Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase.-Reference-Cited by-同舟云学术

Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase.

Published:1988-11 Issue:31 Volume:263 Page:15946-15950
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Hum D W,Bell A W,Rozen R,MacKenzie R E

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference34 articles.

1. Folates and Pterins: Chemistry and Biochemistry of Folates;MacKenzie,1984

2. Methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase and formyltetrahydrofolate synthetase from porcine liver

3. Methylenetetrahydrofolate dehydrogenase – methenyltetrahydrofolate cyclohydrolase – formyltetrahydrofolate synthetase from porcine liver Location of the activities in two domains of the multifunctional polypeptide

4. C1-Tetrahydrofolate synthase from rabbit liver. Structural and kinetic properties of the enzyme and its two domains.

5. Formyl-methenyl-methylenetetrahydrofolate synthetase (combined): Correlation of enzymic activities with limited proteolytic degradation of the protein from yeast

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