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Literature summary for 1.2.1.12 extracted from

  • Cook, W.; Senkovich, O.; Chattopadhyay, D.
    An unexpected phosphate binding site in glyceraldehyde 3-phosphate dehydrogenase: Crystal structures of apo, holo and ternary complex of Cryptosporidium parvum enzyme (2009), BMC Struct. Biol., 9, 09.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Cryptosporidium parvum

Crystallization (Commentary)

Crystallization (Comment) Organism
structure in absence and presence of NAD+ and structure of the ternary enzyme-cofoactor-substrate complex to 2.0 A resolution. The active site can accomodate the substrate in multiple conformations at multiple locations during the initial encounter. the C-3 phosphate group clearly prefers the so-called new phosphate site for initial binding Cryptosporidium parvum

Protein Variants

Protein Variants Comment Organism
C153S about 450fold decrease in activity Cryptosporidium parvum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000032
-
 NAD+
-
 Cryptosporidium parvum
0.762
-
 D-glyceraldehyde 3-phosphate
-
 Cryptosporidium parvum

Organism

Organism UniProt Comment Textmining
Cryptosporidium parvum Q7YYQ9
-
-

Substrates and Products (Substrate)

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