Premium
Properties of recombinant glycine decarboxylase P‐ and H‐protein subunits from the cyanobacterium Synechocystis sp. strain PCC 6803
Author(s) -
Hasse Dirk,
Mikkat Stefan,
Thrun Hans-Albrecht,
Hagemann Martin,
Bauwe Hermann
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.02.037
Subject(s) - synechocystis , recombinant dna , biochemistry , glycine , enzyme , cofactor , cyanobacteria , chemistry , strain (injury) , biology , amino acid , bacteria , gene , genetics , anatomy , mutant
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.