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J. Biol. Chem., Vol. 262, Issue 33, 15825-15828, 11, 1987
M Volokita and CR Somerville
A cDNA clone encoding the peroxisomal enzyme glycolate oxidase (EC
1.1.3.15) was identified by probing a cDNA library of spinach with
synthetic oligonucleotides based on the partial amino acid sequence of the
enzyme. Determination of the DNA sequence of the 1526-nucleotide cDNA
indicated a 1107-nucleotide open reading frame which encodes a polypeptide
of 40,282 daltons. The polypeptide produced by in vitro transcription and
translation of the cDNA insert had the same apparent subunit molecular mass
as the enzyme purified from leaves, indicating that the cDNA encodes a
full-length polypeptide and that no cleavage of the polypeptide is required
for uptake of the polypeptide by peroxisomes. Comparison of the deduced
amino acid sequence with those of two other plant peroxisomal proteins
revealed a region of homology which may be involved in directing proteins
to the peroxisome.
The primary structure of spinach glycolate oxidase deduced from the DNA sequence of a cDNA clone
MSU-DOE Plant Research Laboratory, East Lansing 48824.
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