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B6db references: 17349627

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
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

B6db references