A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5 A resolution (Q27764893)

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English	A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5 A resolution	scientific article

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scholarly article

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A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5 A resolution (English)

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author name string

S Strobl

1

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K Maskos

2

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G Wiegand

3

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R Huber

4

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F X Gomis-Rüth

5

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R Glockshuber

6

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publication date

15 July 1998

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6

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7

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911-21

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The alpha-amylase from the yellow meal worm: complete primary structure, crystallization and preliminary X-ray analysis.

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Crystal structure of yellow meal worm alpha-amylase at 1.64 A resolution

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α-amylase inhibitors from wheat isolation and characterization

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Inhibition of amylases from different origins by albumins from the wheat kernel

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Rye inhibitors of animal alpha-amylases show different specificities, aggregative properties and IgE-binding capacities than their homologues from wheat and barley

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Carbohydrate binding sites in a pancreatic alpha-amylase-substrate complex, derived from X-ray structure analysis at 2.1 A resolution

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Molecular Modelling of the Interaction Between the Catalytic Site of Pig Pancreatic alpha-Amylase and Amylose Fragments

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The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution

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Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: structure analysis and comparison of their binding characteristics

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The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat

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Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex

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RBI, a one-domain alpha-amylase/trypsin inhibitor with completely independent binding sites

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Determination of the three-dimensional structure of the bifunctional alpha-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy

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Natural protein proteinase inhibitors and their interaction with proteinases

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Conformation of Polypeptides and Proteins

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The catalytic mechanism of alpha-amylases based upon enzyme crystal structures and model building calculations.

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Site-directed mutagenesis reveals critical importance of the catalytic site in the binding of alpha-amylase by wheat proteinaceous inhibitor

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Site-directed mutagenesis and expression in Escherichia coli of WMAI-1, a wheat monomeric inhibitor of insect alpha-amylase

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Natural plant enzyme inhibitors. Characterization of an unusual alpha-amylase/trypsin inhibitor from ragi (Eleusine coracana Geartn.).

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Stability and kinetics of a bifunctional amylase/trypsin inhibitor

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Tertiary and Quaternary Structures of 0.19 α-Amylase Inhibitor from Wheat Kernel Determined by X-ray Analysis at 2.06 Å Resolution,

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Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 A resolution

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Bean [alpha]-Amylase Inhibitor Confers Resistance to the Pea Weevil (Bruchus pisorum) in Transgenic Peas (Pisum sativum L.).

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The CCP4 suite: programs for protein crystallography

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AMoRe: an automated package for molecular replacement

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SETOR: hardware-lighted three-dimensional solid model representations of macromolecules

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MOLMOL: a program for display and analysis of macromolecular structures

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Cloning of cDNA, expression, and chromosomal location of genes encoding the three types of subunits of the barley tetrameric inhibitor of insect alpha-amylase

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Complete amino acid sequence of an α-amylase inhibitor in wheat kernel

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Molecular cloning of the barley seed protein CMd: a variant member of the alpha-amylase/trypsin inhibitor family of cereals

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Cloning of cDNA and chromosomal location of genes encoding the three types of subunits of the wheat tetrameric inhibitor of insect alpha-amylase

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10.1016/S0969-2126(98)00092-6

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