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Article

A unique molecular basis for enzyme mistargeting in primary hyperoxaluria type 1.

Clinica chimica acta; international journal of clinical chemistry - 9 Oct 1997

Leiper J M, Danpure C J

Abstract excerpt

The intermediary metabolic enzyme alanine:glyoxylate aminotransferase (AGT) is normally targeted to the peroxisomes in human liver cells. However, in a third of patients suffering from the autosomal recessive disease primary hyperoxaluria type 1 (PH1), AGT is mistargeted to the mitochondria. Such organelle-to-organelle mistargeting is without parallel in human genetic disease. AGT mistargeting results from the...

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Source

Identifiers

PMID: 9435987
DOI: 10.1016/s0009-8981(97)00165-4

Genes

AGT

Provenance

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.

Related research

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A unique molecular basis for enzyme mistargeting in primary hyperoxaluria type 1.PMID 9435987Read ↗

The molecular basis of alanine: glyoxylate aminotransferase mistargeting: the most common single cause of primary hyperoxaluria type 1.Semantic proximity Read ↗

Primary hyperoxaluria type 1: AGT mistargeting highlights the fundamental differences between the peroxisomal and mitochondrial protein import pathways.Semantic proximity Read ↗

Alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting in human hereditary kidney stone disease.Semantic proximity Read ↗

Primary hyperoxaluria type 1: genotypic and phenotypic heterogeneity.Semantic proximity Read ↗

Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1.Semantic proximity Read ↗

Four of the most common mutations in primary hyperoxaluria type 1 unmask the cryptic mitochondrial targeting sequence of alanine:glyoxylate aminotransferase encoded by the polymorphic minor allele.Semantic proximity Read ↗

Mistargeting of peroxisomal L-alanine:glyoxylate aminotransferase to mitochondria in primary hyperoxaluria patients depends upon activation of a cryptic mitochondrial targeting sequence by a point mutation.Semantic proximity Read ↗

Structural implications of a G170R mutation of alanine:glyoxylate aminotransferase that is associated with peroxisome-to-mitochondrion mistargeting.Semantic proximity Read ↗

The role of protein denaturation energetics and molecular chaperones in the aggregation and mistargeting of mutants causing primary hyperoxaluria type I.Semantic proximity Read ↗

Molecular insights into primary hyperoxaluria Type I pathogenesisSemantic proximity Read ↗

Primary hyperoxaluria type 1 caused by peroxisome-to-mitochondrion mistargeting of alanine: glyoxylate aminotransferase.Semantic proximity Read ↗

Biochemical and cellular effects of a novel missense mutation of the AGXT gene associated with Primary Hyperoxaluria Type 1.Semantic proximity Read ↗

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