Journal
AMINO ACIDS
Volume 43, Issue 1, Pages 493-497Publisher
SPRINGER WIEN
DOI: 10.1007/s00726-011-1077-x
Keywords
Electron donor; Proline biosynthesis; Substrate ambiguity; Substrate binding
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Funding
- University of Ferrara
- Spinner Consortium, Emilia Romagna Region
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The streptococcal enzyme that catalyzes the last step in proline biosynthesis was heterologously expressed and the recombinant protein was purified to electrophoretic homogeneity and characterized thoroughly. As for delta(1)-pyrroline-5-carboxylate reductases from other sources, it was able to use either NADH or NADPH as the electron donor in vitro. However, with NADH the activity was markedly inhibited by physiological levels of NADP(+). Results also strengthen the possibility that an unusual ordered substrate binding occurs, in which the dinucleotide binds last.
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