Identification of lysine-238 of Escherichia coli biotin carboxylase as an ATP-binding residue (Q47937887)

6 February 2018

title

Identification of lysine-238 of Escherichia coli biotin carboxylase as an ATP-binding residue (English)

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6 February 2018

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Y Kazuta

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6 February 2018

E Tokunaga

series ordinal

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6 February 2018

E Aramaki

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6 February 2018

H Kondo

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6 February 2018

language of work or name

English

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publication date

1 May 1998

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6 February 2018

published in

FEBS Letters

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6 February 2018

volume

427

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issue

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6 February 2018

page(s)

377-380

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6 February 2018

Acetyl CoA carboxylase, II. Deomonstration of biotin-protein and biotin carboxylase subunits

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Acetyl-CoA carboxylase from Escherichia coli: gene organization and nucleotide sequence of the biotin carboxylase subunit

21 January 2018

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Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase

21 January 2018

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Modification of lactate dehydrogenase by pyridoxal phosphate and adenosine polyphosphopyridoxal

21 January 2018

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

21 January 2018

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Molecular evolution of biotin-dependent carboxylases

21 January 2018

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Phosphate-binding sequences in nucleotide-binding proteins

21 January 2018

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Structure of carbamoyl phosphate synthetase: a journey of 96 A from substrate to product

21 January 2018

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Structure of the multifunctional loops in the nonclassical ATP-binding fold of glutathione synthetase.

21 January 2018

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Catalytic mechanism of biotin carboxylase: steady-state kinetic investigations

21 January 2018

1 reference

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THE PURIFICATION AND PROPERTIES OF NEUROSPORA MALATE DEHYDROGENASE

21 January 2018

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Biotin carboxylase comes into the fold

21 January 2018

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21 January 2018

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/S0014-5793(98)00472-4

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6 February 2018

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6 February 2018