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Issue 15, 1998
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Non-covalent control of site-selective incorporation of the pyridoxal phosphate cofactor into a folded polypeptide motif—mimicking a key step in enzymatic transamination

Abstract

The site-selective incorporation of the pyridoxal phosphate cofactor into a designed polypeptide motif has been achieved and shown to be controlled by the non-covalent interactions between the phosphate group of the cofactor and a single arginine residue on the surface of the folded polypeptide.

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Article type: Paper
DOI: 10.1039/A801741G
Chem. Commun., 1998, 1547-1548

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    Non-covalent control of site-selective incorporation of the pyridoxal phosphate cofactor into a folded polypeptide motif—mimicking a key step in enzymatic transamination

    M. Allert and K. Broo, Chem. Commun., 1998, 1547
    DOI: 10.1039/A801741G

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