1HX0

Structure of pig pancreatic alpha-amylase complexed with the "truncate" acarbose molecule (pseudotrisaccharide)

Summary for 1HX0

• Entry DOI: 10.2210/pdb1hx0/pdb
• Related PRD ID: PRD_900001
• Descriptor: ALPHA AMYLASE (PPA), 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: alpha-amylase, inhibitor, carbohydrate, pancreas, hydrolase
• Biological source: Sus scrofa (pig)
• Total number of polymer chains: 1
• Total formula weight: 57690.74

Authors

Qian, M.,Payan, F. (deposition date: 2001-01-11, release date: 2001-08-08, Last modification date: 2024-11-13)

Primary citation

Qian, M.,Nahoum, V.,Bonicel, J.,Bischoff, H.,Henrissat, B.,Payan, F.
Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex
Biochemistry, 40:7700-7709, 2001

PubMed Abstract: Mammalian alpha-amylases catalyze the hydrolysis of alpha-linked glucose polymers according to a complex processive mechanism. We have determined the X-ray structures of porcine pancreatic alpha-amylase complexes with the smallest molecule of the trestatin family (acarviosine-glucose) which inhibits porcine pancreatic alpha-amylase and yet is not hydrolyzed by the enzyme. A structure analysis at 1.38 A resolution of this complex allowed for a clear identification of a genuine single hexasaccharide species composed of two alpha-1,4-linked original molecules bound to the active site of the enzyme. The structural results supported by mass spectrometry experiments provide evidence for an enzymatically catalyzed condensation reaction in the crystal.

PubMed: 11412124
DOI: 10.1021/bi0102050

Experimental method

X-RAY DIFFRACTION (1.38 Å)