Literature summary for 1.2.1.12 extracted from

Frayne, J.; Taylor, A.; Cameron, G.; Hadfield, A.T.
Structure of insoluble rat sperm glyceraldehyde-3-phosphate dehydrogenase (GAPDH) via heterotetramer formation with Escherichia coli GAPDH reveals target for contraceptive design (2009), J. Biol. Chem., 284, 22703-22712.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure determination by formation of soluble recombinant rat sperm glyceraldehyde-3-phosphate dehydrogenase as a heterotetramer with the Escherichia coli glyceraldehyde-3-phosphate dehydrogenase in a ratio of 1:3. Glyceraldehyde 3-phosphate binds in the Ps pocket in the active site of the sperm enzyme subunit in the presence of NAD	Escherichia coli
structure determination by formation of soluble recombinant rat sperm glyceraldehyde-3-phosphate dehydrogenase as a heterotetramer with the Escherichia coli glyceraldehyde-3-phosphate dehydrogenase in a ratio of 1:3. Refinement to 2.2 A for the holo enzyme, to 2.4 A for the complex with glyceraldehyde 3-phosphate. Glyceraldehyde 3-phosphate binds in the Ps pocket in the active site of the sperm enzyme subunit in the presence of NAD	Rattus norvegicus

Crystallization (Comment)

Organism

structure determination by formation of soluble recombinant rat sperm glyceraldehyde-3-phosphate dehydrogenase as a heterotetramer with the Escherichia coli glyceraldehyde-3-phosphate dehydrogenase in a ratio of 1:3. Glyceraldehyde 3-phosphate binds in the Ps pocket in the active site of the sperm enzyme subunit in the presence of NAD

Escherichia coli

structure determination by formation of soluble recombinant rat sperm glyceraldehyde-3-phosphate dehydrogenase as a heterotetramer with the Escherichia coli glyceraldehyde-3-phosphate dehydrogenase in a ratio of 1:3. Refinement to 2.2 A for the holo enzyme, to 2.4 A for the complex with glyceraldehyde 3-phosphate. Glyceraldehyde 3-phosphate binds in the Ps pocket in the active site of the sperm enzyme subunit in the presence of NAD

Rattus norvegicus

Inhibitors

Inhibitors	Comment	Organism	Structure
alpha-chlorohydrin	the contraceptive activity of alpha-chlorohydrin and its apparent specificity for the sperm isoform in vivo are likely to be due to differences in metabolism to 3-chlorolactaldehyde in spermatozoa and somatic cells	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A9B2	-	-
Rattus norvegicus	Q9ESV6	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
sperm	-	Rattus norvegicus	-

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Release 2023.1 (January 2023)