1.2.1.59: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)

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For detailed information about glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating), go to the full flat file.

Reaction

Synonyms

cgap, chloroplast glyceraldehyde-3-phosphate dehydrogenase, CjGAPDH, Dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide (phosphate)), GAP, GapA, GapB, GAPC, GAPDH, GAPDH2, GBS GAPDH, glyceraldehyde 3-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (NAD(P)), NAD(NADP)-dependent glyceraldehyde-3-phosphate dehydrogenase, NAD(P)-dependent G3P dehydrogenase, NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase, NADP-dependent glyceraldehyde 3-phosphate dehydrogenase, NADP-dependent glyceraldehyde-3-phosphate dehydrogenase, NADP-dependent glyceraldehydephosphate dehydrogenase, pcal_0632, phosphorylating glyceraldehyde-3-phosphate dehydrogenase, STK_13560, Triosephosphate dehydrogenase (NAD(P)), Tsac_2486

ECTree

     1 Oxidoreductases

         1.2 Acting on the aldehyde or oxo group of donors

             1.2.1 With NAD⁺ or NADP⁺ as acceptor

                1.2.1.59 glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)

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Results	in table
16	Activating Compound
3336	AA Sequence
3	Application
1	CAS Registry Number
12	Cloned(Commentary)
25	Cofactor
5	Crystallization (Commentary)
2	Expression
12	General Information
5	General Stability
14	Inhibitors
10	kcat/KM [mM/s]
7	Ki Value [mM]
36	KM Value [mM]
6	Localization
4	Metals/Ions
6	Molecular Weight [Da]
38	Natural Substrates/ Products (Substrates)
63	Organism
7	Pathway
6	PDB ID
7	pH Optimum
2	pH Range
18	Protein Variants
9	Purification (Commentary)
3	Reaction
2	Reaction Type
44	Reference
15	Source Tissue
6	Specific Activity [micromol/min/mg]
83	Substrates and Products (Substrate)
7	Subunits
65	Synonyms
1	Systematic Name
7	Temperature Optimum [°C]
1	Temperature Range [°C]
6	Temperature Stability [°C]
10	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.2.1.59 - glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

purified enzyme in complex with ADP, NAD+, and NADP+, X-ray diffraction structure determination and analysis at 2.05-2.25 A resolution

Campylobacter jejuni

A0A1E7PFR0

763374

wild type and mutant enzyme C150S, sitting drop vapor diffusion method, using 25% (w/v) PEG 1K, 175 mM sodium/potassium tartrate and 100 mM sodium acetate pH 4.5

Campylobacter jejuni

-

723857

crystal structure is determined to 1.81 A resolution. The crystal belongs to space group C222(1), with unit-cell parameters a = 83.4, b = 152.0, c = 118.6 A. Crystallization is performed using the microbatch-under-oil method at 18°C

Methanocaldococcus jannaschii

Q58546

726605

-

Methanothermus fervidus

-

11539

purified His-tagged enzyme in complex with NAD+, microseeding method, mixing of 8.9 mg/ml protein in 25 mM HEPES, pH 7.35, 0.1 M NaCl, and 5 mM 2-mercaptoethanol, with crystallization solution containing 26-36% PEG 4000, 0.1 M MES, pH 6.5, the needle-like crystals are used for microseeding by mixing 0.002 ml of protein plus cofactor mixture, 500 nl water and 500 nl reservoir solution containing seed suspension in 28% PEG 4000, 0.1 M MES, pH 6.5, X-ray diffraction structure determination and analysis at 2.46 A resolution, molecular replacement and modelling

Streptococcus agalactiae

Q8E3E8

741524