Information on EC 3.4.21.117 - stratum corneum chymotryptic enzyme and Organism(s) Homo sapiens and UniProt Accession P49862

Fibronectin + H2O

?

human pro-interleukin 1beta + H2O

human interleukin beta1 + ?

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

-

?

Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 + H2O

?

-

a fluorogenic peptide substrate

683126, 683325

-

?

MeO-succinly-Arg-Pro-Tyr-4-nitroanilide + H2O

?

-

-

?

methoxy-succinyl-Ala-Ala-Pro-Met-4-nitroanilide + H2O

methoxy-succinyl-Ala-Ala-Pro-Met + 4-nitroaniline

methoxy-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O

methoxy-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline

methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide + H2O

methoxy-succinyl-Arg-Pro-Tyr + 4-nitroaniline

N-carbobenzoxy-Gly-Pro-Arg-4-nitroanilide + H2O

N-carbobenzoxy-Gly-Pro-Arg + 4-nitroaniline

N-carbobenzoxy-Val-Gly-Arg-4-nitroanilide + H2O

N-carbobenzoxy-Val-Gly-Arg + 4-nitroaniline

oxidized bovine insulin B chain + H2O

peptides + (Tyr)26

-

recombinant enzyme

product identification, cleavage sites are: Leu6-cysteic acid7, Tyr16-Leu17, Phe25-Tyr26, Tyr26-Tr27

?

polypeptide + H2O

peptides

12 entries

pro-matrix metalloproteinase-2 + H2O

?

-

KLK7 degrades, but does not activate, pro-matrix metalloproteinase-2

-

?

pro-matrix metalloproteinase-9 + H2O

matrix metalloproteinase-9

-

KLK7 degrades and activates pro-matrix metalloproteinase-9, cleavage occurs between Tyr443 and Gly444

the product is a truncated, active matrix metalloproteinase-9 lacking the C-terminal hemopexin domains which is not generated by other proteases

-

?

Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O

Suc-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin

-

707623

-

?

succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O

succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline

-

chromogenic substrate

647343

-

?

succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O

succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin

-

-

?

succinyl-Phe-Leu-Phe-4-nitroanilide + H2O

succinyl-Phe-Leu-Phe + 4-nitroaniline

succinyl-Val-Pro-Phe-4-nitroanilide + H2O

succinyl-Val-Pro-Phe + 4-nitroaniline

additional information

?

-

31 entries

CYR61 + H2O

?

-

-

?

midkine + H2O

?

-

-

?

polypeptide + H2O

peptides

tenascin-C + H2O

?

-

-

?

E-cadherin + H2O

?

-

kallikrein 7 degrades extracellular matrix proteins, and enhances pancreatic cancer cell invasion by shedding E-cadherin, overview

-

?

Fibronectin + H2O

?

-

kallikrein degrades components of the extracellular matrix

-

?

polypeptide + H2O

peptides

8 entries

additional information

?

-

Ca2+

sodium chloride

inhibits the enzyme to over 60% at up to 1 M

Sodium citrate

inhibits the enzyme at up to 750 mM, but not at higher concentrations

Sodium sulfate

inhibits the enzyme at up to 1000 mM, but not at higher concentrations

Ca2+

-

683126, 683325

1-(2-bromobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole

-

1-(2-chlorobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole

-

2-(2-fluoro-phenyl)-5,6,7,8-tertrahydro-benzol[4,5]thieno[2,3-d][1,3]oxazin-4-one

-

Abz-KLASSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Abz-KLDSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Abz-KLESSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Abz-KLGSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Abz-KLHSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Abz-KLISSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Abz-KLKSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Abz-KLLSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Abz-KLMSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Abz-KLNSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Abz-KLPSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Abz-KLQSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Abz-KLRSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Abz-KLSSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Abz-KLTSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Abz-KLVSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Abz-KLWSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

-

Ala-Ala-Phe-chloromethyl ketone

-

Ala-Ala-Phe-chloromethylketone

-

Cu2+

DMSO

catalytic activity of the protease decreases with increasing DMSO concentration

FEIIKKYQ

-

GKCLFSEPPICFPN

peptide inhibitor based on sunflower trypsin inhibitor-1

GKCLFSNPPICFPN

peptide inhibitor based on sunflower trypsin inhibitor-1, displays at least 1000fold selectivity over several proteases that are related by function (KLK5 and KLK14) or specificity (chymotrypsin)

GKCLFSSPPICFPN

peptide inhibitor based on sunflower trypsin inhibitor-1

LEKTI domain 6

i.e. lympho-epithelial Kazaltype-related inhibitor domain 6, specific inhibition, interaction and binding structure analysis, overview

-

succinyl-Ala-Ala-Pro-Phe-chloromethyl ketone

-

Zn2+

(4R)-4-benzyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-(1-naphthyl)methyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2] imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-(4-benzyloxy)benzyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5H-pyrido [10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-(4-hydroxyphenyl)-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5H-pyrido [10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-benzyl-2-(2,4-dimethylphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5-one

-

cytotoxic effect

(4S)-4-benzyl-2-(2,5-dihydroxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo-[4,5-d][1,3]diazepin-5-one

-

(4S)-4-benzyl-2-(2,5-dimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5-one

-

cytotoxic effect

(4S)-4-benzyl-2-(2-hydroxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo-[4,5-d][1,3]diazepin-5-one

-

(4S)-4-benzyl-2-(2-methoxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-benzyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-benzyl-2-(2-methylpropyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-benzyl-2-(3,4,5-trimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2] imidazo[4,5-d][1,3]diazepin-5-one

-

cytotoxic effect

(4S)-4-benzyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5-one

-

mechanism of inhibition, modeling, overview. Cytotoxic effect

(4S)-4-benzyl-2-(3,4-dimethoxyphenyl)-4,5-dihydro-3H-pyrido [10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-ol

-

(4S)-4-benzyl-2-(3-hydroxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo-[4,5-d][1,3]diazepin-5-one

-

(4S)-4-benzyl-2-(3-methoxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-benzyl-2-(3-methylphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-benzyl-2-(4-bromophenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-benzyl-2-(4-methoxyphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-benzyl-2-(4-methylphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-benzyl-2-(4-nitrophenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-benzyl-2-(pyridin-3-yl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-benzyl-2-phenyl-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-benzyl-3,4-dihydro-1H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepine-2,5-dione

-

(4S)-4-benzyloxymethyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2] imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-benzyloxymethyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5H-pyrido [10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-hydroxymethyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2] imi-dazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-methyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]-imidazo[4,5-d][1,3]diazepin-5-one

-

(4S)-4-methyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2] imidazo[4,5-d][1,3]diazepin-5-one

-

(S)-4-benzyl-2-(3,4-dimethoxyphenyl)-3-methyl-3H-pyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5(4H)-one

-

(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-1H-pyrrole-2-carboxamide

-

(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-2-methylbenzamide

-

(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-2-phenylacetamide

-

(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-3,4-dimethoxybenzamide

-

(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-3-phenylpropanamide

-

(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)benzamide

-

(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)cinnamamide

-

(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)isonicotinamide

-

(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)picolinamide

-

Ala-Ala-Phe-chloromethylketone

-

alpha1-Aantichymotrypsin

-

99.6% inhibition at 0.00015 mM

-

alpha1-Macroglobulin

-

44.2% inhibition at 0.00015 mM

-

Alpha1-proteinase inhibitor

-

89.6% inhibition at 0.00015 mM

-

antileukoprotease

-

Aprotinin

chymostatin

Eglin c

-

99.8% inhibition at 0.00015 mM

elafin

-

33.4% inhibition at 0.0015 mM

-

LEKTI

LEKTI fragments

-

i.e. lympho-epithelial Kazaltype-related inhibitor fragments, furin-derived and secreted in cultured keratinocytes and in the epidermis, specifically inhibit KLK5, KLK7, and KLK14 and control desquamation through a pH-dependent interaction, overview

-

pepstatin A

-

weak inhibition, 23.6% inhibition at 0.1 mM

Soybean trypsin inhibitor

-

99.6% inhibition at 0.00015 mM

-

Suc-Ala-Ala-Pro-Phe-chloromethylketone

-

Zn2+

additional information

6 entries

-

kallikrein 5

activates proform of kallikrein 7

665944

-

plasmin

-

-

Thermolysin

-

-

additional information

4 entries

-

0.0009

Abz-AIKFFSA-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0043

Abz-ALFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0032

Abz-FLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.002

Abz-GFSPFRSSRI-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.069

Abz-GFSPFRSSRIGEIKEETT-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0062

Abz-GLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0034

Abz-HLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0027

Abz-ILFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0035

Abz-KAFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.003

Abz-KFFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0018

Abz-KLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0034

Abz-KLYSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0025

Abz-KPFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0019

Abz-KVFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0027

Abz-KYFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0046

Abz-LLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0004

Abz-MISLMKRP-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0017

Abz-NLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0052

Abz-QLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0041

Abz-RLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0021

Abz-VLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0059

Ac-ED(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)KPILFRLGK(4-(4-dimethylaminophenylazo)benzoic acid)E-NH2

kcat/KM: 170000/Msec

0.048

Ac-EFKPILWRLGC-(6-(9-oxo-9H-acridin-10-yl)-hexanoate)E-NH2

Vmax: 12 nM/sec

0.048

KHLF-4-nitroanilide

pH 8.0, 23°C

0.044

KHLY-4-nitroanilide

pH 8.0, 23°C

0.0443

L-Phe-7-amido-4-methylcoumarin

in 50 mM HEPES, pH 7.5, 150 mM NaCl, 0.005% Tween 20, at 25°C

0.0402

L-Tyr-7-amido-4-methylcoumarin

in 50 mM HEPES, pH 7.5, 150 mM NaCl, 0.005% Tween 20, at 25°C

0.0159

Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2

-

0.65

methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide

pH 8.0, 23°C

0.304 - 0.43

methoxy-succinyl-Arg-Pro-Tyr-7-amido-4-methylcoumarin

0.0402 - 0.0443

Phe-7-amido-4-methylcoumarin

0.049

QHLY-4-nitroanilide

pH 8.0, 23°C

0.08

acetyl-Phe-Val-Arg-4-nitroanilide

-

pH 8.0, 37°C

0.65

methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide

-

pH 8.0, 37°C

0.22

succinyl-Phe-Leu-Phe-4-nitroanilide

-

pH 8.0, 37°C

additional information

-

-

0.03

Abz-AIKFFSA-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.1

Abz-ALFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.09

Abz-FLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.03

Abz-GFSPFRSSRI-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

1

Abz-GFSPFRSSRIGEIKEETT-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.03

Abz-GLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.1

Abz-HLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.06

Abz-ILFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.02

Abz-KAFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.02

Abz-KFFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.1

Abz-KLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.85

Abz-KLYSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.02

Abz-KPFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.04

Abz-KVFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.02

Abz-KYFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.07

Abz-LLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.01

Abz-MISLMKRP-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.28

Abz-NLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.15

Abz-QLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.13

Abz-RLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.13

Abz-VLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.48

Ac-EFKPILWRLGC-(6-(9-oxo-9H-acridin-10-yl)-hexanoate)E-NH2

-

7.4

KHLF-4-nitroanilide

pH 8.0, 23°C

12

KHLY-4-nitroanilide

pH 8.0, 23°C

0.000016

L-Phe-7-amido-4-methylcoumarin

in 50 mM HEPES, pH 7.5, 150 mM NaCl, 0.005% Tween 20, at 25°C

0.000033

L-Tyr-7-amido-4-methylcoumarin

in 50 mM HEPES, pH 7.5, 150 mM NaCl, 0.005% Tween 20, at 25°C

1.2

methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide

pH 8.0, 23°C

0.34 - 24.5

methoxy-succinyl-Arg-Pro-Tyr-7-amido-4-methylcoumarin

0.000016 - 0.000033

Phe-7-amido-4-methylcoumarin

7.7

QHLY-4-nitroanilide

pH 8.0, 23°C

0.04

acetyl-Phe-Val-Arg-4-nitroanilide

-

pH 8.0, 37°C

1.2

methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide

-

pH 8.0, 37°C

0.05

succinyl-Phe-Leu-Phe-4-nitroanilide

-

pH 8.0, 37°C

additional information

-

-

29

Abz-AIKFFSA-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

22

Abz-ALFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

27

Abz-FLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

13

Abz-GFSPFRSSRI-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

14

Abz-GFSPFRSSRIGEIKEETT-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

5

Abz-GLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

30

Abz-HLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

21

Abz-ILFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

6.3

Abz-KAFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

5.7

Abz-KFFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

55

Abz-KLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

250

Abz-KLYSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

6.4

Abz-KPFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

20

Abz-KVFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

6

Abz-KYFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

15

Abz-LLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

23

Abz-MISLMKRP-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

165

Abz-NLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

29

Abz-QLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

32

Abz-RLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

62

Abz-VLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

150

KHLF-4-nitroanilide

pH 8.0, 23°C

270

KHLY-4-nitroanilide

pH 8.0, 23°C

1.8

methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide

pH 8.0, 23°C

0.79 - 80.8

methoxy-succinyl-Arg-Pro-Tyr-7-amido-4-methylcoumarin

160

QHLY-4-nitroanilide

pH 8.0, 23°C

0.002

Abz-KLASSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0032

Abz-KLDSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.003

Abz-KLESSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0022

Abz-KLGSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0013

Abz-KLHSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0002

Abz-KLISSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0003

Abz-KLKSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0015

Abz-KLLSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.001

Abz-KLMSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0011

Abz-KLNSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0022

Abz-KLPSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0022

Abz-KLQSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0016

Abz-KLRSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0018

Abz-KLSSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0023

Abz-KLTSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0017

Abz-KLVSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.001

Abz-KLWSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine

pH 7.5, 37°C

0.0006

Cu2+

0.0000031

GKCLFSEPPICFPN

pH 8.0, 23°C

0.00000014

GKCLFSNPPICFPN

pH 8.0, 23°C

0.0000014

GKCLFSSPPICFPN

pH 8.0, 23°C

0.01

Zn2+

0.000063

antileukoprotease

-

pH 8.0, 37°C

-

0.000027

Aprotinin

-

pH 8.0, 37°C

0.00000033

Eglin c

-

pH 8.0, 37°C

0.0016

elafin

-

pH 8.0, 37°C

-

0.0000348

LEKTI

-

additional information

-

inhibition kinetics with LEKTi fragments, overview

-

0.00039

1-(2-bromobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole

Homo sapiens

pH not specified in the publication, temperature not specified in the publication

0.0012

1-(2-chlorobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole

Homo sapiens

pH not specified in the publication, temperature not specified in the publication

0.00007

2-(2-fluoro-phenyl)-5,6,7,8-tertrahydro-benzol[4,5]thieno[2,3-d][1,3]oxazin-4-one

Homo sapiens

-

0.026

LEKTI domain 6

Homo sapiens

-

-

0.0959

(4R)-4-benzyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one

Homo sapiens

-

pH 8..0, 37°C

0.0839

(4S)-4-benzyl-2-(2,4-dimethylphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5-one

Homo sapiens

-

pH 8..0, 37°C

0.0809

(4S)-4-benzyl-2-(2,5-dimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5-one

Homo sapiens

-

pH 8..0, 37°C

0.057

(4S)-4-benzyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one

Homo sapiens

-

pH 8..0, 37°C

0.0557

(4S)-4-benzyl-2-(3,4,5-trimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2] imidazo[4,5-d][1,3]diazepin-5-one

Homo sapiens

-

pH 8..0, 37°C

0.0335

(4S)-4-benzyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5-one

Homo sapiens

-

pH 8..0, 37°C

0.1248

(4S)-4-benzyl-2-(3-hydroxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo-[4,5-d][1,3]diazepin-5-one

Homo sapiens

-

pH 8..0, 37°C

0.072

(4S)-4-benzyl-2-(4-methoxyphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one

Homo sapiens

-

pH 8..0, 37°C

0.068

(4S)-4-benzyl-2-(4-methylphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one

Homo sapiens

-

pH 8..0, 37°C

0.1354

(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-2-methylbenzamide

Homo sapiens

-

pH 8..0, 37°C

0.1492

(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-2-phenylacetamide

Homo sapiens

-

pH 8..0, 37°C

additional information

5.6

assay at

7.5

5.5

-

proteolysis of corneodesmosin

7

-

assay at

647348

7.2

-

assay at

7.4

-

assay at

7.5

-

assay at

7.5 - 8.5

-

assay at

8

additional information

-

enzyme shows optimal activity at neutral pH, and retains significant activity at acidic pH

5.5 - 8

-

no activity at pH 4.0, highest activity at 8.0

25

assay at

25 - 37

assay at

37

assay at

25

-

assay at

37

-

assay at

647343, 647345, 647346, 647348, 683126, 683325, 696964, 731754

-

from ovarian cancer patients

-

enzyme expression analysis in 155 patients, overview

breast carcinoma cell line, enzyme is upregulated by estrogens and slightly by glucocorticoids

647332

central nervous system

-

-

-

-

enzyme expression

-

lung adenocarcinoma cell

-

lymphoblastic leukemia cell

-

-

-

-

ovarian carcinoma cell

prostate cancer cell line

overexpression of the enzyme

-

-

pancreatic cancer cell

-

-

-

-

-

-

-

-

-

testicular carcinoma cell

-

-

-

-

-

-

breast carcinoma cell

cervical adenocarcinoma cell

-

breast cancer patients with KLK7 positive tumors have relatively shorter disease-free survival and overall survival than patients with KLK7 negative tumors

-

-

-

decrease in level of kallikrein 7 in patients with Alzheimer's disease and patients with frontotemporal dementia

664614

cervical cancer cell line

-

increased expression of kallikrein 7 and decreased expression of its inhibitor antileukoprotease might play an important role in cervical adenocarcinoma development

666518

-

50% of the primary and 50% of the established cervical cancer cell lines express kallikrein 7

665069

cervical carcinoma cell

cervical squamous cell carcinoma cell line

-

cervical intraepithelial neoplasia, cervicitis, squamous cervical carcinomas, and cervical adenocarcinomas

708770

colonic adenocarcinoma cell

-

high expression of the enzyme

665069

-

-

colon cancer cell lines and colonic tumors

-

colorectal cancer cell

-

semi-quantitative RT-PCR determination and immunohistochemical analysis

710599

commercial preparation

-

recombinant pro-kallikrein 7

corneocyte

-

plantar

-

-

microglial and oligodendroglia

-

-

intracranial tumor cell

-

keratinocyte cell line

-

the transcriptional changes 3 and 60 h after TNF treatment of normal, human papillomaviruses 16- and human papillomaviruses 18-immortalized keratinocytes is analyzed by microarray analysis. KLK7 shows a differential expression pattern associated with the differential response to TNF. KLK7 expression pattern is is equally expressed in TNF-treated or untreated human papillomaviruses 18-immortalized cells but it is not detected in normal primary keratinocytes or human papillomaviruses 16-immortalized cells

696984

kidney

-

KLK7 expression in the normal kidney shows granular cytoplasmic expression in tubules (stronger intensity in distal than proximal) and no expression in the mesangium

707621

kidney cancer cell

-

KLK7 shows strong expression in low grade in contrast to high grade clear cell renal cell carcinoma, RCC, overview. The expression of KLK7 can distinguish between oncocytoma and chromophobe RCC

707621

lung

lung adenocarcinoma cell

-

expression of KLK7 is decreased

663866

lung cancer cell

oral squamous cell carcinoma cell

-

KLK7 is strongly expressed in the tissue of patients with squamous cell carcinoma and differentiated tumors

-

prostate cancer cell line

-

in the oral cavity, strong reactivity for KLK7 in human oral squamous cell carcinoma tissues, immunohistochemical analysis, overview

692566

ovarian carcinoma cell

-

-

KLK7 and KLK5 are expressed in pancreatic tissues by acinar cells. Motifs in the promoter of KLK7 and KLK 5 are identified for transcription factors which confer pancreatic expression

696538

pancreatic cancer cell

-

-

ALP is significantly decreased in prostate cancers compared with that in benign prostate epithelial cells. Immunohistochemical expression of kallikrein 7 is observed in prostate epithelial cells, whereas little or no staining is observed in prostate cancer. Western blot analysis reveals that hK7 and antileukoprotease are decreased in malignant prostate epithelium

-

-

-

-

significantly increased serum enzyme levels in cervical cancer patients compared to healthy individuals and patients with benign cervical disease

additional information

-

-

-

the enzyme is secreted

-

731402, 732451

evolution

human kallikrein-related peptidase 7 is one member from a cluster of 15 serine peptidases of the chymotrypsin-like S1A family clan PA(S) sharing a high degree of identity and localized at human chromosome locus 19q13.4

physiological function

4 entries

evolution

-

human tissue kallikrein-7 is a chymotryptic serine protease member of tissue kallikrein family.

malfunction

physiological function

5 entries

P49862 pBLAST

KLK7_HUMAN

253

0

27525

Swiss-Prot

Show Sequence

Secretory Pathway (Reliability: 1)

12 entries

25000

-

x * 25000, SDS-PAGE

647342, 647343

?

x * 30000, gylcosylated form, x * 28000 and x * 20000, nonglycosylated froms, SDS-PAGE. X * 25000, calculated from sequence

?

-

x * 25000, SDS-PAGE

647342, 647343

additional information

5 entries

glycoprotein

proteolytic modification

glycoprotein

-

647343

proteolytic modification

kallikrein 7 bound to inhibitors succinyl-Ala-Ala-Pro-Phe-chloromethyl ketone and Ala-Ala-Phe-chloromethyl ketone, sitting-drop vapor diffusion method at 18°C, 0.001 ml protein solution, containing 7 mg/ml enzyme-inhibitor complex, is mixed with 0.001 ml reservoir solution containing 100 mM [bis(2-hydroxyethyl)amino]tris(hydroxymethyl)-methane-HCl, pH 6.0, 25% PEG 3350, and 2.5 M Li2SO4, equilibration against reservoir solution, X-ray diffraction structure determination and analysis at 1.0-2.5 A resolution

purified recombinant enzyme bound to specific inhibitor LEKTI domain 6, 8 mg/ml protein in sodium phosphate buffer, pH 7.5, with a reservoir solution containing 3.2 M ammonium sulfate in 0.1 M HEPES, pH 7.0, X-ray diffraction structure determination and anaylsis at 2.8 A resolution

sitting drop vapour diffusion method, with 100 mM [bis(2-hydroxyethyl)amino]tris(hydroxymethyl)-methane-HCl, pH 6.0, 25% PEG 3350, and 2.5 M Li2SO4 or with 100 mM sodium cacodylate, pH 6.5, 200 mM magnesium acetate, and 30% (v/v) 2-methyl-2,4-pentanediol

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

-

purified recombinant His-tagged enzyme, sitting-drop vapour-diffusion method, 22°C, 0.0001 ml of 8 mg/ml protein in 50 mM sodium phosphate buffer, pH 7.5, mixed with 0.0001 ml of reservoir solution, X-ray diffraction structure determination and anaylsis at 2.8 A resolution

-

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

-

analysis

ELISA-type immunoassay for human kallikrein quantification

H41F

H99A

S195A

mutation in catalytic triad, shows residual catalytic activity

S195A/D102N

inactive

additional information

-

nickel-nitrilotriacetic acid-Sepharose column chromatography and benzamidine-Sepharose column chromatography

recombinant

recombinant and native enzyme

-

-

partially

-

recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)SS periplasm by nickel affinity chromatography

-

recombinant kallikrein 7 from HEK-293F cell culture supernatant by ultrafiltration and dialysis, anion exchange chromatography, and heparin affinity chromatography, followed by metal affinity on an iminodiacetic acid epoxy resin column, elution with L-histidine from the latter column, to homogeneity

-

cloning from keratinocyte library, DNA and RNA sequence determination and analysis, expression of the enzyme in its proform in murine C127 cells, enzyme activation by trypsin

647344

DNA sequence determination and analysis, gene KLK7 mapps to chromosomal locus 19q13.3-13.4, human kallikrein gene family locus

647349

expressed as a His-tagged fusionprotein in Escherichia coli

expressed in Escherichia coli and in a baculovirus-insect cell system

expressed in Escherichia coli M15(pREP4) cells

680680

expression in Pichia pastoris

expression in Saccharomyces cerevisiae

gene KLK7, expression in Escherichia coli with secretion to the the bacterial periplasm

gene KLK7, genetic organization and structure of the kallikrein gene family, clustered on chromosome 19q13.3-q13.4

647332

gene KLK7, overexpression in breast cancer cell lines aMCF-7, OVMZ-6, and MDA-231, quantitative expression analysis in wild-type native cells and in transfected cells, overview

664622

recombinant kallikrein 7 is produced in HEK 293T cells

664621

the gene encoding the enzyme is localized at chromosome locus 19q13.4, recombinant expression in an insect cell line using the baculovirus transfection system

development of an in situ quantitative method of protein expression detection

-

677579

enzyme overexpression in HT-29 cells resulting in increased cell proliferation

-

731402

expressed in the neuroblastoma cell line SH-SY5Y

-

678518

expression analysis by quantitative RT PCR analysis

-

692566

gene KLK7, encoded on chromosome 19, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)SS with secretion to the the bacterial periplasm

-

gene KLK7, expression profiling in BxPC-3 cells from pancreatic adenocarcinomas

-

gene KLK7, stable expression of pro-kallikrein 7 in HEK-293F cells, secretion of the recombinant protein to the cell culture supernatant, activation of the recombinant enzyme by thermolysin

-

KLK genes are located on chromosome 19q13.4

-

710599

stable overexpression of KLK7-253 in SKOV-3 cells, leading to formation of multicellular aggregates, MCAs, that promote cell survival and chemoresistance, with involvement of KLK7 and integrin-regulated cell adhesion. KLK7-253 cells form MCAs invade into mesothelial cell monolayers

-

707990

transgenic mice overexpressing human scce-gene. Epidermal hyperproliferation and decreased skin barrier function in mice overexpressing stratum corneum chymotryptic enzyme

-

663555

increased extracellular calcium-induced KLK7 mRNA expression and protein release in epidermal keratinocyte. Increased protease activity and differential processing of cathelicidin accompanies increased KLK expression. 1,25(OH)2VD3 increases KLK expression independently of differentiation in keratinocytes

-

709408

KLK7 expression is decreased in prostate cancer cells compared to normal benign prostate cells

-

-

diagnostics

medicine

molecular biology

an activity assay for human kallikrein 7 is developed using a blue-fluorescent acridone dye, featuring a remarkably long lifetime that can be quenched by either of the 2 natural amino acids, tyrosine and tryptophan. Incorporating this probe and 1 of the quenching amino acids on either side of the scissile bond of the substrate peptide makes it possible to monitor the enzymatic activity by quantifying the increase in the fluorescence lifetime signal. A systematic investigation of substrate structures leads to a homogenous, microplate-based, compound profiling assay that yields inhibitory constants down into the single-digit nanomolar range

diagnostics

medicine

molecular biology

Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.

The SWISS-PROT protein knowledgebase and its supplement TrEMBL

Nucleic Acids Res.

31

365-370

2003

Homo sapiens (P49862)

12520024

647332

Yousef, G.M.; Diamandis, E.P.

The new human tissue kallikrein gene family: structure, function, and association to disease

Endocr. Rev.

22

184-204

2001

Homo sapiens (P49862)

11294823

647342

Lundstrom, A.; Egelrud, T.

Stratum corneum chymotryptic enzyme: a proteinase which may be generally present in the stratum corneum and with a possible involvement in desquamation

Acta Derm. Venereol.

71

471-474

1991

Homo sapiens

1685827

647343

Egelrud, T.

Purification and preliminary characterization of stratum corneum chymotryptic enzyme: a proteinase that may be involved in desquamation

J. Invest. Dermatol.

101

200-204

1993

Homo sapiens

8393902

647344

Hansson, L.; Stromqvist, M.; Backman, A.; Wallbrandt, P.; Carlstein, A.; Egelrud, T.

Cloning, expression, and characterization of stratum corneum chymotryptic enzyme. A skin-specific human serine proteinase

J. Biol. Chem.

269

19420-19426

1994

Homo sapiens (P49862), Homo sapiens

8034709

Skytt, A.; Stromqvist, M.; Egelrud, T.

Primary substrate specificity of recombinant human stratum corneum chymotryptic enzyme

Biochem. Biophys. Res. Commun.

211

586-589

1995

Homo sapiens

7794273

Franzke, C.W.; Baici, A.; Bartels, J.; Christophers, E.; Wiedow, O.

Antileukoprotease inhibits stratum corneum chymotryptic enzyme. Evidence for a regulative function in desquamation

J. Biol. Chem.

271

21886-21890

1996

Homo sapiens

8702990

647347

Tanimoto, H.; Underwood, L.J.; Shigemasa, K.; Yan Yan, M.S.; Clarke, J.; Parmley, T.H.; O'Brien, T.J.

The stratum corneum chymotryptic enzyme that mediates shedding and desquamation of skin cells is highly overexpressed in ovarian tumor cells

Cancer

86

2074-2082

1999

Homo sapiens

10570434

647348

Nylander-Lundqvist, E.; Egelrud, T.

Formation of active IL-1 beta from pro-IL-1 beta catalyzed by stratum corneum chymotryptic enzyme in vitro

Acta Derm. Venereol.

77

203-206

1997

Homo sapiens

9188871

647349

Yousef, G.M.; Scorilas, A.; Magklara, A.; Soosaipillai, A.; Diamandis, E.P.

The KLK7 (PRSS6) gene, encoding for the stratum corneum chymotryptic enzyme is a new member of the human kallikrein gene family - genomic characterization, mapping, tissue expression and hormonal regulation

Gene

254

119-128

2000

Homo sapiens (P49862), Homo sapiens

10974542

663555

Ny, A.; Egelrud, T.

Epidermal hyperproliferation and decreased skin barrier function in mice overexpressing stratum corneum chymotryptic enzyme

Acta Derm. Venereol.

84

18-22

2004

Homo sapiens

15040472

663866

Planque, C.; de Monte, M.; Guyetant, S.; Rollin, J.; Desmazes, C.; Panel, V.; Lemarie, E.; Courty, Y.

KLK5 and KLK7, two members of the human tissue kallikrein family, are differentially expressed in lung cancer

Biochem. Biophys. Res. Commun.

329

1260-1266

2005

Homo sapiens

15766562

664272

Tan, O.L.; Whitbread, A.K.; Clements, J.A.; Dong, Y.

Kallikrein-related peptidase (KLK) family mRNA variants and protein isoforms in hormone-related cancers: do they have a function?

Biol. Chem.

387

697-705

2006

Homo sapiens

16800730

664273

Prezas, P.; Arlt, M.J.; Viktorov, P.; Soosaipillai, A.; Holzscheiter, L.; Schmitt, M.; Talieri, M.; Diamandis, E.P.; Krueger, A.; Magdolen, V.

Overexpression of the human tissue kallikrein genes KLK4, 5, 6, and 7 increases the malignant phenotype of ovarian cancer cells

Biol. Chem.

387

807-811

2006

Homo sapiens

16800744

664614

Diamandis, E.P.; Scorilas, A.; Kishi, T.; Blennow, K.; Luo, L.Y.; Soosaipillai, A.; Rademaker, A.W.; Sjogren, M.

Altered kallikrein 7 and 10 concentrations in cerebrospinal fluid of patients with Alzheimers disease and frontotemporal dementia

Clin. Biochem.

37

230-237

2004

Homo sapiens

14972646

664621

Kishi, T.; Soosaipillai, A.; Grass, L.; Little, S.P.; Johnstone, E.M.; Diamandis, E.P.

Development of an immunofluorometric assay and quantification of human kallikrein 7 in tissue extracts and biological fluids

Clin. Chem.

50

709-716

2004

Homo sapiens (P49862), Homo sapiens

14764643

664622

Baretton, G.; Luther, T.; Tjan-Heijnen, V.C.; Talieri, M.; Schmitt, M.; Sweep, F.C.; Span, P.N.; Magdolen, V.

Quantitative reverse transcription-PCR assay for detection of mRNA encoding full-length human tissue kallikrein 7: prognostic relevance of KLK7 mRNA expression in breast cancer

Clin. Chem.

52

1070-1079

2006

Homo sapiens (P49862), Homo sapiens

16627559

665069

Santin, A.D.; Cane, S.; Bellone, S.; Bignotti, E.; Palmieri, M.; De Las Casas, L.E.; Roman, J.J.; Anfossi, S.; OBrien, T.; Pecorelli, S.

The serine protease stratum corneum chymotryptic enzyme (kallikrein 7) is highly overexpressed in squamous cervical cancer cells

Gynecol. Oncol.

94

283-288

2004

Homo sapiens

15297163

665944

Caubet, C.; Jonca, N.; Brattsand, M.; Guerrin, M.; Bernard, D.; Schmidt, R.; Egelrud, T.; Simon, M.; Serre, G.

Degradation of corneodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7

J. Invest. Dermatol.

122

1235-1244

2004

Homo sapiens (P49862)

15140227

665947

Vasilopoulos, Y.; Cork, M.J.; Murphy, R.; Williams, H.C.; Robinson, D.A.; Duff, G.W.; Ward, S.J.; Tazi-Ahnini, R.

Genetic association between an AACC insertion in the 3UTR of the stratum corneum chymotryptic enzyme gene and atopic dermatitis

J. Invest. Dermatol.

123

62-66

2004

Homo sapiens (P49862), Homo sapiens

15191543

666518

Tian, X.; Shigemasa, K.; Hirata, E.; Gu, L.; Uebaba, Y.; Nagai, N.; OBrien, T.J.; Ohama, K.

Expression of human kallikrein 7 (hK7/SCCE) and its inhibitor antileukoprotease (ALP/SLPI) in uterine endocervical glands and in cervical adenocarcinomas

Oncol. Rep.

12

1001-1006

2004

Homo sapiens

15492784

666961

Talieri, M.; Diamandis, E.P.; Gourgiotis, D.; Mathioudaki, K.; Scorilas, A.

Expression analysis of the human kallikrein 7 (KLK7) in breast tumors: A new potential biomarker for prognosis of breast carcinoma

Thromb. Haemost.

91

180-186

2004

Homo sapiens

14691584

677579

Psyrri, A.; Kountourakis, P.; Scorilas, A.; Markakis, S.; Camp, R.; Kowalski, D.; Diamandis, E.P.; Dimopoulos, M.A.

Human tissue kallikrein 7, a novel biomarker for advanced ovarian carcinoma using a novel in situ quantitative method of protein expression

Ann. Oncol.

19

1271-1277

2008

Homo sapiens

18325919

678518

Prezas, P.; Scorilas, A.; Yfanti, C.; Viktorov, P.; Agnanti, N.; Diamandis, E.; Talieri, M.

The role of human tissue kallikreins 7 and 8 in intracranial malignancies

Biol. Chem.

387

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2006

Homo sapiens

17132107

680177

Singh, J.; Naran, A.; Misso, N.L.; Rigby, P.J.; Thompson, P.J.; Bhoola, K.D.

Expression of kallikrein-related peptidases (KRP/hK5, 7, 6, 8) in subtypes of human lung carcinoma

Int. Immunopharmacol.

8

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2008

Homo sapiens

18182244

680680

Debela, M.; Magdolen, V.; Schechter, N.; Valachova, M.; Lottspeich, F.; Craik, C.S.; Choe, Y.; Bode, W.; Goettig, P.

Specificity profiling of seven human tissue kallikreins reveals individual subsite preferences

J. Biol. Chem.

281

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2006

Homo sapiens (P49862)

16740631

Deraison, C.; Bonnart, C.; Lopez, F.; Besson, C.; Robinson, R.; Jayakumar, A.; Wagberg, F.; Brattsand, M.; Hachem, J.P.; Leonardsson, G.; Hovnanian, A.

LEKTI fragments specifically inhibit KLK5, KLK7, and KLK14 and control desquamation through a pH-dependent interaction

Mol. Biol. Cell

18

3607-3619

2007

Homo sapiens

17596512

Debela, M.; Hess, P.; Magdolen, V.; Schechter, N.M.; Steiner, T.; Huber, R.; Bode, W.; Goettig, P.

Chymotryptic specificity determinants in the 1.0 A structure of the zinc-inhibited human tissue kallikrein 7

Proc. Natl. Acad. Sci. USA

104

16086-16091

2007

Homo sapiens (P49862), Homo sapiens

17909180

Fernandez, I.S.; Staendker, L.; Forssmann, W.G.; Gimenez-Gallego, G.; Romero, A.

Crystallization and preliminary crystallographic studies of human kallikrein 7, a serine protease of the multigene kallikrein family

Acta Crystallogr. Sect. F

F63

669-672

2007

Homo sapiens

17671364

Ramani, V.C.; Haun, R.S.

The extracellular matrix protein fibronectin is a substrate for kallikrein 7

Biochem. Biophys. Res. Commun.

369

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2008

Homo sapiens

18343220

Johnson, S.K.; Ramani, V.C.; Hennings, L.; Haun, R.S.

Kallikrein 7 enhances pancreatic cancer cell invasion by shedding E-cadherin

Cancer

109

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2007

Homo sapiens

17354228

683366

Shan, S.J.; Scorilas, A.; Katsaros, D.; Rigault de la Longrais, I.; Massobrio, M.; Diamandis, E.P.

Unfavorable prognostic value of human kallikrein 7 quantified by ELISA in ovarian cancer cytosols

Clin. Chem.

52

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2006

Homo sapiens

16916986

Fernandez, I.S.; Staendker, L.; Maegert, H.J.; Forssmann, W.G.; Gimenez-Gallego, G.; Romero, A.

Crystal structure of human epidermal kallikrein 7 (hK7) synthesized directly in its native state in E. coli: insights into the atomic basis of its inhibition by LEKTI domain 6 (LD6)

J. Mol. Biol.

377

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2008

Homo sapiens (P49862), Homo sapiens

18329042

Debela, M.; Beaufort, N.; Magdolen, V.; Schechter, N.M.; Craik, C.S.; Schmitt, M.; Bode, W.; Goettig, P.

Structures and specificity of the human kallikrein-related peptidases KLK 4, 5, 6, and 7

Biol. Chem.

389

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2008

Homo sapiens

18627343

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Pettus, J.R.; Johnson, J.J.; Shi, Z.; Davis, J.W.; Koblinski, J.; Ghosh, S.; Liu, Y.; Ravosa, M.J.; Frazier, S.; Stack, M.S.

Multiple kallikrein (KLK 5, 7, 8, and 10) expression in squamous cell carcinoma of the oral cavity

Histol. Histopathol.

24

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2009

Homo sapiens, Mus musculus

19085836

695895

Buraczewska, I.; Berne, B.; Lindberg, M.; Loden, M.; Toermae, H.

Long-term treatment with moisturizers affects the mRNA levels of genes involved in keratinocyte differentiation and desquamation

Arch. Dermatol. Res.

301

175-181

2009

Homo sapiens

18850104

695928

Xuan, Q.; Yang, X.; Mo, L.; Huang, F.; Pang, Y.; Qin, M.; Chen, Z.; He, M.; Wang, Q.; Mo, Z.N.

Expression of the serine protease kallikrein 7 and its inhibitor antileukoprotease is decreased in prostate cancer

Arch. Pathol. Lab. Med.

132

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2008

Homo sapiens

18976018

Eissa, A.; Diamandis, E.P.

Human tissue kallikreins as promiscuous modulators of homeostatic skin barrier functions

Biol. Chem.

389

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2008

Homo sapiens

18627299

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Dong, Y.; Matigian, N.; Harvey, T.J.; Samaratunga, H.; Hooper, J.D.; Clements, J.A.

Tissue-specific promoter utilisation of the kallikrein-related peptidase genes, KLK5 and KLK7, and cellular localisation of the encoded proteins suggest roles in exocrine pancreatic function

Biol. Chem.

389

99-109

2008

Homo sapiens

18163887

696964

Ramani, V.C.; Hennings, L.; Haun, R.S.

Desmoglein 2 is a substrate of kallikrein 7 in pancreatic cancer

BMC Cancer

8

373

2008

Homo sapiens

19091121

696984

Termini, L.; Boccardo, E.; Esteves, G.H.; Hirata, R.; Martins, W.K.; Colo, A.E.; Neves, E.J.; Villa, L.L.; Reis, L.F.

Characterization of global transcription profile of normal and HPV-immortalized keratinocytes and their response to TNF treatment

BMC Med. Genomics

1

29

2008

Homo sapiens

18588690

698443

Weidinger, S.; Baurecht, H.; Wagenpfeil, S.; Henderson, J.; Novak, N.; Sandilands, A.; Chen, H.; Rodriguez, E.; ORegan, G.M.; Watson, R.; Liao, H.; Zhao, Y.; Barker, J.N.; Allen, M.; Reynolds, N.; Meggitt, S.; Northstone, K.; Smith, G.D.; Strobl, C.; Stahl, C.; Kneib, T.; Klopp, N.; Bieber, T.; Behren, B.e.h.r.e.n.d.

Analysis of the individual and aggregate genetic contributions of previously identified serine peptidase inhibitor Kazal type 5 (SPINK5), kallikrein-related peptidase 7 (KLK7), and filaggrin (FLG) polymorphisms to eczema risk

J. Allergy Clin. Immunol.

122

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2008

Homo sapiens

18774391

Doering, K.; Meder, G.; Hinnenberger, M.; Woelcke, J.; Mayr, L.M.; Hassiepen, U.

A fluorescence lifetime-based assay for protease inhibitor profiling on human kallikrein 7

J. Biomol. Screen.

14

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Homo sapiens (P49862), Homo sapiens

19171917

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Ramani, V.C.; Haun, R.S.

Expression of kallikrein 7 diminishes pancreatic cancer cell adhesion to vitronectin and enhances urokinase-type plasminogen activator receptor shedding

Pancreas

37

399-404

2008

Homo sapiens

18953252

707621

Gabril, M.; White, N.M.; Moussa, M.; Chow, T.F.; Metias, S.M.; Fatoohi, E.; Yousef, G.M.

Immunohistochemical analysis of kallikrein-related peptidases in the normal kidney and renal tumors: potential clinical implications

Biol. Chem.

391

403-409

2010

Homo sapiens

20128686

707623

Ohler, A.; Debela, M.; Wagner, S.; Magdolen, V.; Becker-Pauly, C.

Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation

Biol. Chem.

391

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2010

Homo sapiens

20128684

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Dong, Y.; Tan, O.L.; Loessner, D.; Stephens, C.; Walpole, C.; Boyle, G.M.; Parsons, P.G.; Clements, J.A.

Kallikrein-related peptidase 7 promotes multicellular aggregation via the alpha(5)beta(1) integrin pathway and paclitaxel chemoresistance in serous epithelial ovarian carcinoma

Cancer Res.

70

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2010

Homo sapiens

20332224

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Li, X.; Liu, J.; Wang, Y.; Zhang, L.; Ning, L.; Feng, Y.

Parallel underexpression of kallikrein 5 and kallikrein 7 mRNA in breast malignancies

Cancer Sci.

100

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2009

Homo sapiens

19453546

708770

Termini, L.; Maciag, P.C.; Soares, F.A.; Nonogaki, S.; Pereira, S.M.; Alves, V.A.; Longatto-Filho, A.; Villa, L.L.

Analysis of human kallikrein 7 expression as a potential biomarker in cervical neoplasia

Int. J. Cancer

127

485-490

2010

Homo sapiens

19921697

709408

Morizane, S.; Yamasaki, K.; Kabigting, F.D.; Gallo, R.L.

Kallikrein expression and cathelicidin processing are independently controlled in keratinocytes by calcium, vitamin D3, and retinoic acid

J. Invest. Dermatol.

130

1297-1306

2010

Homo sapiens

20090765

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Talieri, M.; Mathioudaki, K.; Prezas, P.; Alexopoulou, D.K.; Diamandis, E.P.; Xynopoulos, D.; Ardavanis, A.; Arnogiannaki, N.; Scorilas, A.

Clinical significance of kallikrein-related peptidase 7 (KLK7) in colorectal cancer

Thromb. Haemost.

101

741-747

2009

Homo sapiens

19350120

Ramani, V.C.; Kaushal, G.P.; Haun, R.S.

Proteolytic action of kallikrein-related peptidase 7 produces unique active matrix metalloproteinase-9 lacking the C-terminal hemopexin domains

Biochim. Biophys. Acta

1813

1525-1531

2011

Homo sapiens

21616098

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Jamaspishvili, T.; Scorilas, A.; Kral, M.; Khomeriki, I.; Kurfurstova, D.; Kolar, Z.; Bouchal, J.

Immunohistochemical localization and analysis of kallikrein-related peptidase 7 and 11 expression in paired cancer and benign foci in prostate cancer patients

Neoplasma

58

298-303

2011

Homo sapiens

21520985

Oliveira, J.R.; Bertolin, T.C.; Andrade, D.; Oliveira, L.C.; Kondo, M.Y.; Santos, J.A.; Blaber, M.; Juliano, L.; Severino, B.; Caliendo, G.; Santagada, V.; Juliano, M.A.

Specificity studies on Kallikrein-related peptidase 7 (KLK7) and effects of osmolytes and glycosaminoglycans on its peptidase activity

Biochim. Biophys. Acta

1854

73-83

2015

Homo sapiens (P49862), Homo sapiens

25448018

731402

Walker, F.; Nicole, P.; Jallane, A.; Soosaipillai, A.; Mosbach, V.; Oikonomopoulou, K.; Diamandis, E.P.; Magdolen, V.; Darmoul, D.

Kallikrein-related peptidase 7 (KLK7) is a proliferative factor that is aberrantly expressed in human colon cancer

Biol. Chem.

395

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2014

Homo sapiens

25153388

Arama, D.; Soualmia, F.; Lisowski, V.; Longevial, J.; Bosc, E.; Maillard, L.; Martinez, J.; Masurier, N.; El Amri, C.

Pyrido-imidazodiazepinones as a new class of reversible inhibitors of human kallikrein 7

Eur. J. Med. Chem.

93

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2015

Homo sapiens

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732451

Li, W.; Zhao, Y.; Ren, L.; Wu, X.

Serum human kallikrein 7 represents a new marker for cervical cancer

Med. Oncol.

31

208

2014

Homo sapiens

25182706

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Zhang, C.; Zhu, Y.; Rui, W.; Dai, J.; Shen, Z.

Expression of kallikrein-related peptidase 7 is decreased in prostate cancer

Asian J. Androl.

17

106-110

2015

Homo sapiens (P49862), Homo sapiens

25219913

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Haddada, M.; Draoui, H.; Deschamps, L.; Walker, F.; Delaunay, T.; Brattsand, M.; Magdolen, V.; Darmoul, D.

Kallikrein-related peptidase 7 overexpression in melanoma cells modulates cell adhesion leading to a malignant phenotype

Biol. Chem.

399

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2018

Homo sapiens (P49862), Homo sapiens

29498930

Murafuji, H.; Muto, T.; Goto, M.; Imajo, S.; Sugawara, H.; Oyama, Y.; Minamitsuji, Y.; Miyazaki, S.; Murai, K.; Fujioka, H.

Discovery and structure-activity relationship of imidazolinylindole derivatives as kallikrein 7 inhibitors

Bioorg. Med. Chem. Lett.

29

334-338

2019

Homo sapiens (P49862), Homo sapiens, Mus musculus (Q91VE3), Mus musculus

30522951

Yu, Y.; Prassas, I.; Dimitromanolakis, A.; Diamandis, E.P.

Novel biological substrates of human kallikrein 7 identified through degradomics

J. Biol. Chem.

290

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2015

Homo sapiens (P49862), Homo sapiens

26032414