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Transition-State Structure for the...
Journal article

Transition-State Structure for the ADP-Ribosylation of Recombinant Gi α 1 Subunits by Pertussis Toxin †

Abstract

Pertussis toxin ADP-ribosylates a specific Cys side chain in the alpha-subunit of several G-proteins. Recombinant Gialpha1-subunits were rapidly ADP-ribosylated in the absence of betagamma-subunits, with a Km of 800 microM and a kcat of 40 min-1. Addition of betagamma-subunits decreases Km to 0.3 microM with little change of kcat. Kinetic isotope effects established the transition-state structure for ADP-ribosylation of Gialpha1 subunits. The …

Authors

Scheuring J; Berti PJ; Schramm VL

Journal

Biochemistry, Vol. 37, No. 9, pp. 2748–2758

Publisher

American Chemical Society (ACS)

Publication Date

March 1, 1998

DOI

10.1021/bi972594x

ISSN

0006-2960