Leibniz Institute DSMZ
DSMZ Digital Diversity
Login
Classic view
All enzymes
Enzyme history
BRENDA support
Any feedback?
Please rate this page
(search_result.php)
😁
😐
😡
(
0
/150)
Send feedback
BRENDA support
Refine search
Search Reference
Reference:
show
10
50
100
results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search
Recommended Name:
EC Number:
contains
exact
begins with
ends with
use * as joker
BRENDA No.:
contains
exact
begins with
ends with
use * as joker
Authors:
contains
exact
begins with
ends with
use * as joker
Journal:
contains
exact
begins with
ends with
use * as joker
Volume:
contains
exact
begins with
ends with
use * as joker
Pages:
contains
exact
begins with
ends with
use * as joker
Year:
=
<
>
between min-max
use * as joker
Organism:
contains
exact
begins with
ends with
use * as joker
PubMed ID:
=
<
>
between min-max
use * as joker
Show additional data
do not include text mining results
include
results
(Automatic Mining of Enzyme Data)
include
results
(AMENDA + additional results, but less precise)
Search term:
Results
1
-
10
of
42
download as CSV
download all results as CSV
EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
3.4.18.1
36441
On the specificity of bovine spleen cathepsin B2
Biochim. Biophys. Acta
452
503-509
1976
Bos taurus
12811
3.4.18.1
36645
Improved purification of cathepsin B1 and cathepsin B2
Biochim. Biophys. Acta
379
462-475
1975
Bos taurus
1122298
3.4.18.1
36444
Histone hydrolase activity of rat liver lysosomal cathepsin B2
Biochim. Biophys. Acta
293
217-225
1973
Rattus norvegicus
4346573
3.4.18.1
36443
Purification and characterization of rat liver lysosomal cathepsin B2
Biochim. Biophys. Acta
370
308-321
1974
Rattus norvegicus
4429705
3.4.18.1
36445
Cathepsins B1 and B2 in various organs of the rat
Enzymologia
42
363-375
1972
Rattus norvegicus
5029515
3.4.18.1
36392
Engineered human carboxypeptidase B enzymes that hydrolyse hippuryl-L-glutamic acid: reversed-polarity mutants
Protein Eng.
11
1229-1234
1998
Homo sapiens
9930672
3.4.18.1
653947
Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease
Structure Fold. Des.
8
305-313
2000
Homo sapiens
10745011
3.4.18.1
651078
Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase
Eur. J. Biochem.
267
5404-5412
2000
Homo sapiens
10951198
3.4.18.1
663867
Carboxy-monopeptidase substrate specificity of human cathepsin X
Biochem. Biophys. Res. Commun.
329
445-452
2005
Homo sapiens
15737607
3.4.18.1
664854
Carboxypeptidases cathepsins X and B display distinct protein profile in human cells and tissues
Exp. Cell Res.
306
103-113
2005
Homo sapiens
15878337
Results
1
-
10
of
42
download as CSV
download all results as CSV