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Primary Structure of Escherichia coli Glutamine Synthetase

Year: 1972

Type: article

Abstract: Evidence that the glutamine synthetase dodecamer from Escherichia coli is comprised of 12 identical subunits of molecular weight 49,000 has been obtained by end group analysis. Application of the carbamylation procedure to the NH2-terminal analysis revealed only serine. The yield was 98% of that expected from a polypeptide of the size proposed for the monomeric species. The following partial sequence of residues at the NH2 terminus of the molecule was elucidated with the aid of automated sequencing equipment: [see PDF for sequence] Hydrolysis of reduced and carboxymethylated glutamine synthetase by carboxypeptidase A yielded quantitative evidence for the following COOH-terminal sequence: -Leu-Tyr-Tyr-Ser-Val-COOH One mole of valine was released per mole of protein, assuming the subunit molecular weight to be 49,000.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(20)81789-x

Authors: Henry S. Kingdon, Claudia Noyes, Asit Lahiri, Robert L. Heinrikson

Institution: University of Chicago

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W2133575363

FWCI: 2.119

Cites: 28

Cited by: 11

Related to: 10