Impact of Mutating the Key Residues of a Bifunctional 5,10-Methylenetetrahydrofolate Dehydrogenase-Cyclohydrolase from Escherichia coli on Its Activities-Reference-Cited by-同舟云学术

Impact of Mutating the Key Residues of a Bifunctional 5,10-Methylenetetrahydrofolate Dehydrogenase-Cyclohydrolase from Escherichia coli on Its Activities

Published:2015-05-28 Issue:22 Volume:54 Page:3504-3513
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Sah Shivjee¹,Varshney Umesh¹²

Affiliation:

1. Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India

2. Jawaharlal Nehru Centre for Advanced Scientific Research, Bangalore 560064, India

Funder

Department of Biotechnology , Ministry of Science and Technology

Department of Science and Technology, Ministry of Science and Technology

University Grants Commission

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b00400

Reference49 articles.

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

2. Formyl-methenyl-methylenetetrahydrofolate synthetase(combined) from yeast. Biochemical characterization of the protein from an ade3 mutant lacking the formyltetrahydrofolate synthetase function.

3. Methylene tetrahydrofolate dehydrogenase/cyclohydrolase and the synthesis of 10-CHO-THF are essential inLeishmania major

4. Structures of Three Inhibitor Complexes Provide Insight into the Reaction Mechanism of the Human Methylenetetrahydrofolate Dehydrogenase/Cyclohydrolase

5. [85] Formyl-methenyl-methylenetetrahydrofolate synthetase (combined): A multifunctional protein in eukaryotic folate metabolism

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