Dipyrromethane cofactor assembly of porphobilinogen deaminase: formation of apoenzyme and preparation of holoenzyme.
Shoolingin-Jordan
P M
PM
Department of Biochemistry, School of Biological Science, University of Southampton, United Kingdom.
Warren
M J
MJ
Awan
S J
SJ
D001051:Apoenzymes / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D003067:Coenzymes / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D011163:Hydroxymethylbilane Synthase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D007982:Levulinic Acids / Q000378:metabolism; D015394:Molecular Structure; D011162:Porphobilinogen / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D014577:Uroporphyrinogens / Q000302:isolation & purification / Q000378:metabolism
D001051:Apoenzymes; D003067:Coenzymes; D007982:Levulinic Acids; D014577:Uroporphyrinogens; C056776:dipyrromethane cofactor; C024393:hydroxymethylbilane; D011162:Porphobilinogen; D011163:Hydroxymethylbilane Synthase; C032246:levulinic acid