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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מידע ביבליוגרפי
Main Authors: Doan, L, Hassan, A, Lipscomb, S, Dhanda, A, Zhang, Z, Schofield, C
פורמט: Journal article
שפה:English
יצא לאור: 2000
תיאור
סיכום: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.