Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon

Yoshikazu Takada, N. Kaneko, H. Esumi, P. E. Purdue, C. J. Danpure

Research output: Contribution to journalArticle

103 Citations (Scopus)

Abstract

The amino acid sequence of human hepatic peroxisomal L-alanine:glyoxylate aminotransferase 1 (AGT1) deduced from cDNA shows 78% sequence identity with that of rat mitochondrial AGT1, but lacks the N-terminal 22 amino acids (the putative mitochondrial targeting signal). In humans this signal appears to have been depleted during evolution by a point mutation of the initiation codon ATG to ATA. These data suggest that the targeting defect in primary hyperoxaluria type 1, in which AGT1 is diverted from the peroxisomes to the mitochondria, could be due to a point mutation that reintroduces all or part of the mitochondrial signal sequence.

Original languageEnglish (US)
Pages (from-to)517-520
Number of pages4
JournalBiochemical Journal
Volume268
Issue number2
StatePublished - 1990
Externally publishedYes

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Initiator Codon
Point Mutation
Alanine
Amino Acids
Mitochondria
Peroxisomes
Protein Sorting Signals
Rats
Amino Acid Sequence
Complementary DNA
Defects
Liver
Alanine-glyoxylate transaminase

ASJC Scopus subject areas

  • Biochemistry

Cite this

Human peroxisomal L-alanine : glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon. / Takada, Yoshikazu; Kaneko, N.; Esumi, H.; Purdue, P. E.; Danpure, C. J.

In: Biochemical Journal, Vol. 268, No. 2, 1990, p. 517-520.

Research output: Contribution to journalArticle

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