Unknown

Dataset Information

0

Ground-state electronic destabilization via hyperconjugation in aspartate aminotransferase.


ABSTRACT: Binding isotope effects for l-aspartate reacting with the inactive K258A mutant of PLP-dependent aspartate aminotransferase to give a stable external aldimine intermediate are reported. They provide direct evidence for electronic ground-state destabilization via hyperconjugation. The smaller equilibrium isotope effect with deazaPLP-reconstituted K258A indicates that the pyridine nitrogen plays an important role in labilizing the C?-H bond.

SUBMITTER: Griswold WR 

PROVIDER: S-EPMC3425665 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Ground-state electronic destabilization via hyperconjugation in aspartate aminotransferase.

Griswold Wait R WR   Castro Joan Nieto JN   Fisher Andrew J AJ   Toney Michael D MD  

Journal of the American Chemical Society 20120510 20


Binding isotope effects for l-aspartate reacting with the inactive K258A mutant of PLP-dependent aspartate aminotransferase to give a stable external aldimine intermediate are reported. They provide direct evidence for electronic ground-state destabilization via hyperconjugation. The smaller equilibrium isotope effect with deazaPLP-reconstituted K258A indicates that the pyridine nitrogen plays an important role in labilizing the Cα-H bond. ...[more]

Similar Datasets

| S-EPMC3101270 | biostudies-literature
| S-EPMC3651043 | biostudies-literature
| S-EPMC3699461 | biostudies-literature
| S-EPMC6726543 | biostudies-literature
| S-EPMC7181641 | biostudies-literature
| S-EPMC7735706 | biostudies-literature
| S-EPMC5658032 | biostudies-literature
| S-EPMC1766402 | biostudies-literature
| S-EPMC10798825 | biostudies-literature
| S-EPMC6735427 | biostudies-literature