Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21 (Q27671995)

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English	Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21	scientific article

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instance of

scholarly article

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title

Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21 (English)

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main subject

biophysics

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structural biology

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condensed matter physics

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barley

1 reference

based on heuristic

inferred from title

author

Marie S Møller

object named as

Marie Sofie Møller

series ordinal

1

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Anette Henriksen

object named as

Anette Henriksen

series ordinal

4

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Maher Abou Hachem

object named as

Maher Abou Hachem

series ordinal

2

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Birte Svensson

object named as

Birte Svensson

series ordinal

3

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publication date

1 September 2012

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published in

Acta Crystallographica Section F: Structural Biology Communications

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volume

68

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issue

Pt 9

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page(s)

1008-12

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cites work

Crystal structure of an essential enzyme in seed starch degradation: barley limit dextrinase in complex with cyclodextrins

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Crystal structures of the starch-binding domain from Rhizopus oryzae glucoamylase reveal a polysaccharide-binding path

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Overview of the CCP4 suite and current developments

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Isolation and characterization of the gene encoding the starch debranching enzyme limit dextrinase from germinating barley

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A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of barley

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21 January 2018

Comparison of the domain-level organization of starch hydrolases and related enzymes

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MOLREP: an Automated Program for Molecular Replacement

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Secretory expression of functional barley limit dextrinase by Pichia pastoris using high cell-density fermentation

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Identifiers

DOI

10.1107/S1744309112031004

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PMC publication ID

3433187

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PubMed publication ID

22949184

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