Stereospecific mechanism of DJ-1 glyoxalases inferred from their hemithioacetal-containing crystal structures

Author:

Choi Dongwook12,Kim Jihong2,Ha Sura3,Kwon Kyu2,Kim Eun-Hee1,Lee Hee-Yoon3,Ryu Kyoung-Seok14,Park Chankyu2

Affiliation:

1. Division of Magnetic Resonance Research; Korea Basic Science Institute; Chungcheongbuk - Do South Korea

2. Department of Biological Science; Korea Advanced Institute of Science and Technology; Daejeon South Korea

3. Department of Chemistry; Korea Advanced Institute of Science and Technology; Daejeon South Korea

4. Department of Bio-Analytical Science; University of Science and Technology; Daejeon South Korea

Funder

high-field NMR research program of the Korea Basic Science Institute

Basic Science Research Program of the National Research Foundation of Korea

Korea Research Institute of Bioscience and Biotechnology Research Initiative Program

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference56 articles.

1. The formation of methylglyoxal from triose phosphates. Investigation using a specific assay for methylglyoxal;Phillips;Eur J Biochem,1993

2. Mechanism of autoxidative glycosylation: identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose;Wells-Knecht;Biochemistry,1995

3. Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction;Glomb;J Biol Chem,1995

4. alpha-Hydroxyaldehydes, products of lipid peroxidation;Loidl-Stahlhofen;Biochim Biophys Acta,1994

5. Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N alpha-acetylarginine, N alpha-acetylcysteine, and N alpha-acetyllysine, and bovine serum albumin;Lo;J Biol Chem,1994

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