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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.2.16 - 2-phosphoglycerate kinase and Organism(s) Methanothermus fervidus and UniProt Accession Q49156

for references in articles please use BRENDA:EC2.7.2.16
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme, found in a number of methanogenic archaeal genera, is involved in the biosynthesis of cyclic 2,3-bisphosphoglycerate, a thermoprotectant. Activity is stimulated by potassium ions.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Methanothermus fervidus
UNIPROT: Q49156
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Methanothermus fervidus
The enzyme appears in selected viruses and cellular organisms
Synonyms
2-phosphoglycerate kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PGK2
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:2-phosphoglycerate 3-phosphotransferase
The enzyme, found in a number of methanogenic archaeal genera, is involved in the biosynthesis of cyclic 2,3-bisphosphoglycerate, a thermoprotectant. Activity is stimulated by potassium ions.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2-phospho-D-glycerate
ADP + 2,3-diphospho-D-glycerate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
0.3 M, 1.4fold stimulation
Mg2+
required, 8% residual activity in absence of Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
5 mM, almost complete inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
2-phospho-D-glycerate
pH 7.5, 75°C
2.7
ATP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
108
ATP
pH 7.5, 75°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1400000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 35040, caculated from sequence
multimer
x * 32500, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lehmacher, A.; Vogt, A.B.; Hensel, R.
Biosynthesis of cyclic 2,3-diphosphoglycerate. Isolation and characterization of 2-phosphoglycerate kinase and cyclic 2,3-diphosphoglycerate synthetase from Methanothermus fervidus
FEBS Lett.
272
94-98
1990
Methanothermus fervidus (Q49156), Methanothermus fervidus, Methanothermus fervidus ATCC 43054 (Q49156)
Manually annotated by BRENDA team
Lehmacher, A.; Hensel, R.
Cloning, sequencing and expression of the gene encoding 2-phosphoglycerate kinase from Methanothermus fervidus
Mol. Gen. Genet.
242
163-168
1994
Methanothermus fervidus (Q49156), Methanothermus fervidus, Methanothermus fervidus ATCC 43054 (Q49156)
Manually annotated by BRENDA team