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Article

Functionally important residues tyrosine-171 and serine-158 in sepiapterin reductase.

Biochimica et biophysica acta - 18 May 1999

Fujimoto K, Ichinose H, Nagatsu T, Nonaka T, Mitsui Y, Katoh S

Abstract excerpt

The active site of sepiapterin reductase (SPR), which is a member of the NADP(H)-preferring short-chain dehydrogenase/reductase (SDR) family and acts as the terminal enzyme in the biosynthetic pathway of tetrahydrobiopterin cofactor (BH4), was investigated by truncation and site-directed mutagenesis. The truncation mutants showed that N-terminal and C-terminal residues contribute to bind coenzyme and substrate,...

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Share to Alcohol Oxidoreductases
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 10350607
DOI: 10.1016/s0167-4838(99)00054-0

Genes

SPR

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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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