Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.4.22.52 - calpain-1 and Organism(s) Oryctolagus cuniculus and UniProt Accession P06815

for references in articles please use BRENDA:EC3.4.22.52
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.52 calpain-1
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Oryctolagus cuniculus
UNIPROT: P06815 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Oryctolagus cuniculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
broad endopeptidase specificity
Synonyms
mu-calpain, calpain-1, calpain i, calpain 1, capn1, capn2, micro-calpain, capns1, calpain1, calpain-i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
calcium-activated neutral protease I
-
-
-
-
calpain 1
-
-
-
-
calpain I
-
-
-
-
CAPN1 g.p. (Homo sapiens)
-
-
-
-
micro-calpain
-
-
-
-
mu-calpain
-
-
-
-
muCANP
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
689772-75-6
-
78990-62-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
succinyl-bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-bovine-serum-albumin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-casein + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-insulin B + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-protamine + H2O
?
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
activates, Ka: 1.5 mM
Mn2+
-
slight activation
Sr2+
-
activates, Ka: 0.45 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
antipain
-
0.01 mM, 80-90% inhibition
E-64c
-
0.01 mM, 80-90% inhibition
leupeptin
-
0.01 mM, 80-90% inhibition
pepstatin A
-
1 mM, 60-80% inhibition
TLCK
-
0.1 mM, 60-80% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
succinyl-bovine serum albumin
-
pH 7.5, 25°C
-
0.0081
succinyl-casein
-
pH 7.5, 25°C
-
283.5
succinyl-insulin B
-
pH 7.5, 25°C
-
63
succinyl-protamine
-
pH 7.5, 25°C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CAN1_RABIT
302
0
35275
Swiss-Prot
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
1 * 80000 + 1 * 28000, SDS-PAGE
80000
-
1 * 80000 + 1 * 28000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
1 * 80000 + 1 * 28000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
10 min, 15% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
E-F hand structure domains
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the cDNA fragments corresponding to the domains with four consecutive E-F hand structures in the large and small subunits are inserted into an expression vector, pUC8 or pUC17. The resulting plasmids are used to transform Escherichia coli and isopropyl-1-thio-beta-D-galactoside-inducible expression is performed
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Emori, Y.; Kawasaki, H.; Sugihara, H.; Imajoh, S.; Kawashima, S.; Suzuki K.
Isolation and sequence analyses of cDNA clones for the large subunits of two isozymes of rabbit calcium-dependent protease
J. Biol. Chem.
261
9465-9471
1986
Oryctolagus cuniculus (P06815)
Manually annotated by BRENDA team
Minami, Y.; Emori, Y.; Kawasaki, H.; Suzuki, K.
E-F hand structure-domain of calcium-activated neutral protease (CANP) can bind Ca2+ ions
J. Biochem.
101
889-895
1987
Oryctolagus cuniculus (P06815)
Manually annotated by BRENDA team
Penny, I.F.; Taylor, M.A.J.; Harris, A.G.; Etherington, D.J.
Purification and immunological characterization of two calcium-activated neutral proteinases from rabbit skeletal muscle
Biochim. Biophys. Acta
829
244-252
1985
Oryctolagus cuniculus
Manually annotated by BRENDA team
Inomata, M.; Nomoto, M.; Hayashi, M.; Nakamura, M.; Imahori, K.; Kawashima, S.
Comparison of low and high calcium requiring forms of the calcium-activated neutral protease (CANP) from rabbit skeletal muscle
J. Biochem.
95
1661-1670
1984
Oryctolagus cuniculus
Manually annotated by BRENDA team