Literature summary for 3.2.1.1 extracted from

Zhuo, H.; Payan, F.; Qian, M.
Crystal structure of the pig pancreatic alpha-amylase complexed with rho-nitrophenyl-alpha-D-maltoside-flexibility in the active site (2004), Protein J., 23, 379-387.

Search for more literature for 3.2.1.1

Crystallization (Commentary)

Crystallization (Comment)	Organism
enzyme complexed with 4-nitrophenyl alpha-D-maltoside, X-ray diffraction structure determination and analysis at 2.40 A resolution	Sus scrofa

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	P00690	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose + (alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose	the reaction mechanism involves no typical conformational change of the flexible loop, residues 303-309, that constitutes the surface edge of the substrate binding cleft, but only a small movement of the segment from residues 304/305, conformational change of catalytic residue Asp300 upon substrate binding, flexibility of the active site depends on the substrate aglycon bound, overview	Sus scrofa	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
pancreas	-	Sus scrofa	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4-nitrophenyl alpha-D-maltoside + H2O	4-nitrophenol is bound at the ative site	Sus scrofa	4-nitrophenol + alpha-D-maltose	-	?

Synonyms

Synonyms	Comment	Organism
PPA	-	Sus scrofa

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Release 2023.1 (January 2023)