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Literature summary extracted from

  • Yeh, J.I.; Chinte, U.; Du, S.
    Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism (2008), Proc. Natl. Acad. Sci. USA, 105, 3280-3285.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.8 purified GlpD is concentrated to 8 mg/ml and crystallized at 4°C from a solution containing 0.1 M diammonium hydrogen phosphate, 0.1 M Bicine pH 8.5, and 12% w/v PEG 6000. Structure of the native enzyme, structures of enzyme complexed with substrate analogues phosphoenolpyruvate, glyceric acid 2-phosphate, glyceraldehyde-3-phosphate, and product, dihydroxyacetone phosphate Escherichia coli
1.1.5.3 crystal structure analysis: GlpD comprises two major domains, a soluble extramembraneous C-terminal cap domain (residues 389-501) and a N-terminal FAD-binding region, consisting of the substrate binding and base regions (residues 1-388). The dimeric enzyme is formed by monomers related by a noncrystallographic 2fold axis of symmetry and the dimer comprises the unique asymmetric unit. Electrostatic surface calculations show distinct regions of highly positive patches, located at the base region of the enzyme. These regions are likely involved with the negatively charged membrane phospholipid head groups. The cap domain, at the opposite side, exhibits highly negatively electrostatic potential, with large hydrophobic patches between these two distal regions of the enzyme, forming membrane interaction and proposed UQ-binding surfaces Escherichia coli
1.1.5.3 structure of the native enzyme and in complex with dihydroxyacetone phosphate (2.1 A) and in separate complexes with substrate analogues, glyceraldehyde-3-phosphate (2.9 A), glyceric acid 2-phosphate (2.3 A), and phosphoenolpyruvate (2.1 A) are determined. Additionally, in complex with ubiquinone analogues, menadione (2.6 A) and 2-n-heptyl-4-hydroxyquinoline N-oxide (2.9 A) Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.5.3 glyceraldehyde-3-phosphate competitive inhibitor Escherichia coli
1.1.5.3 glyceric acid 2-phosphate competitive inhibitor Escherichia coli
1.1.5.3 phosphoenolpyruvate competitive inhibitor Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.8 Escherichia coli
-
-
-
1.1.5.3 Escherichia coli P13035
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.8
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.3 glyceraldehyde-3-phosphate + NAD(P)+ crystal structure with complexed substrate analogue is determined Escherichia coli ?
-
 ?
1.1.5.3 glyceric acid 2-phosphate + NAD(P)+ crystal structure with complexed substrate analogue is determined Escherichia coli ?
-
 ?
1.1.5.3 phosphoenolpyruvate + NAD(P)+ crystal structure with complexed substrate analogue is determined Escherichia coli ?
-
 ?
1.1.5.3 sn-glycerol 3-phosphate + NAD(P)+
-
 Escherichia coli glycerone phosphate + NAD(P)H + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.5.3 dimer crystal structure Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.1.1.8 GLPD
-
 Escherichia coli
1.1.5.3 GLPD
-
 Escherichia coli
1.1.5.3 sn-glycerol-3-phosphate dehydrogenase
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.3 FAD
-
 Escherichia coli