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Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase.
J Biol Chem. 1988 Nov 05; 263(31):15946-50.JB

Abstract

A DNA clone complementary to the messenger RNA encoding the human trifunctional enzyme 5,10-methylenetetrahydrofolate dehydrogenase-5,10-methenyl-tetrahydrofolate cyclohydrolase-10-formyltetrahydrofolate synthetase has been isolated from a lambda gt10 library. In vitro transcription-translation of the 3.1-kilobase cDNA clone yields a protein of 101 kDa, which is of identical size and exhibits the same immunoreactivity as the enzyme purified from human liver. A coding region of 2805 base pairs in the cDNA encodes a protein of 935 amino acids. The initiator methionine is absent from the purified enzyme and the amino-terminal 30 amino acids derived by automated sequence analysis are identical (arginine at position 18 was not identified) with that deduced from the nucleotide sequence. The amino acid sequence of the human enzyme shows extensive homology with that of the yeast enzyme, although the amino-terminal bifunctional dehydrogenase-cyclohydrolase domain is less homologous than the carboxyl-terminal synthetase domain. A region was identified which probably serves as a link between these two major domains of the human enzyme. The synthetase domain contains two regions that are homologous to consensus sequences for an ATP-binding site.

Authors+Show Affiliations

Department of Biochemistry, McGill University, Montreal, Canada.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

3053686

Citation

Hum, D W., et al. "Primary Structure of a Human Trifunctional Enzyme. Isolation of a cDNA Encoding Methylenetetrahydrofolate Dehydrogenase-methenyltetrahydrofolate Cyclohydrolase-formyltetrahydrofolate Synthetase." The Journal of Biological Chemistry, vol. 263, no. 31, 1988, pp. 15946-50.
Hum DW, Bell AW, Rozen R, et al. Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase. J Biol Chem. 1988;263(31):15946-50.
Hum, D. W., Bell, A. W., Rozen, R., & MacKenzie, R. E. (1988). Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase. The Journal of Biological Chemistry, 263(31), 15946-50.
Hum DW, et al. Primary Structure of a Human Trifunctional Enzyme. Isolation of a cDNA Encoding Methylenetetrahydrofolate Dehydrogenase-methenyltetrahydrofolate Cyclohydrolase-formyltetrahydrofolate Synthetase. J Biol Chem. 1988 Nov 5;263(31):15946-50. PubMed PMID: 3053686.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase. AU - Hum,D W, AU - Bell,A W, AU - Rozen,R, AU - MacKenzie,R E, PY - 1988/11/5/pubmed PY - 1988/11/5/medline PY - 1988/11/5/entrez SP - 15946 EP - 50 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 263 IS - 31 N2 - A DNA clone complementary to the messenger RNA encoding the human trifunctional enzyme 5,10-methylenetetrahydrofolate dehydrogenase-5,10-methenyl-tetrahydrofolate cyclohydrolase-10-formyltetrahydrofolate synthetase has been isolated from a lambda gt10 library. In vitro transcription-translation of the 3.1-kilobase cDNA clone yields a protein of 101 kDa, which is of identical size and exhibits the same immunoreactivity as the enzyme purified from human liver. A coding region of 2805 base pairs in the cDNA encodes a protein of 935 amino acids. The initiator methionine is absent from the purified enzyme and the amino-terminal 30 amino acids derived by automated sequence analysis are identical (arginine at position 18 was not identified) with that deduced from the nucleotide sequence. The amino acid sequence of the human enzyme shows extensive homology with that of the yeast enzyme, although the amino-terminal bifunctional dehydrogenase-cyclohydrolase domain is less homologous than the carboxyl-terminal synthetase domain. A region was identified which probably serves as a link between these two major domains of the human enzyme. The synthetase domain contains two regions that are homologous to consensus sequences for an ATP-binding site. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/3053686/Primary_structure_of_a_human_trifunctional_enzyme__Isolation_of_a_cDNA_encoding_methylenetetrahydrofolate_dehydrogenase_methenyltetrahydrofolate_cyclohydrolase_formyltetrahydrofolate_synthetase_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=3053686 DB - PRIME DP - Unbound Medicine ER -