Modification of tryptophan 149 of inorganic pyrophosphatase from Escherichia coli.
1. The inorganic pyrophosphatase from Escherichia coli was almost completely inactivated on chemical modification of Trp-149 with N-bromosuccinimide (NBS). 2. The presence of a complex of Mg2+ and a substrate analogue, iminodiphosphate (PNP), provided considerable protection against the inactivation, whereas Mg2+ or PNP alone afforded only slight protection.
Institute of High Polymer Research, Faculty of Textile Science and Technology, Shinshu University, Nagano-ken, Japan.
S
S
Kaneko
T
T
Ichiba
N
N
Hirano
A
A
Hachimori
D000595:Amino Acid Sequence; D001665:Binding Sites; D001974:Bromosuccinimide / Q000494:pharmacology; D002942:Circular Dichroism; D004347:Drug Interactions; D004926:Escherichia coli / Q000201:enzymology*; D008274:Magnesium / Q000008:administration & dosage / Q000494:pharmacology; D008969:Molecular Sequence Data; D010710:Phosphates / Q000008:administration & dosage / Q000494:pharmacology; D011755:Pyrophosphatases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D014364:Tryptophan / Q000737:chemistry*
D010710:Phosphates; D014364:Tryptophan; D011755:Pyrophosphatases; D008274:Magnesium; D001974:Bromosuccinimide