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Selective modification of phosphoribulokinase cysteines

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6180371

The most reactive sulfhydryl in native phosphoribulokinase can be selectively alkylated with iodoacetate; complete loss of activity results. Composition and N-terminal analyses of the peptide bearing this -SH show that cys-16 is the modification site. In the presence of Mg and ATP, a nonessential -SH is modified; catalytic activity is unchanged. The peptide bearing this cysteine has been characterized by amino acid composition and N-terminal analyses (Phe-Phe-Asn-Pro-Val-Tyr-(Ile/Leu)...). Enzyme alkylated at this site is subject to reversible oxidative inactivation, showing that this cysteine is not involved in regulation of activity. A cysteine distinct from this nonessential residue is suggested by crosslinking studies to be close (5a) to cys-16. The site-directed inhibitor fluorosulfonylbenzoyladenosine (FSBA) inactivates enzyme by modifying cys-16. Carboxymethylation of enzyme after FSBA incorporation, followed by DTT treatment, unmasks the initial modification site and allows (/sup 14/C)-iodoacetate labeling. The tryptic peptide bearing this residue co-chromatographs with and is identical in composition to the cys-16 containing peptide.

Research Organization:
Medical College of Wisconsin, Milwaukee
OSTI ID:
6180371
Report Number(s):
CONF-870644-
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Vol. 46:6; ISSN FEPRA
Country of Publication:
United States
Language:
English