2.7.2.3: phosphoglycerate kinase
This is an abbreviated version!
For detailed information about phosphoglycerate kinase, go to the full flat file.
Word Map on EC 2.7.2.3
-
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
- 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
Reaction
Synonyms
3-PGK, 3-phosphoglycerate 1-phosphotransferase, 3-phosphoglycerate kinase, 3-phosphoglycerate phosphokinase, 3-phosphoglyceric acid kinase, 3-phosphoglyceric acid phosphokinase, 3-phosphoglyceric kinase, AbPGK, ATP-3-phospho-D-glycerate-1-phosphotransferase, ATP:3-phospho-D-glycerate 1-phosphotransferase, ATP:D-3-phosphoglycerate 1-phosphotransferase, chl-PGK, glycerate 3-phosphate kinase, glycerophosphate kinase, HacPGK1, HacPGK2, HapPGK, hPGK, HsPGK, human 3-phosphoglycerate kinase, kinase (phosphorylating), phosphoglycerate, Mfer_0156, OsPGK2, P-glycerate kinase, PAS-PGK, PfPGK, PGK, PGK 1, PGK-1, PGK-2, pgk-B, PGK1, PGK2, Pgk3, Pgk5, PGKA, PGKase-1, PGKB, PGKC, pgkp1, pgkp2, phosphoglycerate kinase, phosphoglycerate kinase 1, phosphoglycerate kinase 2, phosphoglycerate kinase B, phosphoglycerate kinase-1, phosphoglyceric acid kinase, phosphoglyceric kinase, phosphoglycerokinase, PwPGK, SjPGK, SSO0527, testis-specific phosphoglycerate kinase 2, TRSC58_02767, X chromosome-linked phosphoglycerate kinase-1
ECTree
2.7.2.3 phosphoglycerate kinaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.7.2.3 - phosphoglycerate kinase
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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
2',3'-didehydro-2',3'-dideoxythymidine triphosphate + 3-phospho-D-glycerate
2',3'-didehydro-2',3'-dideoxythymidine diphosphate + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
2',3'-dideoxy-GTP + 3-phospho-D-glycerate
2',3'-dideoxy-GDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
2'-dATP + 3-phospho-D-glycerate
2'-dADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
2'-deoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2'-deoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
2'-dGTP + 3-phospho-D-glycerate
2'-dGDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
2'-dTTP + 3-phospho-D-glycerate
2'-dTDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
3'-deoxy-3'-azidothymidine triphosphate + 3-phospho-D-glycerate
3'-deoxy-3'-azidothymidine diphosphate + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
acyclovir triphosphate + 3-phospho-D-glycerate
acyclovir diphosphate + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
beta-L(-)-dioxolanecytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L(-)-dioxolanecytidine 5'-diphosphate + 1,3-diphosphoglycerate
beta-L-2',3'-dideoxy-3'-thiacytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L-2',3'-dideoxy-3'-thiacytidine 5'-diphosphate + 1,3-diphosphoglycerate
dATP + 3-phospho-D-glycerate
dADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
L-2'-dATP + 3-phospho-D-glycerate
L-2'-dADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
L-2'-dCTP + 3-phospho-D-glycerate
L-2'-dCDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
L-2'-dGTP + 3-phospho-D-glycerate
L-2'-dGDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
L-2'-dTTP + 3-phospho-D-glycerate
L-2'-dTDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
L-ADP + 1,3-bisphosphoglycerate
?
with L-ADP, the transient burst phase of ATP is more clear-cut than with D-ADP, suggesting that the product release steps are slower with L-ADP than with D-ADP. This is in accordance with the lower kcat measured with L-ADP compared to D-ADP
-
-
?
L-ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
L-MgADP is almost as a good substrate for hPGK as the natural D-MgADP
-
-
?
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
isozyme PGK1
-
-
?
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
3.6fold higher activity compared to 2'-deoxycytidine
-
-
?
2'-deoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2'-deoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
-
-
-
?
2'-deoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2'-deoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
isozyme PGK1
-
-
?
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
-
-
-
-
r
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
-
-
-
-
r
ADP + 1,3-bisphosphoglycerate
ATP + 3-phosphoglycerate
using the stopped-flow method it is shown that substrate binding kinetics that lead to the formation of the catalytic PGK-1,3-bisphosphoglycerate-ADP complexes are mutually antagonistic with D-ADP, but much less so with L-ADP. A situation that is similar to that for the formation of the abortive PGK-3-phosphoglycerate-ADP complexes
-
-
?
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
overall increases in amide protection from hydrogen exchange when the W290Y mutant protein binds the substrate and product ligands and an additional increase when the transition-state analogue complex containing a 3-phospho-D-glycerate-(AlF4-)-ADP moiety is formed. Communication between domains is manifested in the accessibility of higher-energy, exchange-competent states. For residue D33, chemical shifts only change significantly upon transition-state analogue binding. For residue S346, chemical shifts change significantly upon ADP and transition-state analogue binding. For residue S58, chemical shifts are affected by 3-phospho-D-glycerate and transition-state analogue binding
-
-
?
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
-
molecular dynamics simulations reveal, that both in the absence and in the presence of ligands the enzyme exhibits a hinge bending type motion but the characteristics of this motion vary considerably. In the apo form, the enzyme exhibits a hinge bending motion of a relatively small amplitude with a time period around 20 ns while the time period of the complexed form is much longer than simulation time. In both cases there is a hinge at the C-terminal side of helix 7, but the hinge points which are near the substrate binding site change upon binding. The apo form is more flexible, there are more hinge points that contribute with similar significance to the hinge bending motion, while in the ternary complex there is only one dominant hinge point. This is located in the vicinity of the substrates, in loop K13. The binding of ADP rigidifies its binding site in the C-domain, while binding 1,3-diphosphoglycerate increases the flexibility of the binding range of the N-domain
-
-
?
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
Esox sp.
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
Frog
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
catalytic residue R38, which also binds the substrate 3-phosphoglycerate, is essential in inducing domain closure. Similarly, residues K219, N336, and E343 which interact with the nucleotide substrates are involved in the process of domain closure. The other catalytic residue, K215, covers a large distance during catalysis but has no direct role in domain closure
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
molecular modeling study show that the beta-phosphates of D- and L-ADP have different orientations when bound to the active site of human PGK. The difference is unexpected because L-ADP is almost as catalytically competent as D-ADP
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
the enzyme favors the forward reaction
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
energy charge is the most important factor in regulating the 2 forms of PGK
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
key enzyme of anaerobic glycolysis in Plasmodium falciparum
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
Pyrococcus woesei Vul 4 / DSM 3773
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
the reaction occurs at 70°C
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
infrared studies reveal unique vibrations associated with the phosphoglycerate kinase-ATP-3-phosphoglycerate ternary complex
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
the enzyme favors the forward reaction
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
Spirulina geitleri
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
binding of 3-phospho-D-glycerate (or maybe 1,3-diphosphoglycerate) disrupts salt bridge between Arg148 and Glu375 and enables the formation of a new interdomain salt bridge between Arg60 and Asp197, which stabilizes the closed conformation
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
key enzyme in glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
Xanthomonas citri pv. glycines NEAU001
-
-
-
-
r
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 + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
Chrysophrys guttulatus
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
Esox sp.
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
Frog
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
absolute specificity for 3-phospho-D-glycerate
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
absolute specificity for 3-phospho-D-glycerate
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
absolute specificity for 3-phospho-D-glycerate
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
absolute specificity for 3-phospho-D-glycerate
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
simultaneous binding of both substrates is essential for domain closure
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
specific for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
specific for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
Pyrococcus woesei Vul 4 / DSM 3773
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
high specificity for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
the isolated N-terminal domain is soluble, monomeric, compactly folded, native-like in structure, and capable of binding 3-phospho-D-glycerate with high affinity
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
high specificity for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
Spirulina geitleri
-
high specificity for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
high specificity for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
high specificity for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
the enzyme plays an essential role in energy production for movement via muscle contraction in Clonorchis sinensis
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
the enzyme is required for ATP generation in the terminal stage of the glycolytic pathway. Important role of PGK in synaptic transmission. Disrupted phosphoglycerate kinase in nubian mutants causes altered ATP generation in nubian animals. Brain extracts show a threefold reduction in resting ATP levels compared with controls. Disruption of ATP generation in nubian animals is accompanied by temperature-dependent defects in neuronal activity with initial seizure activity, followed by an activity-dependent loss of synaptic transmission. Nubian mutants also diaplay structural defects at the synapse, with larger varicosity size but normal varicosity number
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
Pyrococcus woesei Vul 4 / DSM 3773
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
the reaction occurs at 30°C
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
Spirulina geitleri
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
Xanthomonas citri pv. glycines NEAU001
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate.
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate.
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate.
Pyrococcus woesei Vul 4 / DSM 3773
-
-
-
?
beta-L(-)-dioxolanecytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L(-)-dioxolanecytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
isozyme PGK1
-
-
?
beta-L(-)-dioxolanecytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L(-)-dioxolanecytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
3fold higher activity compared to 2'-deoxycytidine
-
-
?
beta-L-2',3'-dideoxy-3'-thiacytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L-2',3'-dideoxy-3'-thiacytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
isozyme PGK1
-
-
?
beta-L-2',3'-dideoxy-3'-thiacytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L-2',3'-dideoxy-3'-thiacytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
4fold higher activity compared to 2'-deoxycytidine
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
1% of the activity with ATP
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
1% of the activity with ATP
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
Spirulina geitleri
-
no activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
low activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
low activity
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
-
27% of the activity with ATP
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
-
isozymes PGK2A, PGK2B, and PGK1 show low activity, isozyme PGK2C shows 119% of the activity with ATP
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
Spirulina geitleri
-
low activity
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
-
isozyme PGK2C with lower activity, all other isozymes show slightly lower activity compared to ATP
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
Spirulina geitleri
-
no activity
-
-
?
dITP + 3-phospho-D-glycerate
dIDP + 1,3-diphosphoglycerate
-
-
-
-
?
dITP + 3-phospho-D-glycerate
dIDP + 1,3-diphosphoglycerate
Spirulina geitleri
-
no activity
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
27% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
27% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
36% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
60% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
60% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
60% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
low activity
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
Spirulina geitleri
-
very low activity
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
low activity
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
low activity
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
42% of the activity with ATP
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
42% of the activity with ATP
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
45% of the activity with ATP
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
64% of the activity with ATP
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
low activity
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
Spirulina geitleri
-
very low activity
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
Esox sp.
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
Frog
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
1% of the activity with ATP
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
1% of the activity with ATP
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
low activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
no activity
-
-
?
additional information
?
-
enzymes is confirmed by total proteome analysis of glycerol-grown cells
-
-
?
additional information
?
-
-
enzyme is identical with the socalled host factor, which activates RNA transcription in Sendai virus, when bound in a complex with host tubulin and a complementary factor
-
-
?
additional information
?
-
3-phosphoglycerate kinase catalyzes phosphoryl transfer from 1,3-biphosphoglycerate to ADP to yield 3-phosphoglycerate and ATP in substrate chain phosphorylation
-
-
?
additional information
?
-
-
3-phosphoglycerate kinase catalyzes phosphoryl transfer from 1,3-biphosphoglycerate to ADP to yield 3-phosphoglycerate and ATP in substrate chain phosphorylation
-
-
?
additional information
?
-
3-phosphoglycerate kinase catalyzes phosphoryl transfer from 1,3-biphosphoglycerate to ADP to yield 3-phosphoglycerate and ATP in substrate chain phosphorylation
-
-
?
additional information
?
-
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
?
additional information
?
-
-
the only analog of 3-phospho-D-glycerate that can replace the substrate is an artificial 3-phospho-D-glycerate in which the phosphate group-O-PO3H2 is replaced by the phosphomethyl group-CH2-PO3H2, i.e. 2-hydroxy-4-phospho-DL-butyric acid
-
-
?
additional information
?
-
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
?
additional information
?
-
Esox sp.
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
?
additional information
?
-
Frog
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
?
additional information
?
-
-
single-nucleotide polymorphisms is an adaptation to the external anoxic environment
-
-
?
additional information
?
-
-
no activity with pyrimidine nucleotides
-
-
?
additional information
?
-
-
no activity with pyrimidine nucleotides
-
-
?
additional information
?
-
-
the only analog of 3-phospho-D-glycerate that can replace the substrate is an artificial 3-phospho-D-glycerate in which the phosphate group-O-PO3H2 is replaced by the phosphomethyl group-CH2-PO3H2, i.e. 2-hydroxy-4-phospho-DL-butyric acid
-
-
?
additional information
?
-
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
?
additional information
?
-
enzyme is identical with the socalled host factor, which activates RNA transcription in Sendai virus, when bound in a complex with host tubulin and a complementary factor
-
-
?
additional information
?
-
-
enzyme is identical with the socalled host factor, which activates RNA transcription in Sendai virus, when bound in a complex with host tubulin and a complementary factor
-
-
?
additional information
?
-
-
enzyme acts as a disulfide reductase, e.g. plasmin reductase, in tumour angiogenesis
-
-
?
additional information
?
-
-
induction of multidrug resistance in cancer cell lines by overexpression of isozyme PGK1
-
-
?
additional information
?
-
-
the enzyme may be involved in the cellular activation of several antiviral nucleoside analogs including dideoxyinosine, acyclovir, L-2'-deoxycytosine and L-2'-deoxythymidine
-
-
?
additional information
?
-
-
phosphoglycerate kinase 1 is induced by hydrogen peroxide in a dose-dependent manner, while its expression is suppressed by a co-treatment with delphinidin (antioxidant). Several antioxidants, including alpha-tocopherol, butylated hydroxytoluene, and Trolox, also inhibit the PGK1 induction caused by hydrogen peroxide
-
-
?
additional information
?
-
-
Mg-ADP or Mg-beta,gamma-imido-adenosine 5'-triphosphate substitute the substrate Mg-ATP in the ternary complexes, they cannot react with 3-phospho-D-glyceroyl phosphate. Domain closure and substrate antagonism are closely related phenomena for PGK. Conformational rearrangements in the hinge generated by binding of both substrates provide the main driving force for domain closure overcoming the slightly unfavourable contact interactions between the domains
-
-
?
additional information
?
-
-
phosphorylates beta-L-dioxolane-cytidine, a novel L-configuration deoxycytidine analogue, under clinical trials for treating cancer
-
-
?
additional information
?
-
-
molecular dynamics simulations are carried out with four different nucleotides (D-/L-ADP and D-/L-CDP) in complex with hPGK and 1,3-bisphospho-D-glycerate (bPG). The binding affinities of CDPs (both enantiomers) for hPGK are found very weak while D- and L-ADP are better substrates. The binding affinity of the bPG substrate is found to be lower in presence of D-ADP than L-ADP which indicates a potential antagonistic effect on one substrate to the other
-
-
?
additional information
?
-
-
phylogenetic tree
-
-
?
additional information
?
-
-
the only analog of 3-phospho-D-glycerate that can replace the substrate is an artificial 3-phospho-D-glycerate in which the phosphate group-O-PO3H2 is replaced by the phosphomethyl group-CH2-PO3H2, i.e. 2-hydroxy-4-phospho-DL-butyric acid
-
-
?
additional information
?
-
-
Pgk1 plays some functional roles in the development of tooth germ and other embryonic organs by forming protein complex with glyceraldehyde-3-phosphate dehydrogenase
-
-
?
additional information
?
-
-
the only analog of 3-phospho-D-glycerate that can replace the substrate is an artificial 3-phospho-D-glycerate in which the phosphate group-O-PO3H2 is replaced by the phosphomethyl group-CH2-PO3H2, i.e. 2-hydroxy-4-phospho-DL-butyric acid
-
-
?
additional information
?
-
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
?
additional information
?
-
-
enzyme is identical with the socalled host factor, which activates RNA transcription in Sendai virus, when bound in a complex with host tubulin and a complementary factor
-
-
?
additional information
?
-
-
no activity with dCTP, dUTP, dTTP
-
-
?
additional information
?
-
-
2',3'-dideoxycytidine is a very poor substrate
-
-
?
additional information
?
-
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
?
additional information
?
-
-
enzyme is identical with the socalled host factor, which activates RNA transcription in Sendai virus, when bound in a complex with host tubulin and a complementary factor
-
-
?
additional information
?
-
-
pressure-jump unfolding kinetics of phosphoglycerate kinase at pressures between 50 and 150 MPa and time dependence of the conformational state of the protein followed by tryptophan fluorescence measurements from 30 s to 2 h: the activation volumes of the unfolding reaction are negative for the folded-intermediate, intermediate-unfolded, and unfolded-intermediate transitions
-
-
?
additional information
?
-
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
?
additional information
?
-
-
the oxidized PGK contains chloroplast-type thioredoxin (Trx)-accessible disulfide bond
-
-
?
additional information
?
-
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
?
additional information
?
-
trout
-
the only analog of 3-phospho-D-glycerate that can replace the substrate is an artificial 3-phospho-D-glycerate in which the phosphate group-O-PO3H2 is replaced by the phosphomethyl group-CH2-PO3H2, i.e. 2-hydroxy-4-phospho-DL-butyric acid
-
-
?
additional information
?
-
-
PGKC 3'-UTR exerts strong regulatory effects in Trypanosoma brucei. The regulatory effects are exerted at the levels of both mRNA stability and translation
-
-
?
