Coenzyme preference of Streptococcus pyogenes δ1-pyrroline-5-carboxylate reductase: evidence supporting NADPH as the physiological electron donor.

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 Acids

journal_title

Amino acids

authors

Petrollino D,Forlani G

doi

10.1007/s00726-011-1077-x

subject

Has Abstract

pub_date

2012-07-01 00:00:00

pages

493-7

issue

1

eissn

0939-4451

issn

1438-2199

journal_volume

43

pub_type

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