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 and a glutamine residue, conserved in both clavaminic acid synthase isozymes 1 and 2, demonstrated that none of these residues is essential for activity.
Doan
L X
LX
The Oxford Centre for Molecular Sciences, Oxford University, South Parks Road, Oxford, OX1 3QY, United Kingdom.
Hassan
A
A
Lipscomb
S J
SJ
Dhanda
A
A
Zhang
Z
Z
Schofield
C J
CJ
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
D017931:DNA Primers; D008024:Ligands; D006639:Histidine; D007501:Iron; D006899:Mixed Function Oxygenases; C066046:clavaminate synthase; D007930:Leucine