|
In enzymology, a diaminopimelate decarboxylase () is an enzyme that catalyzes the chemical reaction :meso-2,6-diaminoheptanedioate L-lysine + CO2 Hence, this enzyme has one substrate, meso-2,6-diaminoheptanedioate, and two products, L-lysine and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is meso-2,6-diaminoheptanedioate carboxy-lyase (L-lysine-forming). Other names in common use include diaminopimelic acid decarboxylase, meso-diaminopimelate decarboxylase, DAP-decarboxylase, and meso-2,6-diaminoheptanedioate carboxy-lyase. This enzyme participates in lysine biosynthesis. It employs one cofactor, pyridoxal phosphate. ==Structural studies== As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and . 抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)』 ■ウィキペディアで「Diaminopimelate decarboxylase」の詳細全文を読む スポンサード リンク
|