Literature DB >> 2870062

Sequence of a peptide susceptible to mixed-function oxidation. Probable cation binding site in glutamine synthetase.

J M Farber, R L Levine.   

Abstract

Mixed-function oxidation of glutamine synthetase from Escherichia coli causes loss of catalytic activity. The inactivation correlates with the loss of 1 of 16 histidine residues/subunit (Levine, R.L. (1983) J. Biol. Chem. 258, 11823-11827). A cyanogen bromide peptide containing the oxidizable histidine has been isolated. Within the protein, the sequence is Met-His-Cys-His-Met. This hydrophilic sequence likely forms one of the divalent metal-binding sites of glutamine synthetase. Binding of Fe2+ to this site permits generation of an activated oxygen species which reacts with a nearby histidine residue. This site-specific free radical mechanism accounts for the specificity of the mixed-function oxidation.

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Year:  1986        PMID： 2870062

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


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