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. 1993 Apr 1;291(Pt 1):37–39. doi: 10.1042/bj2910037

Studies on tissue transglutaminases: interaction of erythrocyte type-2 transglutaminase with GTP.

C M Bergamini 1, M Signorini 1
PMCID: PMC1132477  PMID: 8097088

Abstract

Ca2+ and GTP are the main modulators of type-2 transglutaminases. To study the interaction of the enzyme with GTP, we have employed periodate-oxidized GTP as an affinity-label probe. Dialdehyde GTP bound irreversibly to type-2 transglutaminase in a time-dependent way with 1:1 stoichiometry at complete modification. The reaction took place in the absence, but was more rapid in the presence, of cyanoborohydride. Native GTP prevented incorporation of dialdehyde GTP, and Ca2+ significantly slowed down the reaction rate. The modified enzyme displayed decreased sensitivity to Ca2+, with a sigmoid saturation curve. We conclude that type-2 transglutaminase has a single GTP-binding site, the modification of which by dialdehyde GTP mimics nucleotide binding to the enzyme.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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