The functional involvement of Lys-38 in the heavy subunit of rat kidney γ-glutamylcysteine synthetase: Chemical modification and mutagenesis studies View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1996-04

AUTHORS

Long-sen Chang

ABSTRACT

Rat kidneyγ-glutamylcysteine synthetase (γGCS) was inactivated by reaction with trinitrobenzene sulfonate (TNBS), and the reaction followed pseudo-first-order kinetics. Inactivation kinetics revealed that only one of the amino acid residues modified by TNBS was essential for-γGCS activity. The addition of 10 mM Mg2+ to the TNBS inactivation reaction resulted in a 16-fold increase in the rate of inactivation. Chromatographic analysis on the tryptic hydrolyzates of trinitrophenylated (TNP) derivatives showed that Lys-38 in theγGCS heavy subunit was significantly modified in the presence of Mg2+. In contrast to small changes in the catalytic properties observed by mutation of Lys-38 to Arg, the mutants K38N and K38E had a marked decrease in enzymatic activity and about twofold increase inKm for glutamate. These results suggest that the positively charged Lys-38 may sbe involved in the binding of glutamate toγGCS. More... »

PAGES

321-326

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf01887121

DOI

http://dx.doi.org/10.1007/bf01887121

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1017510130

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8804580


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