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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2003.1
- 수록면
- 228 - 242 (15page)
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초록· 키워드
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Transglutaminase enzymes (TGases) catalyze the
calcium dependent formation of an isopeptide bond
between protein-bound glutamine and lysine substrates.
Previously we have shown that activated
TGase 3 acquires two additional calcium ions at
site two and three. The calcium ion at site three
results in the opening of a channel. At this site,
the channel opening and closing could modulate,
depending on which metal is bound. Here we propose
that the front of the channel could be used
by the two substrates for enzyme reaction. We
propose that the glutamine substrate is directed
from Trp236 into the enzyme, shown by molecular
docking. Then a lysine substrate approaches the
opened active site to engage Trp327, leading to
formation of the isopeptide bond. Further, direct
comparisons of the structures of TGase 3 with
other TGases have allowed us to identify several
residues that might potentially be involved in generic
and specific recognition of the glutamine and
lysine substrates.
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