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Information on EC 2.7.2.3 - phosphoglycerate kinase and Organism(s) Pyrococcus woesei and UniProt Accession P61884
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2.7.2.3 phosphoglycerate kinaseSpecify your search results
Word Map
- 2.7.2.3
- glyceraldehyde-3-phosphate
-
x-linked
- aldolase
- enolase
-
x-chromosome
- hexokinase
- erythrocyte
-
phosphofructokinase
- glucose-6-phosphate
- gapdh
- marrow
-
lentiviral
- anemia
- trypanosoma
- hypoxanthine
-
triosephosphate
-
hematopoietic
- mutase
- glyceraldehyde
- brucei
-
hypoxia-inducible
-
hemolytic
-
phosphoribosyltransferase
- cytomegalovirus
- glycosomal
- triose
-
x-chromosome-linked
- tpi
-
x-inactivation
-
methylation-sensitive
- myoglobinuria
-
n-domain
-
genorm
-
calvin
- hif-1alpha
- hpaii
- mgadp
- fructose-1,6-bisphosphate
-
fructose-bisphosphate
- 2,3-diphosphoglycerate
-
myeloproliferative
-
self-inactivating
-
phosphoglucose
- microbody
-
ligation-mediated
-
atp-generating
-
glucosephosphate
- alpha-enolase
- medicine
- phosphoribulokinase
-
allozyme
- analysis
- biofuel production
The taxonomic range for the selected organisms is: Pyrococcus woesei
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-PGK
-
-
-
-
3-phosphoglycerate kinase
-
-
-
-
3-phosphoglycerate phosphokinase
-
-
-
-
3-phosphoglyceric acid kinase
-
-
-
-
3-phosphoglyceric acid phosphokinase
-
-
-
-
3-phosphoglyceric kinase
-
-
-
-
ATP-3-phospho-D-glycerate-1-phosphotransferase
-
-
-
-
ATP:D-3-phosphoglycerate 1-phosphotransferase
-
-
-
-
glycerate 3-phosphate kinase
-
-
-
-
glycerophosphate kinase
-
-
-
-
kinase (phosphorylating), phosphoglycerate
-
-
-
-
PGK
-
-
-
-
phosphoglyceric acid kinase
-
-
-
-
phosphoglyceric kinase
-
-
-
-
phosphoglycerokinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
residues engaged in 3-phospho-D-glycerate binding: R22, D24, R144, E149, E150, H191, R192, residues engaged in ATP binding: G236, G237, G263, G371, G375, P372, E277, E377, G407, G408, G429-431
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:3-phospho-D-glycerate 1-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY
9001-83-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate.
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Na+
K+
monovalent cations are essential for the activity of the archaeal enzyme with K+ being significantly more efficient than Na+. Non-cooperative K+ binding with an apparent Kd (K+) of 88 mM
K+
monovalent cations are essential for the activity, with K+ being significantly more efficient than Na+. Non-cooperative K+ binding with an apparent Kd of 88 mM
Na+
monovalent cations are essential for the activity of the archaeal enzyme with K+ being significantly more efficient than Na+
Na+
monovalent cations are essential for the activity, with K+ being significantly more efficient than Na+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
3-phospho-D-glycerate
pH 7.5, 70°C, enzyme expressed in Escherichia coli
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
100
temperature optimum beyond 100°C, where activity can not be assayed under the experimental conditions
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
102700
87100 - 90000
recombinant enzyme, gel filtration in presence of 0.6 M KCl, and analytical ultracentrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
the enzyme from the original organism is completely resistant to heat inactivation for 35 min. Expression in Escherichia coli at optimal growth temperatures (37°C) yields a product which shows a tight association with a 28000 Da protein and exhibits low thermal stability (about 80% loss of activity after 5 min) suggesting a misfolding of the protein. As proved by N-terminal amino acid sequence analysis, the 28000 Da protein represents a 226-amino acid C-terminal fragment of the 3-phosphoglycerate kinase. Mutagenesis experiments confirm the assumption that the fragment originates by an internal translation initiation
additional information
additional information
stabilizing effects of anions on thermal stability
additional information
-
stabilizing effects of anions on thermal stability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression in Escherichia coli JM 83
expression in Escherichia coli at optimal growth temperatures (37°C) yields a product which shows a tight association with a 28000 Da protein and exhibits low thermal stability suggesting a misfolding of the protein. As proved by N-terminal amino acid sequence analysis, the 28000 Da protein represents a 226-amino acid C-terminal fragment of the 3-phosphoglycerate kinase. Mutagenesis experiments confirm the assumption that the fragment originates by an internal translation initiation
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
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)
Hess, D.; Hensel, R.
The 3-phosphoglycerate kinase of the hyperthermophilic archaeum Pyrococcus woesei produced in Escherichia coli: loss of heat resistance due to internal translation initiation and its restoration by site-directed mutagenesis
Gene
172
121-124
1996
Pyrococcus woesei (P61884), Pyrococcus woesei
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