activation sequences of human proteinase-activated receptors PARs 1, 2 and 4 to unmask a receptor-activating sequence. Substrate specificity, overview. Analysis of processing of synthetic human and rat proteinase-activated receptor 2, PAR2, derived sequences, representing the cleavage activation domain of PAR2, by kallikrein 8 versus kallikrein 14. KLKs 8 and 14 can both cleave the synthetic PAR2 tethered ligand-containing synthetic peptides to unmask a potential receptor-activating sequence, but each KLK exhibits distinct signalling properties via PARs 1 and 2
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additional information
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KLK14 can cleave synthetic peptides representing the cleavage-activation sequences of human proteinase-activated receptors PARs 1, 2 and 4 to unmask a receptor-activating sequence. Substrate specificity, overview. Analysis of processing of synthetic human and rat proteinase-activated receptor 2, PAR2, derived sequences, representing the cleavage activation domain of PAR2, by kallikrein 8 versus kallikrein 14. KLKs 8 and 14 can both cleave the synthetic PAR2 tethered ligand-containing synthetic peptides to unmask a potential receptor-activating sequence, but each KLK exhibits distinct signalling properties via PARs 1 and 2
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?