Work

Imidazolylacetolphosphate: l-Glutamate Aminotransferase

Year: 1967

Type: article

Abstract: Physical and chemical studies on purified imidazolylacetolphosphate: L-glutamate aminotransferase from Salmonella fyphimurium provide evidence suggesting that the enzyme is composed of two nonidentical subunits.This observation was unexpected since the C gene of the histidine operon in S. fyphimurium, which contains the genetic information for the synthesis of this enzyme, appears to be composed of a single complementation unit.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(18)96160-0

Authors: Robert G. Martin, Mary Jane Voll, Ettore Appella

Institution: National Institutes of Health

Language: English

Topic: Amino Acid Enzymes and Metabolism

Subfield: Biochemistry

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1539866043

FWCI: 4.228

Cites: 25

Cited by: 46

Related to: 10