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
22
download as CSV
download all results as CSV
EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
3.5.2.7
757925
Exploring the substrate specificity and catalytic mechanism of imidazolonepropionase (HutI) from Bacillus subtilis
Phys. Chem. Chem. Phys.
18
27928-27938
2016
Bacillus subtilis
27711543
3.5.2.7
757925
Exploring the substrate specificity and catalytic mechanism of imidazolonepropionase (HutI) from Bacillus subtilis
Phys. Chem. Chem. Phys.
18
27928-27938
2016
Bacillus subtilis 168
27711543
3.5.2.7
687529
A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis
J. Biol. Chem.
281
36929-36936
2006
Bacillus subtilis
16990261
3.5.2.7
685249
A common catalytic mechanism for proteins of the HutI family
Biochemistry
47
5608-5615
2008
Agrobacterium tumefaciens
18442260
3.5.2.7
172090
An evolutionary treasure: Unification of a broad set of amidohydrolases related to urease
Proteins Struct. Funct. Genet.
28
72-82
1997
Caenorhabditis elegans
9144792
3.5.2.7
5766
Cloning and expression in Escherichia coli of histidine utilization genes from Pseudomonas putida
J. Bacteriol.
162
138-146
1985
Pseudomonas putida
2858467
3.5.2.7
172091
Genetic and metabolic control of enzymes responsible for histidine degradation in Salmonella typhimurium. 4-imidazolone-5-propionate amidohydrolase and N-formimino-L-glutamate formiminohydrolase
J. Biol. Chem.
246
3320-3329
1971
Salmonella enterica subsp. enterica serovar Typhimurium
4930059
3.5.2.7
172087
Histidine dissimilation in Streptomyces coelicolor
J. Gen. Microbiol.
128
2029-2040
1982
Streptomyces coelicolor
6129283
3.5.2.7
172089
Imidazolonepropionic acid hydrolase (Bacillus subtilis)
Methods Enzymol.
17B
55-57
1971
Bacillus subtilis
-
3.5.2.7
172088
Imidazolonepropionic acid hydrolase (Rat liver)
Methods Enzymol.
17B
92-95
1971
Rattus norvegicus
-
Results
1
-
10
of
22
download as CSV
download all results as CSV