Aug 1, 1976

Chemical modification of two tryptophan residues abolishes the catalytic activity of aminoacylase

Hoppe-Seyler's Zeitschrift für physiologische Chemie
W Kördel, F R Schneider

Abstract

1) The reaction of 1 H-diazotetrazole and N-bromosuccinimide with aminoacylase was studied under different conditions. A tenfold molar excess of 1 H-diazotetrazole (2 X 10(-4) M) at pH 5.5 abolishes the catalytic activity of the enzyme while modifying only two tryptophan residues. No other amino acid reacted under these conditions as tested by amino acid analysis. 2) With a 40-fold molar excess of N-bromosuccinimide (8 X 10(-4)M) at pH 5.0, two tryptophan residues of the enzyme were oxidized with complete loss of activity. Under these conditions no significant cleavage of the polypeptide chain was observed. Neither tyrosine nor histidine was modified by this reagent, up to a 100-fold molar excess. 3) Substrates and reversible (N-tosylalanine) and irreversible (TosPheCH2Cl) inhibitors of the enzyme do not protect the two reactive tryptophans against the modification reagents. Under more drastic conditions, lysine, tyrosine and histidine residues are also modified by the reagents.

  • References2
  • Citations9

References

  • References2
  • Citations9

Citations

Mentioned in this Paper

Tryptophan
Histidine
Cytokinesis of the Fertilized Ovum
Abufne
Lysine
Tosyl Compounds
Enzyme Activity
Azoles
PMS-Tryptophan
Molar Tooth

About this Paper

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