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Article

Noncoded amino acid replacement probes of the aspartate aminotransferase mechanism.

Biochemistry - 26 Aug 1997

Park Y, Luo J, Schultz P G, Kirsch J F

Abstract excerpt

The primary role of Tyr225 in the aspartate aminotransferase mechanism is to provide a hydrogen bond to stabilize the 3'O- functionality of bound pyridoxal phosphate. The strength of this hydrogen bond is perturbed by replacement of Tyr225 with 3-fluoro-L-tyrosine (FlTyr) by in vitro transcription/translation. This mutant enzyme exhibits kcat/values that are near to those of wild type enzyme; however, the kcat/vs...

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PMID: 9265632
DOI: 10.1021/bi970298e

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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