Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase (Q27730931)

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English	Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase	scientific article

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instance of

scholarly article

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title

Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase (English)

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author

Udo Heinemann

object named as

U Heinemann

series ordinal

4

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author name string

T Keitel

series ordinal

1

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O Simon

series ordinal

2

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R Borriss

series ordinal

3

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language of work or name

English

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publication date

1 June 1993

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published in

Proceedings of the National Academy of Sciences of the United States of America

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volume

90

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issue

11

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page(s)

5287-91

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cites work

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Primary structure of the (1-->3,1-->4)-beta-D-glucan 4-glucohydrolase from barley aleurone

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Crystallographic determination of the mode of binding of oligosaccharides to T4 bacteriophage lysozyme: Implications for the mechanism of catalysis

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Differences in active site structure in a family of beta-glucan endohydrolases deduced from the kinetics of inactivation by epoxyalkyl beta-oligoglucosides.

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DNA sequence of a Fibrobacter succinogenes mixed-linkage beta-glucanase (1,3-1,4-beta-D-glucan 4-glucanohydrolase) gene

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Two beta-glycanase genes are clustered in Bacillus polymyxa: molecular cloning, expression, and sequence analysis of genes encoding a xylanase and an endo-beta-(1,3)-(1,4)-glucanase

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Active site-directed inhibition by optically pure epoxyalkyl cellobiosides reveals differences in active site geometry of two 1,3-1,4-beta-D-glucan 4-glucanohydrolases. The importance of epoxide stereochemistry for enzyme inactivation

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A new substrate for investigating the specificity of beta-glucan hydrolases

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The beta-glucanase gene from Bacillus amyloliquefaciens shows extensive homology with that of Bacillus subtilis

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Structure of the beta-1,3-1,4-glucanase gene of Bacillus macerans: homologies to other beta-glucanases

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Molecular cloning, expression and nucleotide sequence of the endo-beta-1,3-1,4-D-glucanase gene from Bacillus licheniformis. Predictive structural analyses of the encoded polypeptide

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Crystallization of the hybrid Bacillus (1-3,1-4)-beta-glucanase H(A16-M).

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2 June 2018

Structure of the Clostridium thermocellum gene licB and the encoded beta-1,3-1,4-glucanase. A catalytic region homologous to Bacillus lichenases joined to the reiterated domain of clostridial cellulases

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Essential catalytic role of Glu134 in endo-beta-1,3-1,4-D-glucan 4-glucanohydrolase from B. licheniformis as determined by site-directed mutagenesis.

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Hybrid bacillus endo-(1-3,1-4)-beta-glucanases: construction of recombinant genes and molecular properties of the gene products.

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Carboxyl-carboxylate interactions in proteins

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based on heuristic

inferred from PubMed ID database lookup

Hybrid Bacillus (1-3,1-4)-beta-glucanases: engineering thermostable enzymes by construction of hybrid genes

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reference URL

https://pubmed.ncbi.nlm.nih.gov/8099449

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Stereochemically restrained refinement of macromolecular structures

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/8099449

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identification of glutamic acid 105 at the active site of Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan 4-glucanohydrolase using epoxide-based inhibitors

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/8099449

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1073/PNAS.90.11.5287

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ADS bibcode

1993PNAS...90.5287K

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PMC publication ID

46701

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PubMed publication ID

8099449

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ResearchGate publication ID

15100701

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