Structure and catalytic properties of an engineered heterodimer of enolase composed of one active and one inactive subunit (Q35088261)

6 August 2017

title

Structure and catalytic properties of an engineered heterodimer of enolase composed of one active and one inactive subunit (English)

1 reference

6 August 2017

Paul A Sims

1

1 reference

6 August 2017

Ann L Menefee

2

1 reference

6 August 2017

Todd M Larsen

3

1 reference

6 August 2017

Steven O Mansoorabadi

4

1 reference

6 August 2017

George H Reed

5

1 reference

6 August 2017

language of work or name

English

0 references

publication date

8 November 2005

1 reference

Journal of Molecular Biology

6 August 2017

published in

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6 August 2017

volume

355

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6 August 2017

issue

3

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6 August 2017

page(s)

422-431

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SHELXL: high-resolution refinement

6 August 2017

cites work

1 reference

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8 July 2018

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8 July 2018

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8 July 2018

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8 July 2018

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8 July 2018

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Toward identification of acid/base catalysts in the active site of enolase: comparison of the properties of K345A, E168Q, and E211Q variants

8 July 2018

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A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 A resolution

8 July 2018

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Chelation of serine 39 to Mg2+ latches a gate at the active site of enolase: structure of the bis(Mg2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1-A resolution

8 July 2018

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27 September 2018

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The primary structures of two yeast enolase genes. Homology between the 5' noncoding flanking regions of yeast enolase and glyceraldehyde-3-phosphate dehydrogenase genes

27 September 2018

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Nuclear magnetic resonance assignment of the vinyl hydrogens of phosphoenolpyruvate. Stereochemistry of the enolase reaction

27 September 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/16309698

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

The amino acid sequence of yeast enolase. Preparation and characterization of peptides produced by chemical and enzymatic fragmentation.

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/16309698

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Internal thermodynamics of enzymes determined by equilibrium quench: values of Kint for enolase and creatine kinase

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/16309698

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1016/J.JMB.2005.10.050

1 reference

6 August 2017

1 reference

6 August 2017

1 reference