Literature summary for 1.1.5.3 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.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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
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

Crystallization (Comment)

Organism

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

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

Inhibitors	Comment	Organism
glyceraldehyde-3-phosphate	competitive inhibitor	Escherichia coli
glyceric acid 2-phosphate	competitive inhibitor	Escherichia coli
phosphoenolpyruvate	competitive inhibitor	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P13035	-	-

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
dimer	crystal structure	Escherichia coli

Synonyms

Synonyms	Comment	Organism
GLPD	-	Escherichia coli
sn-glycerol-3-phosphate dehydrogenase	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Escherichia coli