1.1.5.3: glycerol-3-phosphate dehydrogenase

This is an abbreviated version!
For detailed information about glycerol-3-phosphate dehydrogenase, go to the full flat file.

Reaction

Synonyms

DsFAD-GPDH, EC 1.1.2.1, EC 1.1.99.5, FAD-dependent glycerol-3-phosphate dehydrogenase, FAD-G3PDH, FAD-glycerol phosphate dehydrogenase, FAD-GPDH, FAD-linked glycerol-3-phosphate dehydrogenase, flavin adenine dinucleotide-dependent glycerol-3-phosphate dehydrogenase, flavin-linked glycerol-3-phosphate ubiquinone oxidoreductase, flavoprotein-dependent glycerol-3-phosphate dehydrogenase, G3PD, GDP, GLPD, GlpO, glycerol-3-phosphate dehydrogenase, glycerol-3-phosphate dehydrogenase 1, glycerol-3-phosphate dehydrogenase 2, glycerol-3-phosphate oxidoreductase, glycerophosphate dehydrogenase, GmGPDH12, GPD1, GPD2, GPDH, mGPDH, mitochondrial glycerol-3-phosphate dehydrogenase, mitochondrial sn-glycerol 3-phosphate dehydrogenase, mtG3PDH, putG3PDH, SDP6, sn-glycerol 3-phosphate dehydrogenase, sn-glycerol-3-phosphate dehydrogenase, ZmGPDH6

ECTree

     1 Oxidoreductases

         1.1 Acting on the CH-OH group of donors

             1.1.5 With a quinone or similar compound as acceptor

                1.1.5.3 glycerol-3-phosphate dehydrogenase

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Results	in table
10	Activating Compound
32033	AA Sequence
1	CAS Registry Number
5	Cloned(Commentary)
31	Cofactor
3	Crystallization (Commentary)
290	Disease/ Diagnostics
2	Expression
17	General Information
2	General Stability
10	IC50 Value
111	Inhibitors
4	Ki Value [mM]
27	KM Value [mM]
39	Localization
21	Metals/Ions
16	Molecular Weight [Da]
25	Natural Substrates/ Products (Substrates)
217	Organism
12	Pathway
4	pH Optimum
1	pH Stability
1	pI Value
7	Posttranslational Modification
13	Purification (Commentary)
2	Reaction
47	Reference
42	Source Tissue
5	Specific Activity [micromol/min/mg]
4	Storage Stability
98	Substrates and Products (Substrate)
12	Subunits
72	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
1	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.1.5.3 - glycerol-3-phosphate dehydrogenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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

P13035

689802

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

P13035

689802

structure of a deletion mutant of Streptococcus sp. GlpO (GlpODELTA, lacking a 50-residue insert that includes a flexible surface region) is determined using multiwavelength anomalous dispersion data and refined at 2.3 A resolution

Streptococcus sp.

-

685288