Noncoded amino acid replacement probes of the aspartate aminotransferase mechanism.

doi:10.1021/bi970298e

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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 transcriptio...

Topics

Alanine
Amino Acids
Arginine
Aspartate Aminotransferases
Aspartic Acid
Escherichia coli
Glutamic Acid
Hydrogen Bonding
Hydrogen-Ion Concentration
Kinetics
Molecular Structure
Mutation
Protein Biosynthesis
Recombinant Proteins
Stereoisomerism
Substrate Specificity
Transcription, Genetic
Tyrosine

Source

Open in PubMed

Identifiers

PMID: 9265632
DOI: 10.1021/bi970298e

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9265632-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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