|
type |
Journal Article |
authors |
Hasse D.; Mikkat S.; Thrun H.A.; Hagemann, M.; Bauwe, H. |
title |
Properties of recombinant glycine decarboxylase P- and H-protein subunits from the cyanobacterium Synechocystis sp. strain PCC 6803.
|
journal |
FEBS Lett |
Activity |
1.4.4.2 |
Family |
1.4.4.2 |
sel |
selected |
ui |
17349627 |
year |
(2007) |
volume |
581 |
number |
7 |
pages |
1297-301 |
| |
keywords |
Amino Acid Oxidoreductases/*metabolism |
abstract |
The multi-enzyme complex glycine decarboxylase is important for one-carbon metabolism, essential for the photorespiratory glycolate cycle of plants, and comprises four different polypeptides, P-, H-, T-, and L-protein. We report on the production and properties of recombinant P-protein from the cyanobacterium Synechocystis and also describe features of recombinant H-protein from the same organism. The P-protein shows enzymatic activity with lipoylated H-protein and very low activity with H-apoprotein or lipoate as artificial cofactors. Its affinity towards glycine is unaffected by the presence and nature of the methyleneamine acceptor molecule. The cyanobacterial H-protein apparently forms stable dimers. |
last changed |
2007/09/28 17:24 |
|