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Literature summary for 1.1.1.8 extracted from

  • Ruberto, A.A.; Childers, C.L.; Storey, K.B.
    Purification and properties of glycerol-3-phosphate dehydrogenase from the liver of the hibernating ground squirrel, Urocitellus richardsonii (2016), Comp. Biochem. Physiol. B, 202, 48-55.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
guanidine hydrochloride
-
Urocitellus richardsonii
guanidinium hydrochloride
-
Urocitellus richardsonii
Urea
-
Urocitellus richardsonii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic analysis, overview. Relative to euthermic liver G3PDH, hibernator liver G3PDH has a decreased affinity for its substrate, glycerol-3-phosphate, at 37°C and 22°C, while at 5°C, there is a significant increase in the affinity for G3P in the hibernating form of the enzyme, relative to the euthermic form. A change in pH from pH 8.0 to pH 7.5 leads to increased G3PDH affinity for NAD+. With a change in pH from pH 8.0 to pH 7.5 at 22°C in the euthermic and hibernator conditions, the Km for NAD+ decreases by 62% and 53%, respectively Urocitellus richardsonii
0.09
-
NAD+ pH 8.0, 5°C, hibernation G3PDH enzyme Urocitellus richardsonii
0.12
-
NAD+ pH 8.0, 5°C, euthermic G3PDH enzyme Urocitellus richardsonii
0.2
-
NAD+ enzyme from euthermic animal, at pH 7.5 and 22°C Urocitellus richardsonii
0.2
-
NAD+ enzyme from hibernating animal, at pH 7.5 and 22°C Urocitellus richardsonii
0.2
-
NAD+ pH 7.5, 22°C, euthermic G3PDH enzyme and hibernation G3PDH enzyme Urocitellus richardsonii
0.32
-
NAD+ enzyme from hibernating animal, at pH 8.0 and 37°C Urocitellus richardsonii
0.32
-
NAD+ pH 8.0, 37°C, hibernation G3PDH enzyme Urocitellus richardsonii
0.39
-
NAD+ enzyme from euthermic animal, at pH 8.0 and 37°C Urocitellus richardsonii
0.39
-
NAD+ pH 8.0, 37°C, euthermic G3PDH enzyme Urocitellus richardsonii
0.41
-
sn-glycerol 3-phosphate enzyme from hibernating animal, at pH 7.5 and 22°C Urocitellus richardsonii
0.41
-
sn-glycerol 3-phosphate pH 7.5, 22°C, hibernation G3PDH enzyme Urocitellus richardsonii
0.42
-
NAD+ enzyme from hibernating animal, at pH 8.0 and 22°C Urocitellus richardsonii
0.42
-
NAD+ pH 8.0, 22°C, hibernation G3PDH enzyme Urocitellus richardsonii
0.48
-
sn-glycerol 3-phosphate enzyme from hibernating animal, at pH 8.0 and 5°C Urocitellus richardsonii
0.48
-
sn-glycerol 3-phosphate pH 8.0, 5°C, hibernation G3PDH enzyme Urocitellus richardsonii
0.5
-
NAD+ enzyme from euthermic animal, at pH 7.5 and 37°C Urocitellus richardsonii
0.5
-
NAD+ pH 7.5, 37°C, euthermic G3PDH enzyme Urocitellus richardsonii
0.52
-
NAD+ enzyme from euthermic animal, at pH 8.0 and 22°C Urocitellus richardsonii
0.52
-
NAD+ pH 8.0, 22°C, euthermic G3PDH enzyme Urocitellus richardsonii
0.57
-
sn-glycerol 3-phosphate enzyme from euthermic animal, at pH 8.0 and 22°C Urocitellus richardsonii
0.57
-
sn-glycerol 3-phosphate pH 8.0, 22°C, euthermic G3PDH enzyme Urocitellus richardsonii
0.61
-
sn-glycerol 3-phosphate enzyme from euthermic animal, at pH 7.5 and 22°C Urocitellus richardsonii
0.61
-
sn-glycerol 3-phosphate pH 7.5, 22°C, euthermic G3PDH enzyme Urocitellus richardsonii
0.63
-
sn-glycerol 3-phosphate enzyme from euthermic animal, at pH 7.5 and 37°C Urocitellus richardsonii
0.63
-
sn-glycerol 3-phosphate pH 7.5, 37°C, euthermic G3PDH enzyme Urocitellus richardsonii
0.69
-
NAD+ enzyme from hibernating animal, at pH 7.5 and 37°C Urocitellus richardsonii
0.69
-
NAD+ pH 7.5, 37°C, hibernation G3PDH enzyme Urocitellus richardsonii
0.83
-
sn-glycerol 3-phosphate enzyme from euthermic animal, at pH 8.0 and 5°C Urocitellus richardsonii
0.83
-
sn-glycerol 3-phosphate pH 8.0, 5°C, euthermic G3PDH enzyme Urocitellus richardsonii
0.88
-
sn-glycerol 3-phosphate enzyme from euthermic animal, at pH 8.0 and 37°C Urocitellus richardsonii
0.88
-
sn-glycerol 3-phosphate pH 8.0, 37°C, euthermic G3PDH enzyme Urocitellus richardsonii
1.17
-
sn-glycerol 3-phosphate enzyme from hibernating animal, at pH 7.5 and 37°C Urocitellus richardsonii
1.17
-
sn-glycerol 3-phosphate pH 7.5, 37°C, hibernation G3PDH enzyme Urocitellus richardsonii
1.51
-
sn-glycerol 3-phosphate enzyme from euthermic animal, at pH 7.5 and 5°C Urocitellus richardsonii
1.51
-
sn-glycerol 3-phosphate pH 7.5, 5°C, euthermic G3PDH enzyme Urocitellus richardsonii
1.56
-
sn-glycerol 3-phosphate enzyme from hibernating animal, at pH 8.0 and 37°C Urocitellus richardsonii
1.56
-
sn-glycerol 3-phosphate pH 8.0, 37°C, hibernation G3PDH enzyme Urocitellus richardsonii
1.61
-
sn-glycerol 3-phosphate enzyme from hibernating animal, at pH 8.0 and 22°C Urocitellus richardsonii
1.61
-
sn-glycerol 3-phosphate pH 8.0, 22°C, hibernation G3PDH enzyme Urocitellus richardsonii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37000
-
x * 37000, SDS-PAGE Urocitellus richardsonii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Urocitellus richardsonii relative to euthermic liver G3PDH, hibernator liver G3PDH has a decreased affinity for its substrate, glycerol-3-phosphate (G3P) at 37°C and 22°C, while at 5°C, there is a significant increase in affinity for G3P in the hibernating form of the enzyme, relative to the euthermic form ?
-
?
sn-glycerol 3-phosphate + NAD+ Urocitellus richardsonii
-
glycerone phosphate + NADH + H+
-
r

Organism

Organism UniProt Comment Textmining
Urocitellus richardsonii
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein potential phosphorylation site Tyr83 is responsible for the differential phosphorylation between euthermic and hibernator G3PDH. There is a 1.70fold increase in phosphorylation of hibernating G3PDH relative to euthermic G3PDH Urocitellus richardsonii

Purification (Commentary)

Purification (Comment) Organism
hydroxyapatite column chromatography, CM-column chromatography, and Cibacron blue affinity column chromatography Urocitellus richardsonii
native enzyme from liver cell extract of euthermic and hibernating animals 272.5-273.5fold by hydroxyapatite chromatography, buffer exchange gel filtration, cation exchange chromatography, affinity chromatography, and ultrafiltration Urocitellus richardsonii

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Urocitellus richardsonii
-
liver from eurthermic and hibernating animals Urocitellus richardsonii
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.174
-
purified euthermic G3PDH enzyme, pH 8.0, 22°C Urocitellus richardsonii
2.9
-
purified hibernator G3PDH enzyme, pH 8.0, 22°C Urocitellus richardsonii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycerone phosphate + NADH + H+
-
Urocitellus richardsonii sn-glycerol 3-phosphate + NAD+
-
r
additional information relative to euthermic liver G3PDH, hibernator liver G3PDH has a decreased affinity for its substrate, glycerol-3-phosphate (G3P) at 37°C and 22°C, while at 5°C, there is a significant increase in affinity for G3P in the hibernating form of the enzyme, relative to the euthermic form Urocitellus richardsonii ?
-
?
sn-glycerol 3-phosphate + NAD+
-
Urocitellus richardsonii glycerone phosphate + NADH + H+
-
r

Subunits

Subunits Comment Organism
? x * 37000, SDS-PAGE Urocitellus richardsonii
More three-dimensional structure modeling of enzyme G3PDH to identify the potential phosphorylation site Tyr83 responsible for the differential phosphorylation between euthermic and hibernator G3PDH, predicted tertiary and quaternary structures, overview Urocitellus richardsonii

Synonyms

Synonyms Comment Organism
G3PDH
-
Urocitellus richardsonii
glycerol 3-phosphate dehydrogenase
-
Urocitellus richardsonii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5 37 assay at, glycerol 3-phosphate oxidation Urocitellus richardsonii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
the half-life at 50°C is 6.74 min in euthermic and 14.31 min in hibernating animals Urocitellus richardsonii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8 assay at, glycerol 3-phosphate oxidation Urocitellus richardsonii

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
A change in pH from pH 8.0 to pH 7.5 leads to increased G3PDH affinity for NAD+. With a change in pH from pH 8.0 to pH 7.5 at 22°C in the euthermic and hibernator conditions, the Km for NAD+ decreases by 62% and 53%, respectively Urocitellus richardsonii

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Urocitellus richardsonii
NADH
-
Urocitellus richardsonii

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.57
-
enzyme from hibernating animal, at pH 7.5 and 22°C Urocitellus richardsonii guanidine hydrochloride
0.57
-
pH 8.0, 22°C, hibernation G3PDH enzyme Urocitellus richardsonii guanidinium hydrochloride
0.69
-
enzyme from euthermic animal, at pH 7.5 and 22°C Urocitellus richardsonii guanidine hydrochloride
0.69
-
pH 8.0, 22°C, euthermic G3PDH enzyme Urocitellus richardsonii guanidinium hydrochloride
1.8
-
enzyme from hibernating animal, at pH 7.5 and 22°C Urocitellus richardsonii Urea
1.8
-
pH 8.0, 22°C, hibernation G3PDH enzyme Urocitellus richardsonii Urea
2.22
-
enzyme from euthermic animal, at pH 7.5 and 22°C Urocitellus richardsonii Urea
2.22
-
pH 8.0, 22°C, euthermic G3PDH enzyme Urocitellus richardsonii Urea

General Information

General Information Comment Organism
additional information three-dimensional structure modeling of enzyme G3PDH to identify the potential phosphorylation site (83Tyr) responsible for the differential phosphorylation between euthermic and hibernator G3PDH. Structural and functional changes in G3PDH support the enzyme's function at a low core body temperature experienced during the species hibernating season Urocitellus richardsonii
physiological function the hibernating form of G3PDH from the liver of Richardson's ground squirrels maintains better functionality at low temperatures and has greater temperature stability. These properties help sustain G3PDH function over the wide range of body temperatures experienced by the species as they cycle though torpor-arousal bouts over the hibernating season Urocitellus richardsonii