Multifunctional Proteins

Cohen, Georges N.

doi:10.1002/047120918x.emb0962

Cited by 2 publications

(1 citation statement)

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“…In many of these organisms at least one of these enzymes is bifunctional, catalyzing both the ®rst reaction, the phosphorylation of aspartate and, surprisingly, the third reaction, the reduction of aspartate semialdehyde to homoserine, in this metabolic sequence. In E. coli there are three aspartokinases, two of which are bifunctional enzymes; the other, aspartokinase III (AK III), is a monofunctional enzyme inhibited by high lysine levels (Cohen & Dautry-Varsat, 1980). The sequence of the AK III catalytic domain has 44% homology to the bifunctional aspartokinase domains.…”

Section: Introductionmentioning

confidence: 99%

Purification, crystallization and preliminary X-ray analysis of aspartokinase III fromEscherichia coli

Blanco¹,

Viola²

2002

Acta Crystallogr D Biol Cryst

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Aspartokinase III catalyzes the commitment step in the aspartate metabolism pathway, the phosphorylation of aspartic acid. The Escherichia coli enzyme has been crystallized in the presence of its natural substrate (aspartic acid) and Mg-ADP and diffraction data has been collected at a synchroton source. The crystals belong to the orthorhombic space group C222 1 , with unit-cell parameters a = 60.44, b = 190.31, c = 99.55 A Ê , and data 99.3% complete to 2.7 A Ê . Solving the structure of AK III will provide the ®rst structure of an aspartokinase from any organism.

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Section: Introductionmentioning

confidence: 99%