1.1.1.8: glycerol-3-phosphate dehydrogenase (NAD+)

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

Word Map on EC 1.1.1.8

1.1.1.8

adipose

adipocytes

dhap

preadipocytes

alpha-gpdh

3-phosphatase

phosphodianion

fad-linked

synthesis

food industry

nutrition

medicine

biotechnology

Reaction

Synonyms

(NAD+)-dependent G3pdh, (NAD+)-dependent glycerol-3-phosphate dehydrogenase, 100383152, alpha glycerophosphate dehydrogenase, alpha-glycerol phosphate dehydrogenase (NAD), alpha-glycerophosphate dehydrogenase (NAD), Cagpd1, Cagpd1p, Cagpd2, Cagpd2p, cG3PDH, CgGPD, cGPdH, cytoplasmic NAD-dependent glycerol-3-phosphate dehydrogenase, cytosolic GPDH, dehydrogenase, glycerol phosphate, DhGPD1, G-3-P dehydrogenase, G3P dehydrogenase, G3PD, G3PD1, G3PD2, G3PD3, G3PDH, GDM, GDP2, GLPD, GLY1, glycerol 1-phosphate dehydrogenase, glycerol 3-phosphate dehydrogenase, glycerol 3-phosphate dehydrogenase 1, glycerol phosphate dehydrogenase (NAD), glycerol-3-phosphate dehydrogenase, glycerol-3-phosphate dehydrogenase 1, glycerophosphate dehydrogenase (NAD), GPD, GPD1, Gpd1p, gpd2p, GPDH, GPDH-1, GPDH-2, GPDH1, GPDH2, GPDH3, GPDH4, GPDH5, GPDH: NAD+ 2 oxidoreductase, GPDH: NAD+ 2 oxidorreductase, GPDHc1, GRMZM2G090747_T01, GRMZM2G155348_T01, GRMZM2G173195_T01, GRMZM6G161711_T01, hydroglycerophosphate dehydrogenase, L-alpha-glycerol phosphate dehydrogenase, L-alpha-glycerophosphate dehydrogenase, L-glycerol 3-phosphate dehydrogenase, L-glycerol phosphate dehydrogenase, L-glycerophosphate dehydrogenase, mGPDH, NAD+-dependent G3P dehydrogenase, NAD+-dependent glycerol 3-phosphate dehydrogenase, NAD+-dependent glycerol-3-phosphate dehydrogenase, NAD+-GPDH, NAD-alpha-glycerophosphate dehydrogenase, NAD-dependent cG3PDH, NAD-dependent glycerol phosphate dehydrogenase, NAD-dependent glycerol-3-phosphate dehydrogenase, NAD-L-glycerol-3-phosphate dehydrogenase, NAD-linked glycerol 3-phosphate dehydrogenase, NADH-dihydroxyacetone phosphate reductase, NADP+-dependent glycerol 3-phosphate dehydrogenase, SFD1, SFD1/GLY1, ZEAMMB73_Zm00001d010670, ZEAMMB73_Zm00001d041962, ZEAMMB73_Zm00001d042152, ZmGPDH1, ZmGPDH3, ZmGPDH4, ZmGPDH5

ECTree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.1.1 With NAD⁺ or NADP⁺ as acceptor

1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+)

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Results	in table
18	Activating Compound
7732	AA Sequence
16	Application
1	CAS Registry Number
28	Cloned(Commentary)
138	Cofactor
9	Crystallization (Commentary)
213	Disease/ Diagnostics
20	Expression
50	General Information
31	General Stability
14	IC50 Value
123	Inhibitors
16	kcat/KM [mM/s]
3	Ki Value [mM]
160	KM Value [mM]
51	Localization
4	Metals/Ions
59	Molecular Weight [Da]
83	Natural Substrates/ Products (Substrates)
399	Organism
5	Pathway
32	PDB ID
33	pH Optimum
18	pH Range
13	pH Stability
6	pI Value
2	Posttranslational Modification
12	Protein Variants
47	Purification (Commentary)
12	Reaction
3	Reaction Type
141	Reference
129	Source Tissue
47	Specific Activity [micromol/min/mg]
22	Storage Stability
166	Substrates and Products (Substrate)
50	Subunits
207	Synonyms
1	Systematic Name
15	Temperature Optimum [°C]
28	Temperature Stability [°C]
15	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.1.1.8 - glycerol-3-phosphate dehydrogenase (NAD+)

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Apis mellifera

287338

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

hanging-drop vapor-diffusion method enzyme/NAD+ complex, enzyme/dihydroxyacetonephosphate complex, enzyme/NAD+/dihydroxyacetonephosphate complex

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

Q00055

721219

homology modeling of structure

Zea mays

A0A1D6HW80, A0A345VNI9, B4FA85, B4FVR2, B4FZV9

762241