101. Scavenging systems for reactive carbonyls in the cyanobacterium Synechocystis sp. PCC 6803.
- Author
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Shimakawa G, Suzuki M, Yamamoto E, Nishi A, Saito R, Sakamoto K, Yamamoto H, Makino A, and Miyake C
- Subjects
- Aldehyde Reductase metabolism, Aldo-Keto Reductases, Amino Acid Sequence, Bacterial Proteins chemistry, Bacterial Proteins metabolism, Molecular Sequence Data, Aldehydes metabolism, Ketones metabolism, Synechocystis metabolism
- Abstract
To elucidate the scavenging systems of sugar- and lipid-derived reactive carbonyls (RCs) in the cyanobacterium Synechocystis sp. PCC 6803 (S. 6803), we selected proteins from S. 6803 based on amino-acid (AA) sequence similarities with proteins from Arabidopsis thaliana, and characterized the properties of the GST-fusion proteins expressed. Slr0942 catalyzed the aldo-keto reductase (AKR) reaction scavenging mainly sugar-derived RCs, methylglyoxal (MG). Slr1192 is the medium-chain dehydrogenase/redutase (MDR). It catalyzed the AKR reaction scavenging several lipid-derived RCs, acrolein, propionaldehyde, and crotonaldehyde. Slr0315 is a short-chain dehydrogenase/redutase (SDR), and it catalyzed only the reduction of MG in the AKR reaction. Slr0381 catalyzed the conversion of hemithioacetal to S-lactoylglutahione (SLG) in the glyoxalase (GLX) 1 reaction. Sll1019 catalyzed the conversion of SLG to glutathione and lactate in the GLX2 reaction. GLX1 and GLX2 compose the glyoxalase system, which scavenges MG. These enzymes contribute to scavenging sugar- and lipid-derived RCs as scavenging systems.
- Published
- 2013
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