Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase (Q27651793)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18725455%20AND%20SRC:MED&resulttype=core&format=json

12 January 2020

title

Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase (English)

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12 January 2020

author

Charles Kendall Stover

6

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12 January 2020

author name string

Igor Mochalkin

1

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12 January 2020

J Richard Miller

2

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12 January 2020

Artem Evdokimov

3

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12 January 2020

Sandra Lightle

4

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12 January 2020

Chunhong Yan

5

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12 January 2020

Grover L Waldrop

7

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publication date

25 August 2008

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12 January 2020

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12 January 2020

volume

17

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12 January 2020

issue

10

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12 January 2020

page(s)

1706-1718

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Domain architecture of pyruvate carboxylase, a biotin-dependent multifunctional enzyme

12 January 2020

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20 March 2017

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20 March 2017

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Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: evidence for cooperativity in biotin carboxylase

20 March 2017

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Molecular dynamics simulations of biotin carboxylase

20 March 2017

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Direct kinetic evidence for half-of-the-sites reactivity in the E1 component of the human pyruvate dehydrogenase multienzyme complex through alternating sites cofactor activation

29 September 2017

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29 September 2017

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29 September 2017

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Single-molecule kinetics reveals signatures of half-sites reactivity in dihydroorotate dehydrogenase A catalysis

29 September 2017

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A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product.

29 September 2017

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29 September 2017

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29 September 2017

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19 June 2018

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27 November 2018

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27 November 2018

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27 November 2018

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27 November 2018

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Site-directed mutagenesis of ATP binding residues of biotin carboxylase. Insight into the mechanism of catalysis

27 November 2018

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Ribosomal tRNA binding sites: three-site models of translation.

27 November 2018

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Mutations at four active site residues of biotin carboxylase abolish substrate-induced synergism by biotin

27 November 2018

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12 December 2020

The biotin domain peptide from the biotin carboxyl carrier protein of Escherichia coli acetyl-CoA carboxylase causes a marked increase in the catalytic efficiency of biotin carboxylase and carboxyltransferase relative to free biotin

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12 December 2020

Do cysteine 230 and lysine 238 of biotin carboxylase play a role in the activation of biotin?

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12 December 2020

Processing of X-ray diffraction data collected in oscillation mode

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12 December 2020

Identifiers

DOI

10.1110/PS.035584.108

2 references

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12 January 2020

1 reference

2 references

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12 January 2020

2 references