2020
DOI: 10.1016/j.plaphy.2020.04.019
|View full text |Cite
|
Sign up to set email alerts
|

The N-terminal domain of Arabidopsis proline dehydrogenase affects enzymatic activity and protein oligomerization

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2

Citation Types

1
1
0

Year Published

2020
2020
2024
2024

Publication Types

Select...
7

Relationship

0
7

Authors

Journals

citations
Cited by 9 publications
(2 citation statements)
references
References 30 publications
1
1
0
Order By: Relevance
“…Purification of the GST:ProDH fusion proteins strongly increased the specific activity of prolinedependent DCPIP reduction, whereas the proline-dependent reduction of NAD + at pH 10 was depleted (Figure 3 and Supplementary Figure S1). The specific activities of the purified GST:ProDH1 N12 and GST:ProDH2 N13 were similar to the activities reported recently for ProDH1 N39 and ProDH2 N29 expressed as fusion proteins with the maltose binding protein (Fabro et al, 2020).…”
Section: Discussionsupporting
confidence: 86%
“…Purification of the GST:ProDH fusion proteins strongly increased the specific activity of prolinedependent DCPIP reduction, whereas the proline-dependent reduction of NAD + at pH 10 was depleted (Figure 3 and Supplementary Figure S1). The specific activities of the purified GST:ProDH1 N12 and GST:ProDH2 N13 were similar to the activities reported recently for ProDH1 N39 and ProDH2 N29 expressed as fusion proteins with the maltose binding protein (Fabro et al, 2020).…”
Section: Discussionsupporting
confidence: 86%
“…The synthesis of proline in plants is catalyzed by P5CS and P5CR. For example, P5CS plays a critical role in the synthesis of proline when plants suffer stress [38]. As the key enzyme in proline synthesis, the activity of P5CS was reinforced by NFT storage in peach fruits while the activity of P5CR was weakened, indicating that NFT accelerated proline synthesis.…”
Section: Discussionmentioning
confidence: 99%