Purification, characterization, cloning, and amino acid sequence of the bifunctional enzyme 5,10-methylenetetrahydrofolate dehydrogenase/5,10-methenyltetrahydrofolate cyclohydrolase from Escherichia coli.-Reference-Cited by-同舟云学术

Purification, characterization, cloning, and amino acid sequence of the bifunctional enzyme 5,10-methylenetetrahydrofolate dehydrogenase/5,10-methenyltetrahydrofolate cyclohydrolase from Escherichia coli.

Published:1991-12 Issue:35 Volume:266 Page:23953-23958
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

D'Ari L.,Rabinowitz J.C.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference45 articles.

1. Occurrence of N10-formyltetrahydrofolic acid and its general involvement in transformylation

2. On the occurrence of N10-formyltetrahydrofolic acid by enzymic formylation of tetrahydrofolic acid and on the mechanism of this reaction

3. Enzymes of Clostridial Purine Fermentation

4. Purification and Characterization of Thermostable 5,10-Methylenetetrahydrofolate Dehydrogenase from Clostridium thermoaceticum

5. [83] Methylenetetrahydrofolate dehydrogenase from Clostridium formicoaceticum and methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase (combined) from Clostridium thermoaceticum

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