We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments This enzyme catalyses the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. The reaction occurs predominantly in the direction of reduction. The enzyme from the bacterium Escherichia coli also catalyses the activity of EC 1.1.1.399, 2-oxoglutarate reductase .
The taxonomic range for the selected organisms is: Sulfurisphaera tokodaii The enzyme appears in selected viruses and cellular organisms
Synonyms
phgdh, phosphoglycerate dehydrogenase, 3-phosphoglycerate dehydrogenase, d-3-phosphoglycerate dehydrogenase, 3-pgdh, 3pgdh, pgdh3, pgdh1, ehpgdh, d-phosphoglycerate dehydrogenase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NAD-dependent D-3-phosphoglycerate dehydrogenase
-
3-phosphoglycerate dehydrogenase
-
-
-
-
3-phosphoglyceric acid dehydrogenase
-
-
-
-
alpha-phosphoglycerate dehydrogenase
-
-
-
-
D-3-phosphoglycerate dehydrogenase
D-3-phosphoglycerate:NAD oxidoreductase
-
-
-
-
dehydrogenase, phosphoglycerate
-
-
-
-
glycerate 3-phosphate dehydrogenase
-
-
-
-
glycerate-1,3-phosphate dehydrogenase
-
-
-
-
phosphoglycerate oxidoreductase
-
-
-
-
phosphoglyceric acid dehydrogenase
-
-
-
-
D-3-phosphoglycerate dehydrogenase
-
-
-
-
D-3-phosphoglycerate dehydrogenase
-
-
PGDH
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-phospho-D-glycerate:NAD+ 2-oxidoreductase
This enzyme catalyses the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. The reaction occurs predominantly in the direction of reduction. The enzyme from the bacterium Escherichia coli also catalyses the activity of EC 1.1.1.399, 2-oxoglutarate reductase [6].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-phospho-D-glycerate + NAD+
2-phosphohydroxypyruvate + NADH + H+
-
activity relative to 3-phospho-D-glycerate: 47%
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH + H+
-
highest activity
-
-
r
3-phospho-D-glycerate + NADP+
3-phosphohydroxypyruvate + NADPH + H+
-
-
-
-
r
DL-glyceraldehyde 3-phosphate + NAD+
?
-
activity relative to 3-phospho-D-glycerate: 9%
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NADP+
-
NADP utilization is not observed in the forward reaction even in the presence of high concentrations of 10 mM NADP and 10 mM 3-phospho-D-glycerate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(NH4)2SO4
-
inhibitory effect on NADPH-dependent 3-phosphohydroxypyruvate reduction
ADP
-
weak inhibitory effect on 3-phospho-D-glycerate oxidation, remaining activity: 86%
AMP
-
weak inhibitory effect on 3-phospho-D-glycerate oxidation, remaining activity: 75%
ATP
-
weak inhibitory effect on 3-phospho-D-glycerate oxidation, remaining activity: 85%
K2HPO4
-
inhibitory effect on NADPH-dependent 3-phosphohydroxypyruvate reduction. It appears that the phosphate ion PO43- exerts its inhibitory effect by binding to the free enzyme and NADPH-enzyme complex
ZnCl2
-
inhibitory effect on 3-phosphohydroxypyruvate reduction, remaining activity: 29%
additional information
-
unlike the Escherichia coli PGDH no inhibition by L-serine
-
3-phosphohydroxypyruvate
-
product inhibition of 3-phospho-D-glycerate oxidation, variable substrate: 3-phospho-D-glycerate, inhibition pattern: competitive
3-phosphohydroxypyruvate
-
product inhibition of 3-phospho-D-glycerate oxidation, variable substrate: NAD, inhibition pattern: non-competitive
NADH
-
product inhibition of 3-phospho-D-glycerate oxidation, variable substrate: 3-phospho-D-glycerate, inhibition pattern: non-competitive
NADH
-
product inhibition of 3-phospho-D-glycerate oxidation, variable substrate: NAD, inhibition pattern: competitive
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(NH4)2SO4
-
enhancing effect on NAD-dependent 3-phospho-D-glycerate oxidation and 3-phosphohydroxypyruvate reduction but inhibitory effect on NADPH-dependent 3-phosphohydroxypyruvate reduction
K2HPO4
-
enhancing effect on NAD-dependent 3-phospho-D-glycerate oxidation and 3-phosphohydroxypyruvate reduction but inhibitory effect on NADPH-dependent 3-phosphohydroxypyruvate reduction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.033
3-phospho-D-glycerate
-
value for 3-phospho-D-glycerate oxidation using NAD+ as a cofactor
0.0096 - 0.12
3-phosphohydroxypyruvate
0.04
NAD+
-
value for 3-phospho-D-glycerate oxidation
0.0013
NADH
-
value for 3-phosphohydroxypyruvate reduction using NADH as a cofactor
0.02
NADPH
-
value for 3-phosphohydroxypyruvate reduction using NADPH as a cofactor
0.0096
3-phosphohydroxypyruvate
-
value for 3-phosphohydroxypyruvate reduction using NADH as a cofactor
0.12
3-phosphohydroxypyruvate
-
value for 3-phosphohydroxypyruvate reduction using NADPH as a cofactor
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2
K2HPO4
-
value of phosphate against 3-phosphohydroxypyruvate
10
K2HPO4
-
value of phosphate against NADPH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
during purification an unexpected decline in enzyme activity is observed if the enzyme is stored in plastic tubes, but not in glass ones
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10
-
3-phospho-D-glycerate oxidation
7.5
-
3-phosphohydroxypyruvate reduction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
53
-
optimum temperature for 3-phospho-D-glycerate oxidation
80
-
optimum for 3-phosphohydroxypyruvate reduction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
homodimer
-
gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
crystal structure is determined using X-ray diffraction to resolution of 1.77 A, crystals are grown at room temperature by sitting-drop method
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3.5 - 11.5
-
enzyme is stable over a wide range of pHs. No decrease in activity after 20 min incubation at 50°C
684698
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
50 - 80
-
enzyme is highly thermostable, retaining more than 90% of its activity after incubation for 1 h at 80°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
enzyme is highly thermostable
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
using a butyl Sepharose 4 Fast Flow column and a Superdex 200 gel filtration column. During purification an unexpected decline in enzyme activity is observed if the enzyme is stored in plastic tubes, but not in glass ones
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expression in Escheriochia coli BL21
expressed in Escherichia coli
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Shimizu, Y.; Sakuraba, H.; Doi, K.; Ohshima, T.
Molecular and functional characterization of D-3-phosphoglycerate dehydrogenase in the serine biosynthetic pathway of the hyperthermophilic archaeon Sulfolobus tokodaii
Arch. Biochem. Biophys.
470
120-128
2008
Sulfurisphaera tokodaii
brenda
Kumar, S.M.; Pampa, K.J.; Manjula, M.; Hemantha Kumar, G.; Kunishima, N.; Lokanath, N.K.
Crystal structures of type IIIH NAD-dependent D-3-phosphoglycerate dehydrogenase from two thermophiles
Biochem. Biophys. Res. Commun.
451
126-130
2014
Pyrococcus horikoshii (O58256), Pyrococcus horikoshii, Sulfurisphaera tokodaii (Q972A9), Sulfurisphaera tokodaii, Pyrococcus horikoshii DSM 12428 (O58256)
brenda