(Q44206241)

English

Transaldolase B: trapping of Schiff base intermediate between dihydroxyacetone and epsilon-amino group of active-site lysine residue by borohydride reduction

scientific article published in January 2002

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

Transaldolase B: trapping of Schiff base intermediate between dihydroxyacetone and epsilon-amino group of active-site lysine residue by borohydride reduction (English)

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

Gunter Schneider

1

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

author name string

Georg A Sprenger

2

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

language of work or name

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publication date

1 January 2002

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Europe PubMed Central

PubMed publication ID

30 November 2017

Methods in Enzymology

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Europe PubMed Central

PubMed publication ID

30 November 2017

354

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

197-201

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

Class I aldolases: substrate specificity, mechanism, inhibitors and structural aspects

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2954016-7

7 January 2021

based on heuristic

inferred from DOI database lookup

Isolation and sequence analysis of a peptide from the active site of transaldolase

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2954016-7

7 January 2021

based on heuristic

inferred from DOI database lookup

Studies on the structure of rabbit muscle aldolase. 3. Primary structure of the BrCN peptide containing the active site

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2954016-7

7 January 2021

based on heuristic

inferred from DOI database lookup

Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2954016-7

7 January 2021

based on heuristic

inferred from DOI database lookup

Disruption of Escherichia coli transaldolase into catalytically active monomers: evidence against half-of-the-sites mechanism.

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2954016-7

7 January 2021

based on heuristic

inferred from DOI database lookup

Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the alpha/beta barrel within the class I aldolase family

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2954016-7

7 January 2021

based on heuristic

inferred from DOI database lookup

The three-dimensional structure of human transaldolase

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2954016-7

7 January 2021

based on heuristic

inferred from DOI database lookup

Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: mechanistic implications for class I aldolases

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2954016-7

7 January 2021

based on heuristic

inferred from DOI database lookup

Lysine144 is essential for the catalytic activity of Saccharomyces cerevisiae transaldolase

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2954016-7

7 January 2021

based on heuristic

inferred from DOI database lookup

Inhibition of the catalytic activity of human transaldolase by antibodies and site-directed mutagenesis

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2954016-7

7 January 2021

based on heuristic

inferred from DOI database lookup

Identification of catalytically important residues in the active site of Escherichia coli transaldolase

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2954016-7

7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

10.1016/S0076-6879(02)54016-7

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

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