Document Detail

Chemical modification by 2,4,6-trinitrobenzenesulfonic acid (TNBS) of an essential amino group in 3-ketovalidoxylamine A C-N lyase.
MedLine Citation:
PMID:  2393971     Owner:  NLM     Status:  MEDLINE    
3-Ketovalidoxylamine A C-N lyase of Flavobacterium saccharophilum is a monomeric protein with a molecular weight of 36000, and contains 32 amino groups and no cysteine or cystine residues. The enzyme was inactivated by 2,4,6-trinitrobenzenesulfonic acid (TNBS) following pseudo-first order kinetics. Substrate of the lyase, p-nitrophenyl-3-ketovalidamine, protected the enzyme against the inactivation, suggesting that the modification occurred at or near the active site. Although several amino groups were modified by TNBS, a plot of log (reciprocal of the half-time of inactivation) versus log (concentration of TNBS) suggested that one amino group has an essential role in catalysis.
M Takeuchi; K Neyazaki; K Matsui
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Chemical & pharmaceutical bulletin     Volume:  38     ISSN:  0009-2363     ISO Abbreviation:  Chem. Pharm. Bull.     Publication Date:  1990 May 
Date Detail:
Created Date:  1990-10-11     Completed Date:  1990-10-11     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0377775     Medline TA:  Chem Pharm Bull (Tokyo)     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  1419-20     Citation Subset:  IM    
Department of Biochemistry, School of Pharmacy, Hokuriku University, Ishikawa, Japan.
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MeSH Terms
Amino Acids / analysis*
Carbon-Nitrogen Lyases*
Chemical Phenomena
Circular Dichroism
Lyases / analysis,  antagonists & inhibitors*
Nitrobenzenes / pharmacology*
Trinitrobenzenesulfonic Acid / pharmacology*
Reg. No./Substance:
0/Amino Acids; 0/Nitrobenzenes; 2508-19-2/Trinitrobenzenesulfonic Acid; EC 4.-/Lyases; EC 4.3.-/Carbon-Nitrogen Lyases; EC A C-N lyase

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