Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase

Robert J. Cook, Robert (Stephen) Lloyd, Conrad Wagner

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

We have isolated and characterized cDNA clones encoding rat liver cytosol 10-formyltetrahydrofolate dehydrogenase (EC 1.5.1.6). An open reading frame of 2706 base pairs encodes for 902 amino acids of Mr 99,015. The deduced amino acid sequence contains exact matches to the NH2-terminal sequence (28 residues) and the sequences of five peptides derived from cyanogen bromide cleavage of the purified protein. The amino acid sequence of 10-formyltetrahydrofolate dehydrogenase has three putative domains. The NH2-terminal sequence (residues 1-203) is 24-30% identical to phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) from Bacillus subtilis (30%), Escherichia coli (24%), Drosophila melanogaster (24%), and human hepatoma HepG2 (27%). Residues 204-416 show no extensive homology to any known protein sequence. Sequence 417-900 is 46% (mean) identical to the sequences of a series of aldehyde dehydrogenase (NADP+) (EC 1.2.1.3). Intact 10-formyltetrahydrofolate dehydrogenase exhibits NADP-dependent aldehyde dehydrogenase activity. The sequence identity to phosphoribosylglycinamide formyltransferase is discussed, and a binding region for 10-formyltetrahydrofolate is proposed.

Original languageEnglish (US)
Pages (from-to)4965-4973
Number of pages9
JournalJournal of Biological Chemistry
Volume266
Issue number8
StatePublished - Mar 15 1991
Externally publishedYes

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Phosphoribosylglycinamide Formyltransferase
Liver
Rats
Aldehyde Dehydrogenase
Complementary DNA
Clone Cells
NADP
Amino Acids
Amino Acid Sequence
Cyanogen Bromide
Bacilli
Bacillus subtilis
Drosophila melanogaster
Base Pairing
Cytosol
Escherichia coli
Open Reading Frames
Hepatocellular Carcinoma
Proteins
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase. / Cook, Robert J.; Lloyd, Robert (Stephen); Wagner, Conrad.

In: Journal of Biological Chemistry, Vol. 266, No. 8, 15.03.1991, p. 4965-4973.

Research output: Contribution to journalArticle

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abstract = "We have isolated and characterized cDNA clones encoding rat liver cytosol 10-formyltetrahydrofolate dehydrogenase (EC 1.5.1.6). An open reading frame of 2706 base pairs encodes for 902 amino acids of Mr 99,015. The deduced amino acid sequence contains exact matches to the NH2-terminal sequence (28 residues) and the sequences of five peptides derived from cyanogen bromide cleavage of the purified protein. The amino acid sequence of 10-formyltetrahydrofolate dehydrogenase has three putative domains. The NH2-terminal sequence (residues 1-203) is 24-30{\%} identical to phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) from Bacillus subtilis (30{\%}), Escherichia coli (24{\%}), Drosophila melanogaster (24{\%}), and human hepatoma HepG2 (27{\%}). Residues 204-416 show no extensive homology to any known protein sequence. Sequence 417-900 is 46{\%} (mean) identical to the sequences of a series of aldehyde dehydrogenase (NADP+) (EC 1.2.1.3). Intact 10-formyltetrahydrofolate dehydrogenase exhibits NADP-dependent aldehyde dehydrogenase activity. The sequence identity to phosphoribosylglycinamide formyltransferase is discussed, and a binding region for 10-formyltetrahydrofolate is proposed.",
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