Structure and Function of Aspartate Aminotransferase

Ueno, Hiroshi; Kagamiyama, Hiroyuki

doi:10.1002/9783527615971.ch5

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1996

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“…A large negative deviation for V39F mutant (Fig. 1) may be ascribed to the enhanced van der Waals interaction with the side chains of Tyr 70 and Ile 37, which causes the stabilization of the "closed" conformation of the enzyme (Kamitori et al, 1990;Ueno & Kagamiyama, 1994). The amino acid substitution at Val 39 evidently changes the catalytic efficiency of AspAt, kcu,/Krn, where major changes occur on K,, but not on kc,, (Hayashi et al, 1991).…”

Section: K Gekko Et Almentioning

confidence: 94%

A large compressibility change of protein induced by a single amino acid substitution

et al. 1996

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The adiabatic compressibility (βs) was determined, by means of the precise sound velocity and density measurements, for a series of single amino acid substituted mutant enzymes of Escherichia coli dihydrofolate reductase (DHFR) and aspartate aminotransferase (AspAT). Interestingly, the βs values of both DHFR and AspAT were influenced markedly by the mutations at glycine‐121 and valine‐39, respectively, in which the magnitude of the change was proportional to the enzyme activity. This result demonstrates that the local change of the primary structure plays an important role in atomic packing and protein dynamics, which leads to the modified stability and enzymatic function. This is the first report on the compressibility of mutant proteins.

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Section: K Gekko Et Almentioning

confidence: 94%