Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.2.1.12 extracted from

  • Berni, R.; Mozzarelli, A.; Rossi, G.L.; Bolognesi, M.; Oberti, R.
    Crystallographic symmetry and coenzyme binding properties of D-glyceraldehyde-3-phosphate dehydrogenase from the tail muscle of Palinurus vulgaris (1979), J. Biol. Chem., 254, 8004-8006.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Palinurus vulgaris

Organism

Organism UniProt Comment Textmining
Palinurus vulgaris
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle tail muscle Palinurus vulgaris
-

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
NAD+ the binding of NAD+ to apoenzyme in solution at 25°C is anticooperative Palinurus vulgaris