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. 1978 Jun 1;171(3):719–723. doi: 10.1042/bj1710719

Kinetic studies with the use of proton-magnetic-resonance spectroscopy of the specific alpha-deuteration of amino acids by Escherichia coli aspartate aminotransferase.

E Gout, S Chesne, C G Beguin, J Pelmont
PMCID: PMC1184019  PMID: 352342

Abstract

Escherichia coli aspartate aminotransferase was exposed to aspartate or phenylalanine without oxo acid in buffered 2H2O. The alpha-hydrogen of the amino acids underwent first-order exchange with respect to both substrate and enzyme. P.m.r. spectroscopy gave consistent reaction-rate constants. The deuterium-exchange rate was only moderately increased by addition of oxo acids and was of the same order as the transamination rate. No beta-deuteration was observed. The C(alpha)-H-bond-breaking step is discussed as a part of the entire transamination mechanism.

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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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