1B93

METHYLGLYOXAL SYNTHASE FROM ESCHERICHIA COLI

Summary for 1B93

Entry DOI	10.2210/pdb1b93/pdb
Descriptor	PROTEIN (METHYLGLYOXAL SYNTHASE), FORMIC ACID, PHOSPHATE ION, ... (4 entities in total)
Functional Keywords	glycolytic bypass, methylglyoxal, lyase
Biological source	Escherichia coli
Cellular location	Cytoplasm: P0A731
Total number of polymer chains	3
Total formula weight	51229.78
Authors	Saadat, D.,Harrison, D.H.T. (deposition date: 1999-02-23, release date: 1999-03-16, Last modification date: 2023-12-27)
Primary citation	Saadat, D.,Harrison, D.H. The crystal structure of methylglyoxal synthase from Escherichia coli. Structure Fold.Des., 7:309-317, 1999 Cited by PubMed Abstract: The reaction mechanism of methylglyoxal synthase (MGS) is believed to be similar to that of triosephosphate isomerase (TIM). Both enzymes utilise dihydroxyacetone phosphate (DHAP) to form an enediol(ate) phosphate intermediate as the first step of their reaction pathways. However, the second catalytic step in the MGS reaction pathway is characterized by the elimination of phosphate and collapse of the enediol(ate) to form methylglyoxal instead of reprotonation to form the isomer glyceraldehyde 3-phosphate. PubMed: 10368300 DOI: 10.1016/S0969-2126(99)80041-0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation