EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.4.21.B10 | - |
Homo sapiens |
3.4.21.B39 | - |
Homo sapiens |
3.4.21.117 | analysis of crystal structure of KLK7: owing to the conformational restrictions of the relatively narrow S1 pocket, the formation of a stabilizing hydrogen bond between the P1-Tyr-OH and the carboxamide of Asn189 has to be mediated by a water molecule. The S2 subsite is less separated from the S4 subsite than in KLK4-6 and less limited in size owing to a different position of the His99 imidazole side chain, which may also contribute to the capacity for the adaptation to P2 side chains of various size | Homo sapiens |
3.4.21.117 | two crystal structures of KLK7 are solved with either of two covalently bound chloromethyl ketone (CMK) inhibitors. Overall, the S1 pocket of KLK7 is larger and more hydrophobic than those of the tryptic KLK4, 5, and 6. The hydrophobicity of the S1 pocket is enhanced by the presence of Ala190 instead of Ser190, and at the bottom of the pocket, Asn189, a polar residue, replaces Asp189, a negatively charged residue. Consistent with specificity, Asn189 insteadof Asp189 would reduce the affinity of KLK7 for basic P1 side chains and allow binding of non-polar residues. The size and shape of the S1 pocket is well suited to accommodate residues with medium and large side chains, explaining the modified chymotryptic specificity. Tyr may be favored over Phe at P1 because of the potential of the carboxyamide group of Asn189 to hydrogen bond to a buried hydroxyl group | Homo sapiens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.B10 | alpha2-Macroglobulin | - |
Homo sapiens | |
3.4.21.B10 | C1-inhibitor | - |
Homo sapiens | |
3.4.21.117 | Ala-Ala-Phe-chloromethylketone | - |
Homo sapiens | |
3.4.21.117 | Suc-Ala-Ala-Pro-Phe-chloromethylketone | - |
Homo sapiens |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.21.B10 | Homo sapiens | - |
- |
- |
3.4.21.B10 | Homo sapiens | Q92876 | - |
- |
3.4.21.B12 | Homo sapiens | Q9Y5K2 | - |
- |
3.4.21.B39 | Homo sapiens | - |
- |
- |
3.4.21.117 | Homo sapiens | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.4.21.B10 | glycoprotein | one glycosylation site | Homo sapiens |
3.4.21.B12 | glycoprotein | one glycosylation site | Homo sapiens |
3.4.21.B39 | glycoprotein | four N-glycosylation sites | Homo sapiens |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.4.21.B39 | stratum corneum | - |
Homo sapiens | - |
3.4.21.117 | breast cancer cell | in contrast to the expression in ovarian cancer, high expression of KLK 7 is strongly associated with good prognosis in breast cancer patients | Homo sapiens | - |
3.4.21.117 | ovary cancer cell | over-expressed in ovarian carcinoma tissues. Elevated KLK 7 mRNA expression in tumor tissue is associated with poorer prognosis for ovarian cancer patients | Homo sapiens | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.B10 | additional information | marked preference for Arg over Lys at position P1. Ala and Met are slightly more preferred at position P1 residues than Lys. Strong specificity for Arg and Lys at the P2 position. Activation cleavage site: EQNK-LVHG | Homo sapiens | ? | - |
? | |
3.4.21.B10 | peptide + H2O | phage-display analysis using optimum hydrolysis conditions reveals a potential cleavage motif for recombinant human KLK6: W(G/T)-A(K)-R(K)-/-(R/K)-A(R/S)-W(G/F). The preferred P1-P19 scissile bond appears to be a dibasic arginine-arginine/arginine-lysine/lysine-arginine doublet | Homo sapiens | ? | - |
? | |
3.4.21.B12 | additional information | 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 | Homo sapiens | ? | - |
? | |
3.4.21.B12 | proform of KLK3 + H2O | Ile-Leu-Ser-Arg-/-Ile-Val activation site | Homo sapiens | ? | - |
? | |
3.4.21.B12 | urokinase-type plasminogen activator + H2O | cleaves after Pro-Arg-Phe-Lys | Homo sapiens | ? | - |
? | |
3.4.21.B12 | urokinase-type plasminogen activator receptor + H2O | cleaves after Thr-Tyr-Ser-Arg as well as in the sequence Val-Gln-Tyr-Arg-/-Ser-Gly | Homo sapiens | ? | - |
? | |
3.4.21.B39 | Ile-Leu-Ser-Arg-Ile-Val | optimal substrate sequences for KLK5 | Homo sapiens | Ile-Leu-Ser-Arg + Ile-Val | - |
? | |
3.4.21.B39 | kallikrein 7 + H2O | Gln-Gly-Asp-Lys-/-Ile-Ile. KLK7 is activated at a low rate | Homo sapiens | ? | - |
? | |
3.4.21.B39 | additional information | KLK5 activates itself efficiently at the cleavage site Ser-Ser-Ser-Arg-/-Ile-Ile. KLK5 is able to induce signaling events via proteinase-activated receptor-2. Strong preference for P1-Arg over Lys (Lys is accepted by the S1 pocket to some extent) and the complete exclusion of chymotrypsin-specific substrates with a Phe or Tyr side chain in P1 position. Preference for Ala and Lys at P2, preference for Gly in P4 | Homo sapiens | ? | - |
? | |
3.4.21.B39 | tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O | best substrate | Homo sapiens | ? | - |
? | |
3.4.21.B39 | tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O | best substrate | Homo sapiens | ? | - |
? | |
3.4.21.117 | acidic-sphingomyelinase + H2O | - |
Homo sapiens | ? | - |
? | |
3.4.21.117 | beta-glucocerebrosidase + H2O | - |
Homo sapiens | ? | - |
? | |
3.4.21.117 | cathelicidin + H2O | - |
Homo sapiens | ? | - |
? | |
3.4.21.117 | insulin beta chain + H2O | the most preferred P1 residue of KLK7 is Tyr, followed by Ala and Met, whereas Phe, Arg, and Lys are ranked quite low. Tyr is favored at S2 over the medium-sized hydrophobic residues Leu, Thr, Met, and Phe. In agreement with these findings, KLK7 cleaves the insulin B-chain after Asn-Gln-His-Leu, Glu-Ala-Leu-Tyr, Gly-Phe-Phe-Tyr, and Arg-Gly-Phe-Phe | Homo sapiens | ? | - |
? | |
3.4.21.117 | additional information | similar to KLK5, KLK7 degrades proteins of corneodesmosomes, which are most likely physiological substrates of KLKs expressed in the stratum corneum of skin | Homo sapiens | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.21.B10 | kallikrein-related peptidase 6 | - |
Homo sapiens |
3.4.21.B10 | KLK6 | - |
Homo sapiens |
3.4.21.B10 | neurosin | - |
Homo sapiens |
3.4.21.B10 | protease M | - |
Homo sapiens |
3.4.21.B10 | serine protease 18 | - |
Homo sapiens |
3.4.21.B10 | serine protease 9 | - |
Homo sapiens |
3.4.21.B12 | EM serine proteinase 1 | - |
Homo sapiens |
3.4.21.B12 | kallikrein-like protein 1 | - |
Homo sapiens |
3.4.21.B12 | KLK4 | - |
Homo sapiens |
3.4.21.B12 | serine protease 17 | - |
Homo sapiens |
3.4.21.B39 | HSC tryptic enzyme | - |
Homo sapiens |
3.4.21.B39 | kallikrein-like protein 2 | - |
Homo sapiens |
3.4.21.B39 | KLK5 | - |
Homo sapiens |
3.4.21.117 | kallikrein 7 | - |
Homo sapiens |
3.4.21.117 | KLK7 | - |
Homo sapiens |