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Literature summary for 3.4.21.B45 extracted from

  • Reid, J.C.; Bennett, N.C.; Stephens, C.R.; Carroll, M.L.; Magdolen, V.; Clements, J.A.; Hooper, J.D.
    In vitro evidence that KLK14 regulates the components of the HGF/Met axis, pro-HGF and HGF-activator inhibitor 1A and 1B (2016), Biol. Chem., 397, 1299-1305 .
    View publication on PubMed
Search for more literature for 3.4.21.B45

Cloned(Commentary)

Cloned (Comment) Organism
expression in Spodoptera frugiperda Sf9 cells Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
HAI-1A no inhibition of KLK14 up to equimolar concentrations (5 nm) of enzyme and inhibitor. As the reaction shifts to containing excess inhibitor, KLK14 is mildly inhibited, with inhibition of 35% obtained when HAI-1A is present at 10fold excess over protease Homo sapiens
HAI-1B no inhibition of KLK14 up to equimolar concentrations (5 nm) of enzyme and inhibitor. As the reaction shifts to containing excess inhibitor, KLK14 is mildly inhibited, with inhibition of 26% obtained when HAI-1B is present at 10fold excess over protease Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.258
-
 QAR-7-amido-4-methylcoumarin 37°C, pH 8.8 Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pro-hepatocyte growth factor + H2O Homo sapiens 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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9P0G3
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the lower catalytic efficiency observed against a peptide substrate for insect cell expressed KLK14, compared with the previously reported yeast expressed protease, is possibly due to N-glycosylation present on the former but not the latter Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Homo sapiens ?
-
 ?
pro-hepatocyte growth factor + H2O 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 Homo sapiens ?
-
 ?
QAR-7-amido-4-methylcoumarin + H2O
-
 Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
KLK14
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
12.1
-
 QAR-7-amido-4-methylcoumarin 37°C, pH 8.8 Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.8
-
 assay at Homo sapiens

General Information

General Information Comment Organism
physiological function the enzyme regulates the components of the hepatocyte growth factor/Met axis, pro-hepatocyte growth factor and hepatocyte growth factorF-activator inhibitor 1A and 1B Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
46.9
-
 QAR-7-amido-4-methylcoumarin 37°C, pH 8.8 Homo sapiens