Mutagenesis studies on the iron binding ligands of clavaminic acid synthase.

Mutagenesis studies on the iron binding ligands of clavaminic acid synthase.

Mutagenesis studies on conserved histidine residues identified as possible metal binding ligands in clavaminic acid synthase isozyme 2 were consistent with His-145 and His-280 acting as iron ligands, in support of crystallographic and previous mutagenesis studies. Mutagenesis of the four cysteines a...

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Главные авторы: Doan, L, Hassan, A, Lipscomb, S, Dhanda, A, Zhang, Z, Schofield, C
Формат: Journal article
Язык:English
Опубликовано: 2000
Описание
Итог:Mutagenesis studies on conserved histidine residues identified as possible metal binding ligands in clavaminic acid synthase isozyme 2 were consistent with His-145 and His-280 acting as iron ligands, in support of crystallographic and previous mutagenesis studies. Mutagenesis of the four cysteines and a glutamine residue, conserved in both clavaminic acid synthase isozymes 1 and 2, demonstrated that none of these residues is essential for activity.

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