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Article

A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1.

Genomics - 1 May 1992

Purdue P E, Lumb M J, Allsop J, Minatogawa Y, Danpure C J

Abstract excerpt

We have synthesized and sequenced alanine:glyoxylate aminotransferase (AGT; HGMW-approved symbol for the gene--AGXT) cDNA from the liver of a primary hyperoxaluria type 1 (PH1) patient who had normal levels of hepatic peroxisomal immunoreactive AGT protein, but no AGT catalytic activity. This revealed the presence of a single point mutation (G----A at cDNA nucleotide 367), which is predicted to cause a...

Topics

Alanine
Amino Acid Sequence
Base Sequence
Glutamates
Glutamic Acid
Glycine
Humans
Hyperoxaluria, Primary
Liver
Microbodies
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Polymerase Chain Reaction

Transaminases

Source

Identifiers

PMID: 1349575
DOI: 10.1016/0888-7543(92)90225-h

Genes

AGT
AGXT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1349575-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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