(Q43923993)

English

Residues involved in the mechanism of the bifunctional methylenetetrahydrofolate dehydrogenase-cyclohydrolase: the roles of glutamine 100 and aspartate 125.

scientific article published on 19 March 2002

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scholarly article

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Europe PubMed Central

PubMed publication ID

28 November 2017

Residues involved in the mechanism of the bifunctional methylenetetrahydrofolate dehydrogenase-cyclohydrolase: the roles of glutamine 100 and aspartate 125. (English)

1 reference

Europe PubMed Central

PubMed publication ID

28 November 2017

author name string

Saravanan Sundararajan

1

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Europe PubMed Central

PubMed publication ID

28 November 2017

Robert E MacKenzie

2

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Europe PubMed Central

PubMed publication ID

28 November 2017

language of work or name

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publication date

19 March 2002

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PubMed publication ID

28 November 2017

Journal of Biological Chemistry

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28 November 2017

277

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Europe PubMed Central

PubMed publication ID

28 November 2017

21

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Europe PubMed Central

PubMed publication ID

28 November 2017

18703-18709

1 reference

Europe PubMed Central

PubMed publication ID

28 November 2017

Methenyltetrahydrofolate cyclohydrolase is rate limiting for the enzymatic conversion of 10-formyltetrahydrofolate to 5,10-methylenetetrahydrofolate in bifunctional dehydrogenase-cyclohydrolase enzymes

1 reference

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Methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase and formyltetrahydrofolate synthetase from porcine liver. Isolation of a dehydrogenase-cyclohydrolase fragment from the multifunctional enzyme

1 reference

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21 January 2018

The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 A resolution

1 reference

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21 January 2018

Structures of three inhibitor complexes provide insight into the reaction mechanism of the human methylenetetrahydrofolate dehydrogenase/cyclohydrolase

1 reference

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Formiminotransferase-cyclodeaminase from procine liver. Purification and physical properties of the enzyme complex

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Expression of active domains of a human folate-dependent trifunctional enzyme in Escherichia coli

1 reference

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Expression of human NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase in Escherichia coli: purification and partial characterization

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 A resolution

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Role of the conserved amino acids of the 'SDN' loop (Ser130, Asp131 and Asn132) in a class A beta-lactamase studied by site-directed mutagenesis

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Active-site mapping and site-specific mutagenesis of glycinamide ribonucleotide transformylase from Escherichia coli

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Heterologous expression and purification of active human phosphoribosylglycinamide formyltransferase as a single domain

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Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase

1 reference

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21 January 2018

Folate activation and catalysis in methylenetetrahydrofolate reductase from Escherichia coli: roles for aspartate 120 and glutamate 28.

1 reference

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21 January 2018

Aspartate 221 of thymidylate synthase is involved in folate cofactor binding and in catalysis

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SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling

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Channeling efficiency in the bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase domain: the effects of site-directed mutagenesis of NADP binding residues

1 reference

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21 January 2018

Methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate-cyclohydrolase-formyltetrahy dro folate synthetase. Affinity labelling of the dehydrogenase-cyclohydrolase active site

1 reference

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21 January 2018

Binding and interconversion of tetrahydrofolates at a single site in the bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase

1 reference

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21 January 2018

Binding of the 2',5'-ADP subsite stimulates cyclohydrolase activity of human NADP(+)-dependent methylenetetrahydrofolate dehydrogenase/cyclohydrolase

1 reference

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21 January 2018

Preparation of 3-aminopyridine adenine dinucleotide and 3-aminopyridine adenine dinucleotide phosphate

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Identification of essential amino acid residues in Clostridiumhistolyticum collagenase using chemical modification reactions

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21 January 2018

Identifiers

10.1074/JBC.M200127200

1 reference

Europe PubMed Central

PubMed publication ID

28 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

28 November 2017

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