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Information on EC 2.7.2.3 - phosphoglycerate kinase and Organism(s) Methanothermus fervidus and UniProt Accession P20971

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This record set is specific for:
Methanothermus fervidus
UNIPROT: P20971 not found.
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Word Map
The taxonomic range for the selected organisms is: Methanothermus fervidus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pgk, phosphoglycerate kinase, pgk-1, 3-phosphoglycerate kinase, phosphoglycerate kinase 1, pgk-2, phosphoglycerate kinase-1, phosphoglycerokinase, phosphoglycerate kinase 2, 3-pgk, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-phosphoglycerate kinase
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Mfer_0156
ordered locus name
3-PGK
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3-phosphoglycerate kinase
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3-phosphoglycerate phosphokinase
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3-phosphoglyceric acid kinase
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-
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3-phosphoglyceric acid phosphokinase
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-
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3-phosphoglyceric kinase
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ATP-3-phospho-D-glycerate-1-phosphotransferase
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ATP:D-3-phosphoglycerate 1-phosphotransferase
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glycerate 3-phosphate kinase
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glycerophosphate kinase
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kinase (phosphorylating), phosphoglycerate
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PGK
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phosphoglyceric acid kinase
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phosphoglyceric kinase
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phosphoglycerokinase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
ATP:3-phospho-D-glycerate 1-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9001-83-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
required as phosphate donor
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.75 - 0.77
3-phospho-D-glycerate
0.73 - 1.1
ATP
0.75 - 0.77
3-phospho-D-glycerate
0.73 - 1.1
ATP
1.1
Mg2+
native and recombinant enzyme, 70°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
149.8 - 338.9
3-phospho-D-glycerate
149.8 - 338.9
ATP
150 - 339
3-phospho-D-glycerate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
100
ATP
pH 7.5, 73°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150
purified recombinant enzyme
75
purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 90
the enzyme shows considerable activity at 40°C, 90°C: optimum
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
2 * 45000, SDS-PAGE
45871
2 * 45871, calculated from sequence
94700
gel filtration, at 600 mM K+, recombinant enzyme
97000
gel filtration, at 600 mM K+, native enzyme
97100
gel filtration at 600 mM K+
45000
2 * 45000, SDS-PAGE
45870
2 * 45870, DNA and amino acid sequence determination
94700
recombinant enzyme, gel filtration in presence of 0.6 M KCl
97100
native enzyme, gel filtration in presence of 0.6 M KCl
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
dimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
83
half-life: 44 min
86
half-life: 44 min
89
half-life: 10 min
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stabilized by anions in decreasing order of efficiency: 2,3-bisphospho-D-glycerate, PO43-, SO42-, Cl-
the stabilizing effects of anions on thermal stability
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial purification of the native enzyme
recombinant, wild-type from Escherichia coli, 51.7fold
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, the protein expressed in the mesophilic host is folded correctly. By comparing the 3-phosphoglycerate kinase sequences of the mesophilic and the two thermophilic Archaea, trends in thermoadaptation are confirmed that can be deduced from comparisons of glyceraldehyde-3-phosphate dehydrogenase sequences from the same organisms. With increasing temperature the average hydrophobicity and the portion of aromatic residues increases, whereas the chain flexibility as well as the content in chemically labile residues (Asn, Cys) decreases
expression in Escherichia coli. The protein which is expressed in the mesophilic host is folded correctly
expression of slightly modified wild-type in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hess, D.; Kruger, K.; Knappik, A.; Palm, P.; Hensel, R.
Dimeric 3-phosphoglycerate kinases from hyperthermophilic Archaea. Cloning, sequencing and expression of the 3-phosphoglycerate kinase gene of Pyrococcus woesei in Escherichia coli and characterization of the protein. Structural and functional comparison with the 3-phosphoglycerate kinase of Methanothermus fervidus
Eur. J. Biochem.
233
227-237
1995
Methanobacterium bryantii, Methanothermus fervidus, Methanothermus fervidus (P20971), Pyrococcus woesei (P61884), Pyrococcus woesei, Methanothermus fervidus DSM 2088 (P20971), Pyrococcus woesei Vul 4 / DSM 3773 (P61884), Pyrococcus woesei DSM 3773 (P61884)
Manually annotated by BRENDA team