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Affinity labeling of spinach phosphoribulokinase subsequent to S-methylation at Cys16

Journal Article · · Journal of Protein Chemistry; (United States)
DOI:https://doi.org/10.1007/BF01024620· OSTI ID:7261102
;  [1];  [2]
  1. Univ. of Tennessee, Oak Ridge (United States)
  2. Oak Ridge National Lab., TN (United States)

The chloroplast enzyme phosphoribulokinase is reversibly deactivated by oxidation of Cys16 and Cys55 to a disulfide. Although not required for catalysis, Cys 16 is an active-site reside positioned at the nucleotide-binding domain. The hyperreactivity of Cys16 has heretofore limited further active-site characterization by chemical modification. To overcome this limitation, the partially active enzyme, S-methylated at Cys16, has been probed with a potential affinity reagent. Treatment of methylated enzyme with bromoacetylethanolamine phosphate results in essentially complete loss of catalytic activity. Inactivation follows pseudo-first-order kinetics and exhibits a rate saturation with an apparent K{sub d} of 3-4mM. ATP, but not ribulose 5-phosphate, affords substantial protection. Complete inactivation correlates with incorporation of 1 mol of ({sup 14}C)reagent per mole of enzyme subunit. Amino acid analysis of the ({sup 14}C)-labeled enzyme demonstrates that only cysteine is modified, and mapping of tryptic digests shows that Cys55 is a major site of alkylation. These results indicate that Cys55 is also located in the ATP-binding domain of the active-site.

DOE Contract Number:
AC05-84OR21400
OSTI ID:
7261102
Journal Information:
Journal of Protein Chemistry; (United States), Journal Name: Journal of Protein Chemistry; (United States) Vol. 9:4; ISSN JPCHD; ISSN 0277-8033
Country of Publication:
United States
Language:
English