Article
Spectroscopic Studies of the EutT Adenosyltransferase from Salmonella enterica: Evidence of a Tetrahedrally Coordinated Divalent Transition Metal Cofactor with Cysteine Ligation.
Biochemistry - 17 Jan 2017
Pallares Ivan G, Moore Theodore C, Escalante-Semerena Jorge C, Brunold Thomas C
Abstract excerpt
The EutT enzyme from Salmonella enterica, a member of the family of ATP:cobalt(I) corrinoid adenosyltransferase (ACAT) enzymes, requires a divalent transition metal ion for catalysis, with Fe(II) yielding the highest activity. EutT contains a unique cysteine-rich HX11CCX2C(83) motif (where H and the last C occupy the 67th and 83rd positions, respectively, in the amino acid sequence) not found in other ACATs and...
Topics
- Adenosine Triphosphate
- Alanine
- Alkyl and Aryl Transferases
- Amino Acid Motifs
- Bacterial Proteins
- Cations, Divalent
- Circular Dichroism
- Cloning, Molecular
- Cobalt
- Cobamides
- Coenzymes
- Coordination Complexes
- Cysteine