(Q27641798)

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The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs

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The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs (English)

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Xavier Robert

1

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Nushin Aghajari

object named as

Nushin Aghajari

7

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author name string

Richard Haser

2

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Tine E Gottschalk

3

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Fabien Ratajczak

4

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Hugues Driguez

5

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Birte Svensson

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publication date

August 2003

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11

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973-84

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8

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Arginine is essential for the alpha-amylase inhibitory activity of the alpha-amylase/subtilisin inhibitor (BASI) from barley seeds

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Crystal structures of the psychrophilic alpha-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor

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Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level

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Barley malt-alpha-amylase. Purification, action pattern, and subsite mapping of isozyme 1 and two members of the isozyme 2 subfamily using p-nitrophenylated maltooligosaccharide substrates

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The Protein Data Bank

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Spacer-modified disaccharide and pseudo-trisaccharide methyl glycosides that mimic maltotriose, as competitive inhibitors for pancreatic alpha-amylase: a demonstration of the "clustering effect"

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Errors in protein structures

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Isozyme hybrids within the protruding third loop domain of the barley alpha-amylase (beta/alpha)8-barrel. Implication for BASI sensitivity and substrate affinity

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Crystal and molecular structure of barley alpha-amylase

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Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis

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Refined molecular structure of pig pancreatic alpha-amylase at 2.1 A resolution

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The bifunctional α-amylase/subtilisin inhibitor of barley: nucleotide sequence and patterns of seed-specific expression.

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Models for the action of barley alpha-amylase isozymes on linear substrates.

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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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Improved activity and modulated action pattern obtained by random mutagenesis at the fourth beta-alpha loop involved in substrate binding to the catalytic (beta/alpha)8-barrel domain of barley alpha-amylase 1.

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Crystallization and structural analysis of intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri

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Modulation of activity and substrate binding modes by mutation of single and double subsites +1/+2 and -5/-6 of barley alpha-amylase 1.

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Barley alpha-amylase Met53 situated at the high-affinity subsite -2 belongs to a substrate binding motif in the beta-->alpha loop 2 of the catalytic (beta/alpha)8-barrel and is critical for activity and substrate specificity

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Expression, purification and preliminary crystallographic studies of alpha-amylase isozyme 1 from barley seeds

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Domain B protruding at the third beta strand of the alpha/beta barrel in barley alpha-amylase confers distinct isozyme-specific properties.

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Specific inhibition of barley alpha-amylase 2 by barley alpha-amylase/subtilisin inhibitor depends on charge interactions and can be conferred to isozyme 1 by mutation

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Expression of cDNAs encoding barley alpha-amylase 1 and 2 in yeast and characterization of the secreted proteins

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