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Information on EC 3.4.21.119 - kallikrein 13 and Organism(s) Mus musculus and UniProt Accession P36368

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.119 kallikrein 13
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Mus musculus
UNIPROT: P36368 not found.
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The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Hydrolyses mouse Ren2 protein (a species of prorenin present in the submandibular gland) on the carboxy side of the arginine residue at the Lys-Arg-/- pair in the N-terminus, to yield mature renin
Synonyms
kallikrein 13, prece, mgk-13, prorenin converting enzyme, prorenin-converting enzyme, kallikrein-related peptidase 13, gk-13, glandular kallikrein 13, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glandular kallikrein K13
-
tissue kallikrein
-
GK-13
-
-
glandular kallikrein 13
-
-
mK13
-
-
PRECE
-
-
prorenin converting enzyme
-
-
prorenin-converting enzyme
-
-
S01.306
-
-
-
-
additional information
-
enzyme is neither trypsin-like nor kallikrein
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolyses mouse Ren2 protein (a species of prorenin present in the submandibular gland) on the carboxy side of the arginine residue at the Lys-Arg-/- pair in the N-terminus, to yield mature renin
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
342900-44-1
-
9001-01-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
35 kDa pro-interleukin 1beta + H2O
17.5 kDa interleukin 1beta + 20 kDa interleukin 1beta
show the reaction diagram
-
cleavage of Leu113-Leu114 bond
-
-
?
benzyloxycarbonyl-Arg-Val-Arg-Arg-4-methyl-coumaryl-7-amide + H2O
benzyloxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
low activity
-
-
?
benzyloxycarbonyl-Gln-Arg-Arg-4-methyl-coumaryl-7-amide + H2O
benzyloxycarbonyl-Gln-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
best substrate
-
-
?
benzyloxycarbonyl-Glu-Lys-Lys-4-methyl-coumaryl-7-amide + H2O
benzyloxycarbonyl-Glu-Lys-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
low activity
-
-
?
benzyloxycarbonyl-Leu-Lys-Arg-4-methyl-coumaryl-7-amide + H2O
benzyloxycarbonyl-Leu-Lys-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
mouse prorenin Ren2 + H2O
renin + ?
show the reaction diagram
-
specific cleavage of Lys-Arg bond of mouse prorenin Ren2
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
Prorenin + H2O
Renin + ?
show the reaction diagram
pyroglutamyl-Arg-Tyr-Lys-Arg-4-methyl-coumaryl-7-amide + H2O
pyroglutamyl-Arg-Tyr-Lys-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
polypeptide + H2O
peptides
show the reaction diagram
Prorenin + H2O
Renin + ?
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
antipain
benzamidine
diisopropyl fluorophosphate
-
2 mM, 35% inhibition
leupeptin
Phenylmethylsulfonylfluoride
-
-
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0011
-
purified enzyme, substrate benzyloxycarbonyl-Gln-Arg-Arg-4-methyl-coumaryl-7-amide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
7.5 - 8.5
-
-
8 - 8.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5 - 9.8
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene KLK13 or EGFB2, glandular kallikrein K13 precursor
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low activity
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
of granular convoluted tubular cell, co-localization of enzyme and pro-interleukin 1beta
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
EGFB2_MOUSE
261
0
28689
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10000
-
1 * 17000 + 1 * 10000, SDS-PAGE
17000
-
1 * 17000 + 1 * 10000, SDS-PAGE
27000
54000
-
about, gel filtration and crystal structure
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
additional information
-
enzyme contains 2 disulfide bridges at cystines 22-157 and 136-201
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
both hanging and sitting drop vapour diffusion method, protein solution: 57 mg/ml, precipitant solution: 10-15% PEG 8000, 200 mM Li2SO4, 100 mM sodium cacodylate, pH 6.5, room temperature, X-ray diffraction structure determination and analysis
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
Mus musculus (P36368)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Nakayama, K.; Kim, W.S.; Hatsuzawa, K.; Hashiba, K.; Murakami, K.
Tissue distribution and characterization of prorenin-converting enzyme in mouse
Biochem. Biophys. Res. Commun.
158
369-376
1989
Mus musculus
Manually annotated by BRENDA team
Nakayama, K.; Kim, W.S.; Nakagawa, T.; Nagahama, M; Murakami, K.
Substrate specificity of prorenin converting enzyme of mouse submandibular gland. Analysis using site-directed mutagenesis
J. Biol. Chem.
265
21027-21031
1990
Mus musculus
Manually annotated by BRENDA team
Timm, D.E.
The crystal structure of the mouse glandular kallikrein-13 (prorenin converting enzyme)
Protein Sci.
6
1418-1425
1997
Mus musculus
Manually annotated by BRENDA team
Kim, W.S.; Hatsuzawa, K.; Ishizuka, Y.; Hashiba, K.; Murakami, K.; Nakayama, K
A processing enzyme for prorenin in mouse submandibular gland. Purification and characterization
J. Biol. Chem.
265
5930-5933
1990
Mus musculus
Manually annotated by BRENDA team
Yao, C.; Karabasil, M.R.; Purwanti, N.; Li, X.; Akamatsu, T.; Kanamori, N.; Hosoi, K.
Tissue kallikrein mK13 is a candidate processing enzyme for the precursor of interleukin-1beta in the submandibular gland of mice
J. Biol. Chem.
281
7968-7976
2006
Mus musculus
Manually annotated by BRENDA team