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

BRENDA support

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

Reaction

ATP
+
3-phospho-D-glycerate
=
ADP
+
3-phospho-D-glyceroyl phosphate

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 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.2 Phosphotransferases with a carboxy group as acceptor
                2.7.2.3 phosphoglycerate kinase

Temperature Stability

Temperature Stability on EC 2.7.2.3 - phosphoglycerate kinase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
104
half-life: 10 min
24
-
two stable, folded conformers with an abrupt conformational transition occurring at 24°C. The transition state thermodynamics for the low- to high-temperature conformational change are calculated from slow-scan-rate differential scanning calorimetry measurements where it is found that the free energy barrier for the conversion is 90 kJ/mol and the transition state possesses a significant unfolding quality
25
-
30 min, 27% loss of activity
30 - 40
recombinant enzyme, highly stable at
37
-
30 min, nearly 80% loss of activity
47
-
midpoint temperature Tm, without a ligand, carboxamidomethylated enzyme, value determined by differential scanning calometry
52.5
melting temperature
52.8
-
Tm (wild-type): 52.8°C, t1/2 (wild-type, 37°C): 3 years
54
-
midpoint temperature Tm, mutant enzyme W308F/W333F, with 3-phosphoglycerate and MgADP- as ligand, value determined by differential scanning calometry
55
-
midpoint temperature Tm, with MgATP2- as ligand, unmodified enzyme, value determined by differential scanning calometry
58
-
midpoint temperature Tm, with 3-phosphoglycerate as ligand, unmodified enzyme, value determined by differential scanning calometry
63
-
midpoint temperature Tm, with 3-phosphoglycerate and MgADP- as ligand, wild-type enzyme, value determined by differential scanning calometry
79
-
20 min, no loss of activity
83
half-life: 44 min
86
half-life: 44 min
89
half-life: 10 min
92
-
5 min, 75% loss of activity
additional information