Abstract:
: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 δ1-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.
journal_name
Amino Acidsjournal_title
Amino acidsauthors
Petrollino D,Forlani Gdoi
10.1007/s00726-011-1077-xsubject
Has Abstractpub_date
2012-07-01 00:00:00pages
493-7issue
1eissn
0939-4451issn
1438-2199journal_volume
43pub_type
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