Work

N-Formimino-l-glutamate Iminohydrolase from Histidine-adapted Pseudomonas

Year: 1972

Type: article

Abstract: N-Formimino-l-glutamate iminohydrolase has been purified 700-fold to homogeneity from extracts of histidineadapted Pseudomonas sp. The products of the reaction are equimolar amounts of ammonia and N-formyl-l-glutamate. The enzyme has a molecular weight of 100,000 and 2 subunits of equal molecular weight.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(19)45599-3

Authors: Reed B. Wickner, Herbert Tabor

Institutions: National Institutes of Health, National Institute of Arthritis and Musculoskeletal and Skin Diseases

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: W1594224927

FWCI: 0.906

Cites: 32

Cited by: 14

Related to: 10