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J. Biol. Chem., Vol. 269, Issue 40, 24596-24601, 10, 1994
TS Lai, KE Achyuthan, MA Santiago and GS Greenberg
A series of truncation mutants lacking 218, 229, 250, and 269 amino acid
residues from the carboxyl terminus of blood coagulation factor XIII
A-chains (FXIII A), designated as delta K513, delta A502, delta Y481, and
delta K462, respectively, were expressed in Escherichia coli to define the
minimum structure required for transglutaminase activity. delta K513 and
delta A502 displayed a 3.8-4.7-fold reduction in the Kcat with no change in
the Km for the glutamine substrate and a 2-fold increase in the Km of the
primary amine substrate. There was no detectable transglutaminase activity
for either thrombin-activated delta Y481 or delta K462. The rate of ammonia
release of thrombin- activated delta K513 and delta A502 was reduced 6- and
4-fold, respectively, whereas ammonia release was not detected for the
delta Y481 and delta 462 mutants. The Kact for calcium ions of the delta
K513 mutant was similar to recombinant FXIIIa, whereas, it was increased by
approximately 3-fold for the delta A502 mutant. The rate of fibrin
gamma-chain dimer formation for the delta K513 and delta A502 mutants was
reduced by approximately 19-fold. delta K462 did not bind to fibrin, while
all of the other thrombin-cleaved mutants were bound. In conclusion, these
results documented that the carboxyl-terminal calcium binding domain
(Asp468-Glu495) was important for FXIIIa to adopt the correct conformation
to ensure that efficient catalysis occurred.
Carboxyl-terminal truncation of recombinant factor XIII A-chains. Characterization of minimum structural requirement for transglutaminase activity
Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710.
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