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Information on EC 3.4.21.117 - stratum corneum chymotryptic enzyme
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3.4.21.117 stratum corneum chymotryptic enzymeSpecify your search results
Word Map
- 3.4.21.117
- klk7
-
desquamation
- keratinocytes
-
cornified
- corneocyte
- netherton
-
corneodesmosomes
-
desmogleins
- corneodesmosin
-
spink5
- medicine
-
desmocollin
- vaspin
- diagnostics
- molecular biology
-
desquamatory
The enzyme appears in viruses and cellular organisms
Synonyms
kallikrein 7, stratum corneum chymotryptic enzyme, kallikrein-related peptidase 7, kallikrein-7, human stratum corneum chymotryptic enzyme, tissue kallikrein 7, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
hK7
human stratum corneum chymotryptic enzyme
kallikrein 7
kallikrein-related peptidase 7
KLK7
S01.300
-
-
-
-
SCCE
additional information
hK7
exhibits a chymotrypsin-like specificity preferring large hydrophobic or polar residues at the P1 position
kallikrein 7
-
-
-
-
kallikrein 7
-
-
kallikrein 7
-
the human kallikrein gene 7 is also known as the human stratum corneum chymotryptic enzyme
KLK7
-
-
additional information
-
KLK7 belongs to the kallikrein-related peptidase family
additional information
-
the enzyme belongs to the kallikrein subgroup of the serine protease enzyme family
additional information
-
the enzyme belongs to the multigene kallikrein serine protease family
additional information
the enzyme belongs to the human tissue kallikrein serine proteinase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cleavage of proteins with aromatic side chains in the P1 position
specific for amino acid residues with aromatic side chains in the P1 position
-
cleavage of proteins with aromatic side chains in the P1 position
enzyme exhibits a marked preference for cleavage downstream of Arg residues
-
cleavage of proteins with aromatic side chains in the P1 position
substrate binding pocket contains an Asn residue
cleavage of proteins with aromatic side chains in the P1 position
enzyme is a chymotrypsin-like serine protease
-
cleavage of proteins with aromatic side chains in the P1 position
enzyme is a chymotrypsin-like serine protease
cleavage of proteins with aromatic side chains in the P1 position
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
155215-90-0
-
9001-01-8
-
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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-AIKFFSA-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-AIKFF + SA-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-ALFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-ALF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-FLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-FLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-GFSPFRSSRI-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-GFSPF + RSSRI-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-GFSPFRSSRIGEIKEETT-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-GFSPF + RSSRIGEIKEETT-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-GLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-GLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-HLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-HLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-ILFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-ILF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KAFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KAF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KFFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KFF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KLFSSE-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KLF + SSE-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KLTWLPL-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KLTW + LPL-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KLYSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KLY + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KPFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KPF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KVFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KVF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KYFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KYF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-LLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-LLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-LMEKWTW-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-LMEKW + TW-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-MISLMKRP-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-MISLM + KRP-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-NLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-NLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-PHVMRFP-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-PHVM + RFP-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-QLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-QLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-RLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-RLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-VARPYYL-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-VARPYY + L-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-VLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-VLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-VQFYQGP-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-VQFY + QGP-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-VQMRGFA-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-VQM + RGF + A-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-YNPFVFT-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-YNPF + VF + T-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-YWSIQPF-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-Y + WSIQPF + Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Ac-ED(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)KPILFRLGK(4-(4-dimethylaminophenylazo)benzoic acid)E-NH2 + H2O
?
-
-
-
?
Ac-EFKPILWRLGC-(6-(9-oxo-9H-acridin-10-yl)-hexanoate)E-NH2 + H2O
?
-
-
-
?
acetyl-Phe-Val-Arg-4-nitroanilide + H2O
acetyl-Phe-Val-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
benzoyl-Phe-Val-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
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
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
desmoglein 1 + H2O
?
-
kallikrein 7 cleaves both recombinant desmoglein 1 and desmoglein 2 in vitro
-
-
?
desmoglein 2 + H2O
?
-
kallikrein 7 cleaves both recombinant desmoglein 1 and desmoglein 2 in vitro. Ectopic expression of kallikrein 7 in BxPC-3 pancreatic cancer cells which express desoglein 2 but not desmoglein 1 or kallikrein 7 confirms the cleavage of desmoglein 2 in vivo
-
-
?
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
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
-
-
?
L-Tyr-7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
-
-
-
?
LLVY-7-amido-4-methylcoumarin + H2O
LLVY + 7-amino-4-methylcoumarin
-
-
-
?
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
methoxy-succinyl-Arg-Pro-Tyr-7-amido-4-methylcoumarin + H2O
methoxy-succinyl-Arg-Pro-Tyr + 7-amino-4-methylcoumarin
-
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-p-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + p-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
o-aminobenzoyl-FRAPR-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
low activity
-
-
?
o-aminobenzoyl-FRLVR-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-FR + LVR-(2,4-dinitrophenyl)ethylenediamine
-
low activity
-
?
o-aminobenzoyl-SVIRRVQ-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-TSVIRRPQ-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
low activity
-
-
?
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
?
Phe-7-amido-4-methylcoumarin + H2O
Phe + 7-amino-4-methylcoumarin
-
-
-
?
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
-
?
SANSNPAMAPRERKAGCKNFFWKTFTSC + H2O
SANSNPAMAPRERKAGCKNFF + WKTFTSC
-
-
-
?
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
Suc-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-AAPF-7-amido-4-methylcoumarin + H2O
succinyl-AAPF + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
chromogenic substrate
-
-
?
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-Ala-Val-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Val-Pro-Phe + 4-nitroaniline
-
-
-
?
succinyl-Leu-Leu-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Tyr-7-amido-4-methylcoumarin + H2O
Tyr + 7-amino-4-methylcoumarin
-
-
-
?
beta-amyloid peptide + H2O
?
-
degradation, the enzyme cleaves after both Phe residues within the core of Abeta42 in vitro, thereby inhibiting A? fibril formation and promoting the degradation of preformed fibrils
-
-
?
corneodesmosin + H2O
?
-
KLK7 degrades corneodesmosomes CDSN, DSC1, and DSG1
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
low activity
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
i.e. S2288
-
-
?
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
-
-
?
human pro-interleukin 1beta + H2O
human interleukin beta1 + ?
-
several claevage sites
product can be further degraded by the enzyme leading to its inactivation, product is in the active form
?
human pro-interleukin 1beta + H2O
human interleukin beta1 + ?
-
recombinant enzyme and substrate
product can be further degraded by the enzyme leading to its inactivation, product is in the active form
?
human pro-interleukin 1beta + H2O
human interleukin beta1 + ?
-
substrate is in the inactive form
product can be further degraded by the enzyme leading to its inactivation, product is in the active form
?
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 + H2O
?
-
a fluorogenic peptide substrate
-
-
?
methoxy-succinyl-Ala-Ala-Pro-Met-4-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Met + 4-nitroaniline
-
chromogenic substrate
-
-
?
methoxy-succinyl-Ala-Ala-Pro-Met-4-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Met + 4-nitroaniline
-
low activity
-
-
?
methoxy-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
chromogenic substrate
-
-
?
methoxy-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
low activity
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + 4-nitroaniline
-
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + 4-nitroaniline
-
best substrate
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + 4-nitroaniline
-
chromogenic substrate
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + 4-nitroaniline
-
i.e. S2586
-
-
?
N-carbobenzoxy-Gly-Pro-Arg-4-nitroanilide + H2O
N-carbobenzoxy-Gly-Pro-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
N-carbobenzoxy-Gly-Pro-Arg-4-nitroanilide + H2O
N-carbobenzoxy-Gly-Pro-Arg + 4-nitroaniline
-
low activity
-
-
?
N-carbobenzoxy-Val-Gly-Arg-4-nitroanilide + H2O
N-carbobenzoxy-Val-Gly-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
N-carbobenzoxy-Val-Gly-Arg-4-nitroanilide + H2O
N-carbobenzoxy-Val-Gly-Arg + 4-nitroaniline
-
low activity
-
-
?
polypeptide + H2O
peptides
-
mediates shedding and desquamation of skin cells
-
?
polypeptide + H2O
peptides
-
involved in desquamation in plantar stratum corneum
-
?
polypeptide + H2O
peptides
-
involved in desquamation in plantar stratum corneum
-
?
polypeptide + H2O
peptides
-
involved in desquamation in plantar stratum corneum
-
?
polypeptide + H2O
peptides
-
catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continous sheeding of the cells from the skin surface
-
?
polypeptide + H2O
peptides
-
catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continous sheeding of the cells from the skin surface
-
?
polypeptide + H2O
peptides
involved in pathological keratinization, psoriasis, and ovarian cancer
-
?
succinyl-Phe-Leu-Phe-4-nitroanilide + H2O
succinyl-Phe-Leu-Phe + 4-nitroaniline
-
chromogenic substrate
-
-
?
succinyl-Phe-Leu-Phe-4-nitroanilide + H2O
succinyl-Phe-Leu-Phe + 4-nitroaniline
-
low activity
-
-
?
succinyl-Val-Pro-Phe-4-nitroanilide + H2O
succinyl-Val-Pro-Phe + 4-nitroaniline
-
chromogenic substrate
-
-
?
succinyl-Val-Pro-Phe-4-nitroanilide + H2O
succinyl-Val-Pro-Phe + 4-nitroaniline
-
low activity
-
-
?
additional information
?
-
-
the enzyme causes canine atopic dermatitis
-
-
?
additional information
?
-
recombinant enzyme proform is activated by digestion with trypsin
-
-
?
additional information
?
-
-
recombinant enzyme proform is activated by digestion with trypsin
-
-
?
additional information
?
-
-
enzyme may contribute to tumor cell growth, tumor spread, and the metastatic potential of ovarian tumor cells
-
-
?
additional information
?
-
AACC insertion in the stratum corneum chymotryptic enzyme gene may result in a change to activity of stratum corneum chymotryptic enzyme within the skin barrier. Stratum corneum chymotryptic enzyme could have an important role in the development of atopic dermatitis
-
-
?
additional information
?
-
-
AACC insertion in the stratum corneum chymotryptic enzyme gene may result in a change to activity of stratum corneum chymotryptic enzyme within the skin barrier. Stratum corneum chymotryptic enzyme could have an important role in the development of atopic dermatitis
-
-
?
additional information
?
-
-
epidermal hyperproliferation and decreased skin barrier function in mice overexpressing stratum corneum chymotryptic enzyme
-
-
?
additional information
?
-
-
gene expression might be involved in lung tumorigenesis
-
-
?
additional information
?
-
-
increased expression of kallikrein 7 and decreased expression of its inhibitor antileukoprotease might play an important role in cervical adenocarcinoma development
-
-
?
additional information
?
-
kallikrein 7 is involved in desquamation
-
-
?
additional information
?
-
succinyl-Ala-Ala-Pro-Phe-tripeptidyl-p-nitroanilide is no substrate
-
-
?
additional information
?
-
the most favored P1 residue of hK7 is Tyr followed by Ala, Met, and Nle, whereas Phe is ranked rather low, and Trp seems to be totally excluded, at S2, the most preferred residue is again Tyr, well ahead of the medium-sized hydrophobic residues Leu, Nle, Thr, Met, and Phe, whereas Gly is almost not tolerated, at S3 and S4, nearly all residues are accepted with a slight preference for hydrophobic side chains
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?
additional information
?
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high enzyme activity shows a significantly better prognosis in breast cancer
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?
additional information
?
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high enzyme activity shows a significantly better prognosis in breast cancer
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?
additional information
?
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kallikrein 7 is involved in pathological keratinization, psoriasis and ovarian cancer
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?
additional information
?
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kallikrein 7 participates in normal desquamation by facilitating cell shedding at the skin surface, and it degrades components of the extracellular matrix, the aberrant expression and secretion of kallikrein 7 in human tumors may facilitate metastasis by directly degrading components of the extracellular matrix and may thus play an important role in tumorigenesis, overview, the enzyme is implicated in the degradation of intercellular cohesive structures in the stratum corneum preceding desquamation
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?
additional information
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the enzyme participates in skin desquamation but is also implicated in diverse skin diseases and is a potential biomarker of ovarian cancer
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?
additional information
?
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the enzyme participates in skin desquamation but is also implicated in diverse skin diseases and is a potential biomarker of ovarian cancer
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?
additional information
?
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active site structure and substrate specificity, overview, kallikrein 7 exhibits large positively charged surface patches, representing putative exosites for prime side substrate recognition, overview
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?
additional information
?
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active site structure and substrate specificity, overview, kallikrein 7 exhibits large positively charged surface patches, representing putative exosites for prime side substrate recognition, overview
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?
additional information
?
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similar to KLK5, KLK7 degrades proteins of corneodesmosomes, which are most likely physiological substrates of KLKs expressed in the stratum corneum of skin
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?
additional information
?
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the P3-P'3' sequence NLYRVR is identified as a preferred substrate for the enzyme, glutamate at position P3' is also well accepted, substrate specificity, overview. No activity with Abz-KVYFFFRENAI-Q-N-[2,4-dinitrophenyl]-ethylenediamine. Kininogenase activity of the enzyme using as substrate a synthetic peptide derived from human kininogen (Abz-MISLMKRPPGFSPFRSSRI-NH2) containing the amino acids F and M as two possible cleavage site
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?
additional information
?
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the P3-P'3' sequence NLYRVR is identified as a preferred substrate for the enzyme, glutamate at position P3' is also well accepted, substrate specificity, overview. No activity with Abz-KVYFFFRENAI-Q-N-[2,4-dinitrophenyl]-ethylenediamine. Kininogenase activity of the enzyme using as substrate a synthetic peptide derived from human kininogen (Abz-MISLMKRPPGFSPFRSSRI-NH2) containing the amino acids F and M as two possible cleavage site
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?
additional information
?
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recombinant KLK7 clearly shows Tyr over Phe preference at the P1 site. No activity is detected against substrates with Lys or Ala in P1 sites, and minimum activity (about 10% activity compared with trypsin-like KLKs) is observed against substrates with Arg in the P1 site
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?
additional information
?
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recombinant KLK7 clearly shows Tyr over Phe preference at the P1 site. No activity is detected against substrates with Lys or Ala in P1 sites, and minimum activity (about 10% activity compared with trypsin-like KLKs) is observed against substrates with Arg in the P1 site
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?
additional information
?
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KLK7 exerts chymotryptic-like cleavage preferences. KLK7 subsite preferences are also characterised in the P2-P2 region, demonstrating a preference for hydrophobic residues in the non-prime and hydrophilic residues in the prime subsites
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?
additional information
?
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KLK7 exerts chymotryptic-like cleavage preferences. KLK7 subsite preferences are also characterised in the P2-P2 region, demonstrating a preference for hydrophobic residues in the non-prime and hydrophilic residues in the prime subsites
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?
additional information
?
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enzyme exhibits a marked preference for cleavage downstream of Arg residues
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?
additional information
?
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the enzyme shows a unique extended chymotrypsin-like specificity and beta-amyloid peptide-degrading capacity
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?
additional information
?
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the enzyme's consensus motif is RX0(Y/F)-/-(Y/F)-/-(S/A/G/T) or RX0(Y/F)-/-(S/T/A) (0 = hydrophobic)
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?
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NATURAL SUBSTRATE
NATURAL 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
beta-amyloid peptide + H2O
?
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degradation, the enzyme cleaves after both Phe residues within the core of Abeta42 in vitro, thereby inhibiting A? fibril formation and promoting the degradation of preformed fibrils
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?
E-cadherin + H2O
?
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kallikrein 7 degrades extracellular matrix proteins, and enhances pancreatic cancer cell invasion by shedding E-cadherin, overview