High resolution reaction intermediates of rabbit muscle fructose-1,6-bisphosphate aldolase: substrate cleavage and induced fit. (Q46471193)

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11 January 2020

title

High resolution reaction intermediates of rabbit muscle fructose-1,6-bisphosphate aldolase: substrate cleavage and induced fit (English)

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11 January 2020

author

Julien Lafrance-Vanasse

2

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11 January 2020

author name string

Miguel St-Jean

1

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11 January 2020

Brigitte Liotard

3

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11 January 2020

Jurgen Sygusch

4

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11 January 2020

language of work or name

English

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publication date

3 May 2005

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Journal of Biological Chemistry

11 January 2020

published in

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11 January 2020

volume

280

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11 January 2020

issue

29

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11 January 2020

page(s)

27262-27270

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Complexes of muscle aldolase in equilibrium with fructose 1,6-bisphosphate.

11 January 2020

cites work

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Chemical trapping of complexes of dihydroxyacetone phosphate with muscle fructose-1,6-bisphosphate aldolase

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Molecular architecture of rabbit skeletal muscle aldolase at 2.7-A resolution

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A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases

21 January 2018

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Inhibition of rabbit muscle aldolase by phosphorylated aromatic compounds

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A lysine to arginine substitution at position 146 of rabbit aldolase A changes the rate-determining step to Schiff base formation.

21 January 2018

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Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its natural substrate in a cleavage-defective mutant at 2.3 A(,)

21 January 2018

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Snapshots of catalysis: the structure of fructose-1,6-(bis)phosphate aldolase covalently bound to the substrate dihydroxyacetone phosphate

21 January 2018

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Covalent intermediate trapped in 2-keto-3-deoxy-6- phosphogluconate (KDPG) aldolase structure at 1.95-A resolution

21 January 2018

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Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase

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Crystal structure of an archaeal class I aldolase and the evolution of (betaalpha)8 barrel proteins

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The pyridoxal phosphate-binding site of rabbit muscle aldolase

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The Stereochemistry of the Ivanov and Reformatsky Reactions. I

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Acyclic stereoselection. 7. Stereoselective synthesis of 2-alkyl-3-hydroxy carbonyl compounds by aldol condensation

21 January 2018

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Fructose 1,6-bisphosphate aldolase from liver: the absolute configuration of the intermediate carbinolamine

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Fructose 1,6-bisphosphate: isomeric composition, kinetics, and substrate specificity for the aldolases

21 January 2018

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21 January 2018

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

21 January 2018

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Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M502413200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15870069%20AND%20SRC:MED&resulttype=core&format=json

11 January 2020

1 reference