title: Mutagenesis studies on the iron binding ligands of clavaminic acid synthase.
abstract: 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.
authors: The Oxford Centre for Molecular Sciences, Oxford University, South Parks Road, Oxford, OX1 3QY, United Kingdom.
authors: L X
authors: LX
authors: Doan
authors: A
authors: A
authors: Hassan
authors: S J
authors: SJ
authors: Lipscomb
authors: A
authors: A
authors: Dhanda
authors: Z
authors: Z
authors: Zhang
authors: C J
authors: CJ
authors: Schofield
mesh_terms: D019943:Amino Acid Substitution; D001483:Base Sequence; D017931:DNA Primers; D006639:Histidine / Q000737:chemistry / Q000378:metabolism; D007501:Iron / Q000378:metabolism*; D007930:Leucine / Q000737:chemistry / Q000378:metabolism; D008024:Ligands; D006899:Mixed Function Oxygenases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed
chemical_list: D017931:DNA Primers; D008024:Ligands; D006639:Histidine; D007501:Iron; D006899:Mixed Function Oxygenases; C066046:clavaminate synthase; D007930:Leucine