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Literature summary for 1.2.1.12 extracted from

  • Perez, A.; Wolfe, J.; Schermerhorn, J.; Qian, Y.; Cela, B.; Kalinowski, C.; Largoza, G.; Fields, P.; Brandt, G.
    Thermal stability and structure of glyceraldehyde-3-phosphate dehydrogenase from the coral Acropora millepora (2021), RSC Adv., 11, 10364-10374 .
No PubMed abstract available
Search for more literature for 1.2.1.12

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray diffraction structure determination and analysis at 2.4 A resolution, structure modeling Acropora millepora

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+ Acropora millepora
-
 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Acropora millepora A0A3F2YLZ0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Acropora millepora 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?

Subunits

Subunits Comment Organism
homotetramer
-
 Acropora millepora

Synonyms

Synonyms Comment Organism
glyceraldehyde-3-phosphate dehydrogenase
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 Acropora millepora

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 the thermal stability of glyceraldehyde-3-phosphate dehydrogenase increases significantly in the presence of its cofactor NAD+. Incubation of Acropora millepora GAPDH with NAD+ increases its melting temperature by 15°C Acropora millepora
63.2
-
 enzyme without NAD+ Acropora millepora
78.4
-
 NAD+-bound enzyme Acropora millepora

Cofactor

Cofactor Comment Organism Structure
NAD+ analysis of the structure of the cofactor-enzyme complex (PDB ID 6PX2) reveals variable NAD+ occupancy across the four monomers of the tetrameric enzyme. The NAD+ binding sites of the tetramer are occupied to different extents, overview Acropora millepora

General Information

General Information Comment Organism
metabolism glyceraldehyde-3-phosphate dehydrogenase is a critical metabolic enzyme in the stony coral Acropora millepora Acropora millepora
additional information the GAPDH enzyme from the reef-building stony coral Acropora millepora is a rather typical eukaryotic GAPDH, comprising an N-terminal NAD+-binding Rossman fold and a catalytic domain that provides important active site residues Acropora millepora