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]

General Information

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

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

malfunction

Chlamydomonas reinhardtii

P50362

the enzyme GapDH interacts with the intrinsically disordered protein CP12, when oxidized but not when reduced, in chloroplasts forming a stable complex. In this bienzyme complex, the activity of ADK3 is unchanged while the NADPH-dependent activity of GAPDH is significantly inhibited. The ADK3-GAPDH bienzyme complex is unable to recruit phosphoribulokinase (PRK), in contrast with the ternary complex formed between GAPDH-CP12 and PRK. The interaction between ADK3 and GAPDH might be a mechanism to regulate the crucial ATP: NADPH ratio within chloroplasts to optimize the Calvin-Benson cycle during rapid fluctuation in environmental resources

763014

physiological function

7 entries

additional information

5 entries

physiological function

Corynebacterium glutamicum

Q01651

glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an enzyme that catalyzes an inevitable step in the central metabolism of most industrially important sugars such as glucose, fructose and sucrose. During the glycolysis of 1 mol glucose and 2 mol of NAD(P)H are generated at this enzymatic reaction with the oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate

743222

physiological function

Streptococcus agalactiae

Q8E3E8

the enzyme plays a key role in glycolysis. GAPDH localized on the surface of some bacteria is thought to be involved in macromolecular interactions and bacterial pathogenesis. GAPDH on the surface of group B streptococcus (GBS) enhances bacterial virulence and is a potential vaccine candidate

741524

physiological function

Chlamydomonas reinhardtii

P50362

in Chlamydomonas reinhardtii, the chloroplast GAPDH is a homotetrameric A4-isoform that lacks regulatory cysteine residues found in the B subunit of the heterotetrameric A2B2-GAPDH isoform. Whereas A2B2-GAPDHs from higher plants are autonomously regulated, CP12 is required to confer redox regulation to the algal A4-GAPDH. In contrast, the CP12-like tail bearing two cysteine residues present on ADK3 is not involved in its redoxregulation

763014

physiological function

Campylobacter jejuni

A0A1E7PFR0

phosphorylating glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is a ubiquitous cellular enzyme that has a defined role in glycolysis and other pathways where it catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate. The enzyme complexes with ADP and might be moonlighting

763374

physiological function

Corynebacterium glutamicum ATCC 13032

-

glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an enzyme that catalyzes an inevitable step in the central metabolism of most industrially important sugars such as glucose, fructose and sucrose. During the glycolysis of 1 mol glucose and 2 mol of NAD(P)H are generated at this enzymatic reaction with the oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate

-

physiological function

Streptococcus agalactiae NEM316

-

the enzyme plays a key role in glycolysis. GAPDH localized on the surface of some bacteria is thought to be involved in macromolecular interactions and bacterial pathogenesis. GAPDH on the surface of group B streptococcus (GBS) enhances bacterial virulence and is a potential vaccine candidate

-

physiological function

Corynebacterium glutamicum ATCC13032

-

glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an enzyme that catalyzes an inevitable step in the central metabolism of most industrially important sugars such as glucose, fructose and sucrose. During the glycolysis of 1 mol glucose and 2 mol of NAD(P)H are generated at this enzymatic reaction with the oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate

-

additional information

Chlamydomonas reinhardtii

P50362

ADK3, like CP12, can protect GAPDH against thermal inactivation and aggregation. CP12 acts as a chaperone for GAPDH. Detection o f a solubilizing effect of ADK3 on GAPDH

763014

additional information

Chlamydomonas reinhardtii

-

ADK3, like CP12, can protect GAPDH against thermal inactivation and aggregation. CP12 acts as a chaperone for GAPDH. Detection o f a solubilizing effect of ADK3 on GAPDH

763014

additional information

Thermoanaerobacterium saccharolyticum

I3VY89

comparison of Gapdh protein from Clostridium thermocellum and Thermoanaerobacterium saccharolyticum, homology modeling, overview. The Gapdh from Thermoanaerobacterium saccharolyticum is less sensitive to ethanol and the NAD+/NADH ratio. Recombinant Gapdh from Thermoanaerobacterium saccharolyticum expressed in Clostridium thermocellum cells can improve the growth rate and ethanol resistance

762842

additional information

Thermoanaerobacterium saccharolyticum DSM 8691

-

comparison of Gapdh protein from Clostridium thermocellum and Thermoanaerobacterium saccharolyticum, homology modeling, overview. The Gapdh from Thermoanaerobacterium saccharolyticum is less sensitive to ethanol and the NAD+/NADH ratio. Recombinant Gapdh from Thermoanaerobacterium saccharolyticum expressed in Clostridium thermocellum cells can improve the growth rate and ethanol resistance

-

additional information

Thermoanaerobacterium saccharolyticum JW/SL-YS485

-

comparison of Gapdh protein from Clostridium thermocellum and Thermoanaerobacterium saccharolyticum, homology modeling, overview. The Gapdh from Thermoanaerobacterium saccharolyticum is less sensitive to ethanol and the NAD+/NADH ratio. Recombinant Gapdh from Thermoanaerobacterium saccharolyticum expressed in Clostridium thermocellum cells can improve the growth rate and ethanol resistance

-