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Literature summary for 1.1.1.8 extracted from

  • Alarcon, D.A.; Nandi, M.; Carpena, X.; Fita, I.; Loewen, P.C.
    Structure of glycerol-3-phosphate dehydrogenase (GPD1) from Saccharomyces cerevisiae at 2.45 A resolution (2012), Acta Crystallogr. Sect. F, 68, 1279-1283.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene YDL022W, phylogenetic analysis, expression in Escherichia coli strain BL21 Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant untagged enzyme, hanging drop vapour diffusion method using a reservoir solution consisting of 12% PEG 8000, 0.1 M Tris-HCl, pH 8.5, 0.3 M MgCl2, X-ray diffraction structure determination and analysis at 2.45 A resolution, molecular replacement and modeling Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Saccharomyces cerevisiae 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sn-glycerol 3-phosphate + NAD+ Saccharomyces cerevisiae
-
glycerone phosphate + NADH + H+
-
r

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q00055 gene YDL022W encoding GPD1
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain BL21 by anion exchange chromatography to over 95% purity Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sn-glycerol 3-phosphate + NAD+
-
Saccharomyces cerevisiae glycerone phosphate + NADH + H+
-
r

Subunits

Subunits Comment Organism
More the enzyme monomer is organized with N- and C-terminal domains. The N-terminal domain contains a classic Rossmann fold with the (beta-alpha-beta-alpha-beta)2 motif typical of many NAD+-dependent enzymes, while the C-terminal domain is mainly alpha-helical, structure comparisons, overview Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
glycerol-3-phosphate dehydrogenase
-
Saccharomyces cerevisiae
GPD1
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Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
NAD+ dependent on Saccharomyces cerevisiae
NADH dependent on Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution structural and phylogenetic comparisons reveal four main structure types among the five families of glycerol-3-phosphate and glycerol-1-phosphate dehydrogenases, overview Saccharomyces cerevisiae
metabolism the interconversion of glycerol 3-phosphate and dihydroxyacetone phosphate by glycerol-3-phosphate dehydrogenases provides a link between carbohydrate and lipid metabolism. Glycerol 3-phosphate from the breakdown of phospholipids and triglycerides (via glycerol kinase) is converted into the glycolysis intermediate dihydroxyacetone phosphate, while the reverse reaction produces glycerol 3-phosphate, which is required for the synthesis of triglycerides and phospholipids Saccharomyces cerevisiae
physiological function the interconversion of glycerol 3-phosphate and dihydroxyacetone phosphate by glycerol-3-phosphate dehydrogenases provides Saccharomyces cerevisiae with protection against osmotic and anoxic stress. The concerted action of cytosolic (NAD+-dependent) G3PDHs and membrane-bound (FAD-dependent) G3PDHs transfers reducing equivalents from cytosolic NADH into the electron-transport chain of both bacteria and mitochondria Saccharomyces cerevisiae