Work

Ornithine racemase uses a catalytic cysteine

Year: 2025

Type: article

Abstract: O, consistent with the function of Cys-164 as an acid/base catalyst. These data are consistent with a concerted mechanism for the racemization. Gel filtration of OrnR shows a mixture of dimeric and tetrameric assemblies.

Source: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

DOI: 10.1016/j.bbapap.2025.141120

Authors: Robert S. Phillips, Xuan Tran, Brooke Mangano

Institution: University of Georgia

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: $3,900

Funders: National Institutes of Health, National Institute of General Medical Sciences

Awards: G5740881941, Structural and proton dynamics of pyridoxal-5'-phosphate dependent enzymes (resubmission), G9000229905

OpenAlex ID: W4417535613

FWCI: 0.26

Cites: 34

Cited by: 1

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