• Applied Biological Chemistry
• /
• v.17 no.3
• /
• pp.184-192
• /
• 1974

In the presence of 2N hydrochloric acid, N-bromosuccinimide reacts with 8-aminoquinoline to yield 5,7-dibromo-8-aminoquinoline in aqueous medium. This reaction proceeds readily and quantitatively at room temperature. The mechanism of this reaction is investigated in this work. A new titrimetric method for the micro-determination of 8-aminoquinoline by the use of N-bromosuccinimide is described. The proposed method is quite simple, rapid and yet shows relatively high accuracy over the suggested range. The experimental error does not exceed ${\pm}1.78$ per cent. Results are reported for the comparative analysis of 8-aminoquinoline by the proposed method and by bromimetry.

• BMB Reports
• /
• v.31 no.2
• /
• pp.139-143
• /
• 1998

The catabolic ${\alpha}-acetolactate$ synthase purified from Serratia marcescens ATCC 25419 was rapidly inactivated by the tryptophane-specific reagent, N -bromosuccinimide, and the arginine-specific reagent, phenylglyoxal. The enzyme was inactivated slowly by the cysteine-specific reagent N-ethylmaleimide. The second-order rate constants for the inactivation by N-bromosuccinimide, phenylglyoxal. and N -ethylmaleimide were $114,749M^{-1}min^{-1}$, $304.3M^{-1}min^{-1}$, and $5.1M^{-1}min^{-1}$, respectively. The reaction order with respect to N-bromosuccinimide, phenylglyoxal, and N-ethylmaleimide were 1.5,0.71, and 0.86, respectively. The inactivation of the catabolic aacetolactate synthase by these modifying reagents was protected by pyruvate. These results suggest that essential tryptophane, arginine, and cysteine residues are located at or near the active site of the catabolic ${\alpha}-acetolactate$ synthase.

• Journal of the Korean Chemical Society
• /
• v.31 no.5
• /
• pp.476-478
• /
• 1987

• Archives of Pharmacal Research
• /
• v.13 no.4
• /
• pp.367-370
• /
• 1990

A novel method for the microdetermination of vitamin A in its pure state and pharmaceutical preparation using NBS is reported. The new method is easy, simple and accurate.

• Journal of the Korean Chemical Society
• /
• v.46 no.4
• /
• pp.402-404
• /
• 2002

• Microbiology and Biotechnology Letters
• /
• v.34 no.2
• /
• pp.121-128
• /
• 2006

The purified xylanase from Bacillus alcalophilus AX2000 was modified with various chemical modifiers to determine amino acid residues in the active site of the enzyme. Treatment of the enzyme with group-specific reagents such as carbodiimide or N-bromosuccinimide resulted in complete loss of enzyme activity. These results suggested that these reagents reacted with glutamic acid or aspartic acid and tryptophan residues located at or near the active site. In each case, inactivation was performed by pseudo first-order kinetics. Inhibition of enzyme activity by carbodiimide and N-bromosuccinimide showed non-competitive and competitive inhibition type, respectively. Addition of xylan to the enzyme solution containing N-bromosuccinimide prevented the inactivation, indicating the presence of tryptophan at the substrate binding site. Analysis of kinetics for inactivation showed that the loss of enzyme activity was due to modification of two glutamic acid or aspartic acid residues and single tryptophan residue.

• Journal of Life Science
• /
• v.15 no.4 s.71
• /
• pp.633-640
• /
• 2005

The purified xylanase from Bacillus pumilus TX703 was modified with various chemical modifiers to determine the active sites of the enzyme. Treatment of the enzyme with group-specific reagents such as carbodiimide or N-bromosuccinimide resulted in complete loss of enzyme activity. These results assumed that these reagents reacted with glutamic acid or aspartic acid and tryptophan residues located at or near the active site. In each case, inactivation was performed by pseudo first-order kinetics. Inhibition of enzyme activity by carbodiimide and W-bromosuccinimide showed non-competitive and competitive inhibition type, respectively. Addition of xylan to the enzyme solution containing N-bromosuccinimide prevented the inactivation, indicating the presence of tryptophan at the substrate binding site. Analysis of kinetics for inactivation showed that the loss of enzyme activity was due to modification of two glutamic acid or aspartic acid residues and single tryptophan residue.

• BMB Reports
• /
• v.32 no.3
• /
• pp.294-298
• /
• 1999

Myo-inositol monophosphate phosphatase is a key enzyme in the phosphoinositide cell-signaling system. Incubation of myo-inositol monophosphate phosphatase from porcine brain with N-bromosuccinimide (NBS) resulted in a time-dependent loss of enzyme activity. The inactivation followed pseudo-first-order kinetics with the second-order rate constant of $3.8{\times}10^3\;M^{-1}min^{-1}$. The time course of the reaction was significantly affected by the substrate myo-inositol-1-phosphate, which afforded complete protection against the loss of catalytic activity. Spectrophotometric studies indicated that about one oxindole group per molecule of enzyme was formed following complete loss of enzymatic activity. It is suggested that the catalytic function of myo-inositol monophosphate phosphatase is modulated by the binding of NBS to a specific tryptophan residue at or near the substrate binding site of the enzyme.

• BMB Reports
• /
• v.31 no.3
• /
• pp.258-263
• /
• 1998

Acetolactate synthase (ALS) is the common enzyme in the biosynthetic pathways leading to leucine, valine, and isoleucine. Tobacco ALS was expressed in E. coli and purified to homogeneity. The recombinant tobacco ALS was inactivated by thiol-specific reagents, N-ethylmaleimide (NEM) and 5,5'-dithio-bis-(2-nitrobenzoic acid) (DTNB). Inactivation of the ALS by NEM followed pseudo-first order kinetics and was first order with respect to the modifier. The substrate pyruvate protected the enzyme against the inactivation by NEM and DTNB. Extrapolation to complete inactivation of the enzyme by DTNB showed modification of approximately 2 out of 4 total cysteinyl residues (or 2 cysteinyl and 1 cysteinyl residues), with approximately 1 residue protected by pyruvate. The tobacco ALS was also inactivated by the tryptophanspecific reagent, N-bromosuccinimide (NBS), and was similarly protected by pyruvate. The kinetics of the inactivation was first-order with respect to NBS. The present data suggest that cysteinyl and tryptophanyl residues play a key role in the catalytic function of the enzyme.

• Archives of Pharmacal Research
• /
• v.16 no.2
• /
• pp.152-154
• /
• 1993

By using N-bromophthalimide (NBP) as halonium ion source for the Hofmann rearrangement, a series of primary amide could be ocnverted to the corresponding cabamate in excellent yields. So NBP was throught to be very effective and practical halonium ion source for the Hofmann rearrangement.