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
135
download as CSV
download all results as CSV
EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
2.7.2.1
760947
Acetate kinase (AcK) is essential for microbial growth and betel-derived compounds potentially target AcK, PhoP and MDR proteins in M. tuberculosis, V. cholerae and pathogenic E. coli an in silico and in vitro study
Curr. Top. Med. Chem.
18
2731-2740
2018
Escherichia coli
30663567
2.7.2.1
760947
Acetate kinase (AcK) is essential for microbial growth and betel-derived compounds potentially target AcK, PhoP and MDR proteins in M. tuberculosis, V. cholerae and pathogenic E. coli an in silico and in vitro study
Curr. Top. Med. Chem.
18
2731-2740
2018
Mycobacterium tuberculosis
30663567
2.7.2.1
760947
Acetate kinase (AcK) is essential for microbial growth and betel-derived compounds potentially target AcK, PhoP and MDR proteins in M. tuberculosis, V. cholerae and pathogenic E. coli an in silico and in vitro study
Curr. Top. Med. Chem.
18
2731-2740
2018
Mycobacterium tuberculosis H37Rv
30663567
2.7.2.1
761116
Acetate kinase and peptidases are associated with the proteolytic activity of Lactobacillus helveticus isolated from fermented food
Food Microbiol.
94
103651
2021
Lactobacillus helveticus
33279076
2.7.2.1
746769
Acetate kinase-an enzyme of the postulated phosphoketolase pathway in Methylomicrobium alcaliphilum 20Z
Antonie van Leeuwenhoek
108
965-974
2015
Methylotuvimicrobium alcaliphilum
26275877
2.7.2.1
746769
Acetate kinase-an enzyme of the postulated phosphoketolase pathway in Methylomicrobium alcaliphilum 20Z
Antonie van Leeuwenhoek
108
965-974
2015
Methylotuvimicrobium alcaliphilum 20Z
26275877
2.7.2.1
761006
Biosynthesis of (deoxy)guanosine-5'-triphosphate by GMP kinase and acetate kinase fixed on the surface of E. coli
Enzyme Microb. Technol.
122
82-89
2019
Escherichia coli
30638512
2.7.2.1
760452
Characterization of a Rhodobacter sphaeroides primary fatty acid kinase
Arch. Microbiol.
203
861-864
2021
Cereibacter sphaeroides
33040182
2.7.2.1
757471
Characterization of the phosphotransacetylase-acetate kinase pathway for ATP production in Porphyromonas gingivalis
J. Oral Microbiol.
11
1588086
2019
Porphyromonas gingivalis
31007866
2.7.2.1
757471
Characterization of the phosphotransacetylase-acetate kinase pathway for ATP production in Porphyromonas gingivalis
J. Oral Microbiol.
11
1588086
2019
Porphyromonas gingivalis ATCC 33277
31007866
Results
1
-
10
of
135
download as CSV
download all results as CSV