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Information on EC 3.4.21.B40 - kallikrein 9
for references in articles please use BRENDA:EC3.4.21.B40
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preliminary BRENDA-supplied EC number
EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.21 Serine endopeptidases
3.4.21.B40 kallikrein 9
The enzyme appears in viruses and cellular organisms
- 3.4.21.B40
- kallikreins
- nerve
- glandular
-
submaxillary
- ngf
-
gamma-subunit
-
esteropeptidase
-
beta-ngf
- gamma-ngf
-
beta-nerve
- prorenin
-
anti-egf
- diagnostics
Reaction Schemes
showproteolytic cleavage of polypeptides, preferential cleavage site at paired basic amino acid residues
Synonyms
egf-bp, epidermal growth factor-binding protein, egf-binding protein, hmw-egf, kallikrein 9, epidermal growth factor urogastrone, human tissue kallikrein 9, high molecular weight epidermal growth factor, s3 kallikrein, kallikrein-related peptidase 9, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
K9
kallikrein 9
KLK9
S01.307
-
-
-
-
tissue kallikrein
kallikrein 9
-
has chymotrypsin-like substrate specificity in addition to trypsin-like specificity
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
proteolytic cleavage of polypeptides, preferential cleavage site at paired basic amino acid residues
proteolytic cleavage of polypeptides, preferential cleavage site at paired basic amino acid residues
preference for Xaa-Arg-Arg- motif
-
proteolytic cleavage of polypeptides, preferential cleavage site at paired basic amino acid residues
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
9001-01-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-TSVIRRVQ-ethylenediamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
AAPF-7-amido-4-methylcoumarin + H2O
AAPF + 7-amino-4-methylcoumarin
Substrates: 15% activity compared to LLVY-7-amido-4-methylcoumarin
Products: -
Products: -
?
benzyloxycarbonyl-Arg-Val-Arg-Arg-4-methyl-coumaryl-7-amide + H2O
benzyloxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
Substrates: low activity
Products: -
Products: -
?
benzyloxycarbonyl-Gln-Arg-Arg-4-methyl-coumaryl-7-amide + H2O
benzyloxycarbonyl-Gln-Arg-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Glu-Lys-Lys-4-methyl-coumaryl-7-amide + H2O
benzyloxycarbonyl-Glu-Lys-Lys + 7-amino-4-methylcoumarin
-
Substrates: low activity
Products: -
Products: -
?
benzyloxycarbonyl-Leu-Lys-Arg-4-methyl-coumaryl-7-amide + H2O
benzyloxycarbonyl-Leu-Lys-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
LLVY-7-amido-4-methylcoumarin + H2O
LLVY + 7-amino-4-methylcoumarin
Substrates: preferred substrate
Products: -
Products: -
?
o-aminobenzoyl-SVIRRVQ-ethylenediamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-TSVIRRPQ-ethylenediamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
p-toluenesulfonyl-L-arginine methyl ester + H2O
p-toluenesulfonyl-L-arginine + methyl alcohol
-
Substrates: -
Products: -
Products: -
?
pre-[epidermal growth factor] + H2O
epidermal growth factor + ?
-
Substrates: -
Products: -
Products: -
?
Pyr-Arg-Tyr-Lys-Arg-4-methyl-coumaryl-7-amide + H2O
Pyr-Arg-Tyr-Lys-Arg + 7-amino-4-methylcoumarin
-
Substrates: best substrate
Products: -
Products: -
?
prorenin 2 + H2O
renin 2 + ?
-
Substrates: recombinant substrate, enzymatically inactive proform
Products: product is the enzymatically active enzyme form
Products: product is the enzymatically active enzyme form
?
prorenin 2 + H2O
renin 2 + ?
-
Substrates: specific for mouse prorenin 2 from submandibular gland
Products: product is the enzymatically active enzyme form
Products: product is the enzymatically active enzyme form
?
additional information
?
-
Substrates: enzyme is regulated by steroid hormones in breast cancer cell line BT-474
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme has strong preference for tyrosine over phenylalanine at the P1 cleavage position
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has strong preference for tyrosine over phenylalanine at the P1 cleavage position
Products: -
Products: -
?
additional information
?
-
-
Substrates: rK9 is able to accommodate aromatic residues in position P1, and prefer a prolyl and hydrophobic residues in position P2'
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pre-[epidermal growth factor] + H2O
epidermal growth factor + ?
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is regulated by steroid hormones in breast cancer cell line BT-474
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Na+ has no significant effect on the enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
serpin A3
most potent serpin inhibitor, complete inhibition at 0.001 mM
-
Zn2+
reversible inhibition. 5 mM ZnCl2 almost completely abolishes the enzyme activity. EDTA (final concentration of 50 mM) completely reverses the Zn2+ inhibition
additional information
EDTA alone does not have any inhibitory effect on the enzyme activity
-
additional information
-
EDTA alone does not have any inhibitory effect on the enzyme activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Androgen-Insensitivity Syndrome
Induction of epidermal growth factor by tri-iodo-L-thyronine in the submandibular glands of mice with testicular feminization.
Carcinogenesis
Epidermal Growth Factor (EGF) Autocrine Activation of Human Platelets Promotes EGF Receptor-Dependent Oral Squamous Cell Carcinoma Invasion, Migration, and Epithelial Mesenchymal Transition.
Hypertension
Increased Klk9 Urinary Excretion Is Associated to Hypertension-Induced Cardiovascular Damage and Renal Alterations.
Infections
Epidermal growth factor-binding protein in Mycobacterium avium and Mycobacterium tuberculosis: a possible role in the mechanism of infection.
Neoplasms
Epidermal Growth Factor (EGF) Autocrine Activation of Human Platelets Promotes EGF Receptor-Dependent Oral Squamous Cell Carcinoma Invasion, Migration, and Epithelial Mesenchymal Transition.
Neoplasms
The soluble protease ADAMDEC1 released from activated platelets hydrolyzes platelet membrane pro-epidermal growth factor (EGF) to active high-molecular-weight EGF.
Ovarian Neoplasms
Clinical relevance of kallikrein-related peptidase 9, 10, 11, and 15 mRNA expression in advanced high-grade serous ovarian cancer.
Tuberculosis
Epidermal growth factor-binding protein in Mycobacterium avium and Mycobacterium tuberculosis: a possible role in the mechanism of infection.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0016
o-aminobenzoyl-TSVIRRVQ-ethylenediamine
-
o-aminobenzoyl-TSVIRRVQ-ethylenediamine
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0005
-
purified enzyme, substrate Pyr-Arg-Tyr-Lys-Arg-4-methyl-coumaryl-7-amide
0.298
with LLVY-7-amido-4-methylcoumarin as substrate, at pH 8.0 and 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene KLK9, submandibular glandular kallikrein 9 precursor
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
isozyme 1 shows a wide tissue distribution. The isozyme expression levels do vary between healthy and cancer tissue, overview
brenda
additional information
no enzyme expression in uterus, heart, adrenal gland, colon, spleen, skeletal muscle, pancreas, kidney, and fetal liver
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
at 37°C, the enzyme retains about 75% and 50% activity after 6-12 h and 48 h, respectively
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, gene is part of the human kallikrein multigene family, that mapps on chromosome 19q13.3-q13.4
gene (CANFA)KLK9, DNA and amino acid sequence determination and analysis, genetic structure and splicing events, overview. Sequence comparison with the human gene, detailed overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
the ELISAs for free and bound forms of KLK9 may be highly useful for the detection of KLK9 in a broad range of biological samples, thus enabling the clarification of KLK9 function and use as a potential disease biomarker
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q9UKQ9), Mus musculus (P15949), Rattus norvegicus (P07647)
brenda
Yousef, G.M.; Diamandis, E.P.
The expanded human kallikrein gene family: locus characterization and molecular cloning of a new member, KLK-L3 (KLK9)
Genomics
65
184-194
2000
Homo sapiens (Q9UKQ9)
brenda
Kikkawa, Y.; Yamanaka, N.; Tada, J.; Kanamori, N.; Tsumura, K.; Hosoi, K.
Prorenin processing and restricted endoproteolysis by mouse tissue kallikrein family enzymes (mK1, mK9, mK13, and mK22)
Biochim. Biophys. Acta
1382
55-64
1998
Mus musculus
brenda
El Moujahed, A.; Brillard-Bourdet, M.; Juliano, M.A.; Moreau, T.; Chagas, J.R.; Gutman, N.; Prado, E.S.; Gauthier, F.
Kininogen-derived fluorogenic substrates for investigating the vasoactive properties of rat kallikreins. Identification of a T-kinin-releasing rat kallikrein
Eur. J. Biochem.
247
652-658
1997
Rattus norvegicus
brenda
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
brenda
Memari, N.; Grass, L.; Nakamura, T.; Karakucuk, I.; Diamandis, E.P.
Human tissue kallikrein 9: production of recombinant proteins and specific antibodies
Biol. Chem.
387
733-740
2006
Homo sapiens
brenda
Chao, J.
Mouse kallikrein 9, epidermal growth factor-binding protein
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. )Academic Press
2
1602-1603
2004
Mus musculus
-
brenda
Yamada, A.; Nakamura, Y.; Sugita, D.; Shirosaki, S.; Ohkuri, T.; Katsukawa, H.; Nonaka, K.; Imoto, T.; Ninomiya, Y.
Induction of salivary kallikreins by the diet containing a sweet-suppressive peptide, gurmarin, in the rat
Biochem. Biophys. Res. Commun.
346
386-392
2006
Rattus norvegicus
brenda
Angelopoulou, K.; Karagiannis, G.S.
The canine kallikrein-related peptidases 9 and 10: structural characterization and expression in mammary cancer
Mamm. Genome
20
758-767
2010
Canis lupus familiaris (D2IJT6)
brenda
Filippou, P.S.; Farkona, S.; Brinc, D.; Yu, Y.; Prassas, I.; Diamandis, E.P.
Biochemical and functional characterization of the human tissue kallikrein 9
Biochem. J.
474
2417-2433
2017
Homo sapiens (Q9UKQ9), Homo sapiens
brenda
Filippou, P.; Korbakis, D.; Farkona, S.; Soosaipillai, A.; Karakosta, T.; Diamandis, E.P.
A new enzyme-linked immunosorbent assay (ELISA) for human free and bound kallikrein 9
Clin. Proteomics
14
4
2017
Homo sapiens (Q9UKQ9), Homo sapiens
brenda
EXTERNAL LINKS (specific for EC-Number 3.4.21.B40)
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