PMID:2510713
| Citation |
Miller, AD, Packman, LC, Hart, GJ, Alefounder, PR, Abell, C and Battersby, AR (1989) Evidence that pyridoxal phosphate modification of lysine residues (Lys-55 and Lys-59) causes inactivation of hydroxymethylbilane synthase (porphobilinogen deaminase). Biochem. J. 262:119-24 |
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| Abstract |
A recombinant strain of Escherichia coli has been constructed that produces approx. 200 times the amount of hydroxymethylbilane synthase found in wild-type E. coli [Hart, Abell & Battersby (1986) Biochem. J. 240, 273-276]. Enzyme purified from this strain is shown to be permanently inactivated by pyridoxal 5'-phosphate/NaB1H3(3)H1. The inactivation is not complete despite the fact that approx. 1 mol of lysine residues is modified per mol of enzyme. Evidence is gained showing that (a) modification of one of two conserved lysine residues (Lys-55 or Lys-59) results in inactivation of hydroxymethylbilane synthase and (b) these lysine residues are present in or close to the active site. |
| Links | |
| Keywords |
Amino Acid Sequence; Ammonia-Lyases/antagonists & inhibitors; Binding Sites; Escherichia coli/enzymology; Hydroxymethylbilane Synthase/antagonists & inhibitors; Lysine/metabolism; Plasmids; Protease Inhibitors/metabolism; Pyridoxal Phosphate/pharmacology |
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