Work

Probing the potential metal binding site in Escherichia coli 3‐deoxy‐ d ‐arabino‐heptulosonate 7‐phosphate synthase (phenylalanine‐sensitive)

Year: 1998

Type: article

Abstract: The active site residues of the proposed metal binding site of DAH 7-P synthase (phe) were probed by site-directed mutagenesis of C61 to glycine and serine, H64 to glycine, and with the double mutant C61H/H64C. While C61S and C61H/ H64C were inactive, both C61G and H64G were active. All mutants, regardless of enzymatic activity, bound one equivalent of Fe2+ per monomeric unit. Even though C61 and H64 were shown not to be metal ligands for the DAH 7-P synthase (phe), they may provide some of the backbone interactions/secondary structural elements necessary to properly form the metal binding pocket.

Source: FEBS Letters

DOI: 10.1016/s0014-5793(98)01545-2

Authors: Appavu K Sundaram, David L Howe, Galina Ya Sheflyan, Ronald W Woodard

Institution: University of Michigan

Language: English

Topic: Enzyme Structure and Function

Subfield: Structural Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: U.S. Department of Health and Human Services, National Institute of General Medical Sciences

Award: Mechanism of KDO 8-P and DAH 7-P Synthase