Literature summary for 1.2.1.12 extracted from

Yamaguchi, M.; Tsuchiya, Y.; Hishinuma, K.; Chikuma, T.; Hojo, H.
Conformational change of glyceraldehyde-3-phosphate dehydrogenase induced by acetylleucine chloromethyl ketone is followed by unique enzymatic degradation (2003), Biol. Pharm. Bull., 26, 1648-1651.

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General Stability

General Stability	Organism
acetylleucine chloromethyl ketone binds to GAPDH to modulate the conformation of the enzyme, the modified enzyme is susceptible to chymotrypsin-like protease activity, cleavage at TRp195-Arg196	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
acetylleucine chloromethyl ketone	binds to GAPDH to modulate the conformation of the enzyme, the modified enzyme is susceptible to chymotrypsin-like protease activity, cleavage at TRp195-Arg196; irreversible inhibition, enzyme modified by acetylleucine chloromethyl ketone is deduced to be digested at the peptide bond Trp196-Arg196	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
U-937 cell	-	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
GAPDH	-	Homo sapiens

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Release 2023.1 (January 2023)