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Article

Role of the conserved active site residue tryptophan-24 of human dihydrofolate reductase as revealed by mutagenesis.

Biochemistry - 5 Feb 1991

Beard W A, Appleman J R, Huang S M, Delcamp T J, Freisheim J H, Blakley R L

Abstract excerpt

The active sites of all bacterial and vertebrate dihydrofolate reductases that have been examined have a tryptophan residue near the binding sites for NADPH and dihydrofolate. In cases where the three-dimensional structure has been determined by X-ray crystallography, this conserved tryptophan residue makes hydrophobic and van der Waals interactions with the nicotinamide moiety of bound NADPH, and its indole...

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Identifiers

PMID: 1991124
DOI: 10.1021/bi00219a038

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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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