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Ligand 5,10-methenyltetrahydrofolate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

histidine metabolism, purine metabolism, reductive acetyl coenzyme A pathway

KEGG

Biosynthesis of cofactors, Carbon fixation pathways in prokaryotes, Carbon metabolism, Microbial metabolism in diverse environments, One carbon pool by folate

MetaCyc

folate transformations I, folate transformations II (plants), folate transformations III (E. coli), formaldehyde oxidation VII (THF pathway), formate assimilation into 5,10-methylenetetrahydrofolate, L-histidine degradation III, purine nucleobases degradation I (anaerobic), purine nucleobases degradation II (anaerobic), reductive acetyl coenzyme A pathway I (homoacetogenic bacteria), reductive glycine pathway of autotrophic CO2 fixation, tetrahydrofolate salvage from 5,10-methenyltetrahydrofolate more

Show all BRENDA pathways known for 5,10-methenyltetrahydrofolate

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (7 results)

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Show Natural Substrate (7 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.1.15

5,10-methenyltetrahydrofolate + NADH + H+ = 5,10-methylenetetrahydrofolate + NAD+

765009

-

1.5.1.15

L-5,10-methenyl-tetrahydrofolate + NADH = L-5,10-methylenetetrahydrofolate + NAD+

392077, 392092, 392086, 392088, 392090, 392091, 392093, 392075, 392076, 392078, 392079, 392080, 392081, 392082, 392084, 392085, 392087, 392083, 392089

-

1.5.1.15

2 entries

1.5.8.4

5,10-methenyltetrahydrofolate + FADH2 = 5,10-methylene tetrahydrofolate + FAD

657277

-

3.5.4.9

5,10-methenyl-tetrahydrofolate + H2O = 10-formyltetrahydrofolate + H+

701402

-

3.5.4.9

5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate

209738, 209721, 209731, 485728, 209737, 209729, 209739, 209742, 209728, 392333, 712483, 734262, 209719, 209740, 209734, 209736, 712988, 209732, 1505, 209725, 209727, 209722, 209726, 1518, 209720, 209730, 712978, 700281, 209741, 209718, 735050, 744335, 701402

-

3.5.4.9

5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate + ?

698187

-

3.5.4.9

N5,N10-methenyltetrahydrofolate + H2O = N10-formyltetrahydrofolate

720406

-

3.5.4.9

4 entries

In Vivo Product in Enzyme-catalyzed Reactions (16 results)

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Show Natural Product (16 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.1.15

L-5,10-methylenetetrahydrofolate + NAD+ = 5,10-methenyl-tetrahydrofolate + NADH

0

-

1.5.1.15

5,10-methylenetetrahydrofolate + NAD+ = 5,10-methenyltetrahydrofolate + NADH

0

-

1.5.1.15

5,10-methylenetetrahydrofolate + NAD+ = 5,10-methenyltetrahydrofolate + NADH + H+

0

-

1.5.1.15

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH + H+

0

-

1.5.1.5

5,10-methylene tetrahydrofolate + NAD+ = 5,10-methenyl tetrahydrofolate + NADH + H+

0

-

1.5.1.5

5,10-methylene tetrahydrofolate + NADP+ = 5,10-methenyl tetrahydrofolate + NADPH

0

-

1.5.1.5

5,10-methylene tetrahydrofolate + NADP+ = 5,10-methenyl tetrahydrofolate + NADPH + H+

0

-

1.5.1.5

5,10-methylene-tetrahydrofolate + NAD+ = 5,10-methenyl-tetrahydrofolate + NADH

0

-

1.5.1.5

5,10-methylene-tetrahydrofolate + NADP+ = 5,10-methenyl-tetrahydrofolate + NADPH + H+

0

-

1.5.1.5

5,10-methylene tetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH

0

-

1.5.1.5

5,10-methylenetetrahydrofolate + NAD+ = 5,10-methenyltetrahydrofolate + NADH + H+

0

-

1.5.1.5

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH + H+

0, 392313, 392316, 392306, 392310, 392309

-

1.5.1.15

4 entries

1.5.1.5

8 entries

3.5.4.9

10-formyltetrahydrofolate = 5,10-methenyltetrahydrofolate + H2O

0

-

4.3.1.4

5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH3

0

-

6.3.3.2

ATP + 5-formyltetrahydrofolate = ADP + 5,10-methenyltetrahydrofolate + phosphate

0

-

6.3.3.2

ATP + 5-formyltetrahydrofolate = ADP + phosphate + 5,10-methenyltetrahydrofolate

652430, 0, 652260, 652326, 649293

-

6.3.3.2

2 entries

Substrate in Enzyme-catalyzed Reactions (16 results)

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Show Substrate (16 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.1.15

5,10-methenyltetrahydrofolate + NADH + H+ = 5,10-methylenetetrahydrofolate + NAD+

765009

-

1.5.1.15

L-5,10-methenyl-tetrahydrofolate + NADH = L-5,10-methylenetetrahydrofolate + NAD+

392077, 392092, 392086, 392088, 392090, 392091, 392093, 392075, 392076, 392078, 392079, 392080, 392081, 392082, 392084, 392085, 392087, 392083, 392089

-

1.5.1.15

2 entries

1.5.8.4

5,10-methenyltetrahydrofolate + FADH2 = 5,10-methylene tetrahydrofolate + FAD

657277

-

2.1.1.45

(R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP

692639

-

2.1.1.45

(R)-5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP

692639

-

2.1.2.2

N5,N10-anhydroformyl-5,6,7,8tetrahydrofolic acid + 2-amino-N-ribosylacetamide 5'-phosphate + H2O = formylglycinamide ribotide + tetrahydrofolic acid + 2-formamido-N-ribosylacetamide 5'-phosphate

485713

-

2.1.2.2

N5,N10-anhydroformyltetrahydrofolate + glycinamide ribotide + H2O = N10-formyltetrahydrofolate + formylglycinamide ribotide

485718, 485713

-

2.1.2.2

N5,N10-anhydroformyltetrahydrofolic acid + glycinamide ribonucleotide = formylglycinamide ribonucleotide + ?

485742

-

2.1.1.45

2 entries

2.1.2.2

3 entries

2.1.2.3

N5,N10-anhydroformyltetrahydrofolic acid + glycinamide ribonucleotide = N10-formyltetrahydrofolic acid + formylglycinamide ribonucleotide

485742

-

3.5.4.9

(6R,S)-5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate

743250

-

3.5.4.9

(6R,S)-methenyltetrahydrofolate + H2O = ?

209736, 209738

-

3.5.4.9

5,10-methenyl-tetrahydrofolate + H2O = 10-formyltetrahydrofolate + H+

701402

-

3.5.4.9

5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate

209738, 209721, 209731, 485728, 209737, 209729, 209739, 209742, 209728, 392333, 712483, 734262, 209719, 209740, 209734, 209736, 712988, 209732, 654529, 1505, 209725, 209727, 209722, 209726, 1518, 209720, 209730, 712978, 700281, 209741, 209718, 688323, 735050, 744335, 654797, 656050, 701402, 726831

-

3.5.4.9

5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate + ?

698187

-

3.5.4.9

5,10-methenyltetrahydrofolate + H2O = 5-formyltetrahydrofolate

654529

-

3.5.4.9

N5,N10-methenyltetrahydrofolate + H2O = N10-formyltetrahydrofolate

720406

-

3.5.4.9

7 entries

Product in Enzyme-catalyzed Reactions (26 results)

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Show Product (26 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.1.15

L-5,10-methylenetetrahydrofolate + NAD+ = 5,10-methenyl-tetrahydrofolate + NADH

0

-

1.5.1.15

5,10-methylenetetrahydrofolate + NAD+ = 5,10-methenyltetrahydrofolate + NADH

0

-

1.5.1.15

5,10-methylenetetrahydrofolate + NAD+ = 5,10-methenyltetrahydrofolate + NADH + H+

0

-

1.5.1.15

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH + H+

0

-

1.5.1.5

5,10-methylene tetrahydrofolate + NAD+ = 5,10-methenyl tetrahydrofolate + NADH + H+

0

-

1.5.1.5

5,10-methylene tetrahydrofolate + NADP+ = 5,10-methenyl tetrahydrofolate + NADPH

0

-

1.5.1.5

5,10-methylene tetrahydrofolate + NADP+ = 5,10-methenyl tetrahydrofolate + NADPH + H+

0

-

1.5.1.5

5,10-methylene-tetrahydrofolate + NAD+ = 5,10-methenyl-tetrahydrofolate + NADH

0

-

1.5.1.5

5,10-methylene-tetrahydrofolate + NADP+ = 5,10-methenyl-tetrahydrofolate + NADPH + H+

0

-

1.5.1.5

(6R,S)-5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH + H+

0

-

1.5.1.5

5,10-methylene tetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH

0

-

1.5.1.5

5,10-methylenetetrahydrofolate + NAD+ = 5,10-methenyltetrahydrofolate + NADH + H+

0

-

1.5.1.5

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH + H+

0, 392313, 392316, 392306, 392310, 392309

-

3.4.19.9

5,10-methenyltetrahydrofolate glutamate + H2O = 5,10-methenyltetrahydrofolate + L-glutamate

0

-

3.4.19.9

5,10-methenyltetrahydrofolate heptaglutamate + 7 H2O = 5,10-methenyltetrahydrofolate + 7 L-glutamate

0

-

3.4.19.9

5,10-methenyltetrahydrofolate hexaglutamate + 6 H2O = 5,10-methenyltetrahydrofolate + 6 L-glutamate

0

-

3.5.4.9

10-formyltetrahydrofolate = 5,10-methenyltetrahydrofolate + H2O

0

-

3.5.4.9

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH + H+

0

-

4.3.1.4

5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH3

0

-

4.3.1.4

5-formiminotetrahydrofolate = 5,10-methenyltetrahydrofolate + NH3

34325, 34328, 34326, 485770, 34313, 34314, 34315, 34316, 34318, 34319, 34320, 34312, 34317, 34311, 485769, 34322, 34323, 34321

-

6.3.3.2

ATP + (6R,S)-5-formyltetrahydrofolate = ADP + phosphate + 5,10-methenyltetrahydrofolate

0

-

6.3.3.2

ATP + (6S)-5-formyltetrahydrofolate = ADP + 5,10-methenyltetrahydrofolate + phosphate

0

-

6.3.3.2

ATP + 5-formyltetrahydrofolate = ADP + 5,10-methenyltetrahydrofolate + phosphate

0

-

6.3.3.2

ATP + 5-formyltetrahydrofolate = ADP + phosphate + 5,10-methenyltetrahydrofolate

652430, 0, 652260, 649293, 652326

-

6.3.3.2

CTP + 5-formyltetrahydrofolate = CDP + phosphate + 5,10-methenyltetrahydrofolate

0

-

6.3.3.2

UTP + 5-formyltetrahydrofolate = UDP + phosphate + 5,10-methenyltetrahydrofolate

0

-

1.5.1.15

4 entries

1.5.1.5

9 entries

3.4.19.9

3 entries

3.5.4.9

2 entries

4.3.1.4

2 entries

6.3.3.2

6 entries

Enzyme Cofactor/Cosubstrate (21 results)

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Show Cofactor (21 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.45

-

688294

-

2.1.2.11

dependent on

756787

-

2.1.2.2

-

172166

-

2.1.2.2

-

485714, 485716

-

2.1.2.2

-

485727

-

2.1.2.2

3 entries

2.1.2.8

-

757025

-

4.1.99.13

required

728529

-

4.1.99.3

-

702373, 693173, 694876, 690897, 694884, 692014, 727999, 748854

-

4.1.99.3

acts as a light-harvesting pigment

693836

-

4.1.99.3

an electron transfer pathway exists in DASH cryptochrome, where the 5,10-methenyltetrahydrofolate cofactor is photoreduced to 5,10-methylenetetrahydrofolate. Reduction requires the intact tryptophan triad. DASH cryptochrome forms 5,10-methylenetetrahydrofolate when treated with UV-A. Light-driven formation of 5,10-methylenetetrahydrofolate by DASH cryptochrome can be coupled with the formation of NADPH in the presence of 5,10-methylenetetrahydrofolate dehydrogenase

704520

-

4.1.99.3

an electron transfer pathway exists in photolyase, where the 5,10-methenyltetrahydrofolate cofactor is photoreduced to 5,10-methylenetetrahydrofolate. Reduction requires the intact tryptophan triad. Photolyase forms 5,10-methylenetetrahydrofolate when treated with UV-A. Light-driven formation of 5,10-methylenetetrahydrofolate by photolyase can be coupled with the formation of NADPH in the presence of 5,10-methylenetetrahydrofolate dehydrogenase

704520

-

4.1.99.3

antenna cofactor

702373

-

4.1.99.3

bound at the interface between N-terminal and C-terminal domain

703352

-

4.1.99.3

Cry3

703352

-

4.1.99.3

FAD and 5,10-methenyltetrahydrofolate act as chromophore and antenna molecules, respectively

728434

-

4.1.99.3

observed in the cleft between the two domains, where it interacts with two critical amino acid residues, Cys292 and Lys293

748854

-

4.1.99.3

-

678403, 703398, 706557, 704191

-

4.1.99.3

contains the chromophore methenyltetrahydrofolate

692023

-

4.1.99.3

is the solar panel or photoantenna of the enzyme

746749

-

4.1.99.3

MTHF, the molecule is bound as an antenna molecule and found in substoichiometric amounts

747724

-

4.1.99.3

the enzyme utilizes the the antenna cofactor to harvest light energy for the repair of thymine dimers in DNA. For this purpose, the enzyme evolved to bind the cofactor and red-shift its absorption maximum by 25 nm

664598

-

4.1.99.3

14 entries

Activator in Enzyme-catalyzed Reactions (3 results)

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Show Activating Compound (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

4.1.99.3

binds to the enzyme and acts as a light-harvesting pigment

727010

-

4.1.99.3

cofactor

33505, 33509

-

4.1.99.3

the enzyme contains 5,10-methenyltetrahydrofolic acid

33501

-

4.1.99.3

3 entries

Inhibitor in Enzyme-catalyzed Reactions (2 results)

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Show Inhibitors (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.5.1.53

-

760548

-

2.1.2.1

-

441407

-

3D Structure of Enzyme-Ligand-Complex (PDB) (1 result)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (1 entry)

EC NUMBER

ENZYME 3D STRUCTURE

1.12.98.2

6huy, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (21 results)

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Show Turnover Number (21 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.5.1.15

0.688

-

pH 7.6, 22°C

765009

1.5.1.15

1.58

-

-

392076

1.5.1.15

4.063

-

pH 7.6, 22°C

765009

1.5.1.5

0.01

-

pH 7.6, 30°C, mutant enzyme D121A

744335

1.5.1.5

0.06

-

pH 7.6, 30°C, mutant enzyme G122D

744335

1.5.1.5

2.6

-

pH 7.6, 30°C, mutant enzyme C58Y

744335

1.5.1.5

14.3

-

pH 7.6, 30°C, mutant enzyme K54S

744335

1.5.1.5

19.9

-

pH 7.6, 30°C, wild-type enzyme

744335

3.5.4.9

0.01

-

pH 7.6, 30°C, mutant enzyme D121A

744335

3.5.4.9

0.025

-

pH 7.6, 30°C, mutant enzyme G122D

744335

3.5.4.9

4.75

-

pH 7.6, 30°C, mutant enzyme C58Y

744335

3.5.4.9

40.9

-

pH 7.6, 30°C, wild-type enzyme

744335

3.5.4.9

57.4

-

pH 7.6, 30°C, mutant enzyme R191E

744335

3.5.4.9

107

-

forward reaction, recombinant mutant S197T

654797

3.5.4.9

118

-

forward reaction, recombinant mutant S197A

654797

3.5.4.9

123

-

forward reaction, recombinant mutant R173E

654797

3.5.4.9

128

-

forward reaction, recombinant mutant R173A

654797

3.5.4.9

134

-

forward reaction, recombinant wild-type enzyme

654797

3.5.4.9

141

-

forward reaction, recombinant mutant R173K

654797

3.5.4.9

177

-

forward reaction, recombinant mutant S197D

654797

3.5.4.9

185

-

forward reaction, recombinant mutant S197R

654797

1.5.1.15

3 entries

1.5.1.5

5 entries

3.5.4.9

13 entries

K_M Value (56 results)

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Show KM Value (56 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.5.1.15

0.03

-

-

392091

1.5.1.15

0.0632

-

pH 7.6, 22°C

765009

1.5.1.15

0.096

-

-

392091

1.5.1.15

0.145

-

pH 7.6, 22°C

765009

1.5.1.15

0.15

-

-

392078

1.5.1.15

0.155

-

-

392091

1.5.1.15

1

-

-

392076

1.5.1.5

0.068

-

pH 7.6, 30°C, mutant enzyme G122D

744335

1.5.1.5

0.104

-

pH 7.6, 30°C, mutant enzyme D121A

744335

1.5.1.5

0.205

-

pH 7.6, 30°C, mutant enzyme K54S

744335

1.5.1.5

0.279

-

pH 7.6, 30°C, wild-type enzyme

744335

1.5.1.5

0.302

-

pH 7.6, 30°C, mutant enzyme C58Y

744335

2.1.1.45

0.3

-

30fold higher than wild-type thymidylate synthase

692639

2.1.1.45

0.3

-

mutant K48Q

692639

2.1.2.2

0.00576

-

-

485714

2.1.2.2

0.058

-

-

485713

3.5.4.9

0.0045

-

pH 7.6, 30°C, mutant enzyme G122D

744335

3.5.4.9

0.009

-

pH 7.0, 23°C

654529

3.5.4.9

0.015

-

pH 7.6, 30°C, mutant enzyme D121A

744335

3.5.4.9

0.0164

-

-

209736

3.5.4.9

0.019

-

forward reaction, recombinant mutant S197D

654797

3.5.4.9

0.021

-

forward reaction, recombinant mutant R173A and R173K

654797

3.5.4.9

0.025

-

forward reaction, recombinant mutant S197T

654797

3.5.4.9

0.025

-

forward reaction, recombinant wild-type enzyme

654797

3.5.4.9

0.026

-

at pH 7.9 and 22°C

735050

3.5.4.9

0.026

-

pH 7.6, 30°C, wild-type enzyme

744335

3.5.4.9

0.026

-

forward reaction, recombinant mutant R173E

654797

3.5.4.9

0.028

-

pH 7.6, 30°C, mutant enzyme R191E

744335

3.5.4.9

0.031

-

-

209738

3.5.4.9

0.038

-

forward reaction, recombinant mutant S197A

654797

3.5.4.9

0.04

-

-

209728, 209729

3.5.4.9

0.04

-

pH 7.6, 30°C, mutant enzyme C58Y

744335

3.5.4.9

0.05

-

30°C, recombinant mutant R250A

656050

3.5.4.9

0.06

-

30°C, recombinant wild-type enzyme

656050

3.5.4.9

0.071

-

30°C, recombinant loop5G mutant

656050

3.5.4.9

0.072

-

30°C, recombinant mutant Y240A

656050

3.5.4.9

0.074

-

-

209729

3.5.4.9

0.075

-

-

209728

3.5.4.9

0.077

-

30°C, recombinant loop3G mutant

656050

3.5.4.9

0.08

-

-

209741

3.5.4.9

0.09

-

-

209722

3.5.4.9

0.13

-

-

209727

3.5.4.9

0.14

-

mutant K56R

209742

3.5.4.9

0.157

-

pH 7.6, temperature not specified in the publication

743250

3.5.4.9

0.19

-

-

209719

3.5.4.9

0.19

-

pH 7.2, 35°C

209721

3.5.4.9

0.23

-

forward reaction, recombinant mutant S197R

654797

3.5.4.9

0.25

-

-

209722, 209728, 1505

3.5.4.9

0.32

-

mutant S49Q

209742

3.5.4.9

0.34

-

wild-type DC301

209742

3.5.4.9

0.48

-

mutant Y52F

209742

3.5.4.9

0.52

-

mutant S49A

209742

3.5.4.9

0.56

-

mutants C147A, T148A

209742

3.5.4.9

1.22

-

mutant Y52A

209742

3.5.4.9

1.62

-

mutant Y52F

209742

3.5.4.9

2.36

-

mutant C147Q

209742

1.5.1.15

7 entries

1.5.1.5

5 entries

2.1.1.45

2 entries

2.1.2.2

2 entries

3.5.4.9

40 entries

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.1.2.1

3

-

-

441407

References & Links

Literature References (127)

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Show Reference (127 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

1505

6990198

Formyl-methenyl-methylenetetrahydrofolate synthetase (combined): a multifunctional protein in eukaryotic folate metabolism

1980

Paukert, J.L.; Rabinowitz, J.C.

Methods Enzymol.

66

616-626

1518

8304211

Enzymes for synthesis of 10-formyltetrahydrofolate in plants. Characterization of a monofunctional 10-formyltetrahydrofolate synthetase and copurification of 5,10-methylenetetrahydrofolate dehydrogenase and 5,10-methenyltetrahydrofolate cyclohydrolase activities

1993

Cossins, E.A.; Kirk, C.D.; Imeson, H.C.; Zheng, L.l.

Adv. Exp. Med. Biol.

338

707-710

33501

7938208

DNA photolyase from the fungus Neurospora crassa. Purification, characterization and comparison with other photolyases

1994

Eker, A.P.M.; Yajima, H.; Yasui, A.

Photochem. Photobiol.

60

125-133

33505

1840665

Cloning, sequencing, expression and characterization of DNA photolyase from Salmonella typhimurium

1991

Li, Y.F.; Sancar, A.

Nucleic Acids Res.

19

4885-4890

33509

8038161

Characterization of a medium wavelength type DNA photolyase: purification and properties of photolyase from Bacillus firmus

1994

Malhotra, K.; Kim, S.T.; Sancar, A.

Biochemistry

33

8712-8718

34311

-

Formimino-tetrahydrofolic acid and methenyltetrahydrofolic acid as intermediates in the formation of N10-formyltetrahydrofolic acid

1956

Rabinowitz, J.C.; Pricer, W.E.

J. Am. Chem. Soc.

78

5702-5704

34312

6016330

Metabolism of formiminoglycine. Formiminotetrahydrofolate cyclodeaminase

1967

Uyeda, K.; Rabinowitz, J.C.

J. Biol. Chem.

242

24-31

34313

4472378

The purification of formiminotransferase and cyclodeaminase by combination of affinity chromatography and isoelectric focusing

1974

Slavik, K.; Zizkovsky, V.; Slavikova, V.; Fort, P.

Biochem. Biophys. Res. Commun.

59

1173-1184

34314

241297

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

1975

Drury, E.J.; Bazar, L.S.; MacKenzie, R.E.

Arch. Biochem. Biophys.

169

662-668

34315

999878

Formiminotransferase cyclodeaminase from porcine liver. An octomeric enzyme containing bifunctional polypeptides

1976

Beaudet, R.; MacKenzie, R.E.

Biochim. Biophys. Acta

453

151-161

34316

561642

Formiminotransferase-cyclodeaminase from porcine liver. A sulfhydryl essential for the deaminase activity of the bifunctional enzyme

1977

Drury, E.J.; MacKenzie, R.E.

Can. J. Biochem.

55

919-923

34317

7374505

Formiminotransferase-cyclodeaminase: a bifunctional enzyme from porcine liver

1980

MacKenzie, R.E.

Methods Enzymol.

66

626-630

34318

7410436

The bifunctional enzyme formiminotransferase-cyclodeaminase is a tetramer of dimers

1980

MacKenzie, R.E.; Aldridge, M.; Paquin, J.

J. Biol. Chem.

255

9474-9478

34319

7350916

Tetrahydropterolypolyglutamate derivatives as substrates of two multifunctional proteins with folate-dependent enzyme activities

1980

MacKenzie, R.E.; Baugh, C.M.

Biochim. Biophys. Acta

611

187-195

34320

4066660

Channeling between the active sites of formiminotransferase-cyclodeaminase. Binding and kinetic studies

1985

Paquin, J.; Baugh, C.M.; MacKenzie, R.E.

J. Biol. Chem.

260

14925-14931

34321

-

Formimino-L-glutamate

1985

Cooperman, J.M.

Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )

8

514-521

34322

3593701

Dissociation of the octameric bifunctional enzyme formiminotransferase-cyclodeaminase in urea. Isolation of two monofunctional dimers

1987

Findlay, W.A.; MacKenzie, R.E.

Biochemistry

26

1948-1954

34323

3390440

Renaturation of formiminotransferase-cyclodeaminase from guanidine hydrochloride. Quaternary structure requirements for the activities and polyglutamate specificity

1988

Findlay, W.A.; MacKenzie, R.E.

Biochemistry

27

3404-3408

34325

9677386

A formiminotransferase cyclodeaminase isoform is localized to the Golgi complex and can mediate interaction of trans-Golgi network-derived vesicles with microtubules

1998

Hennig, D.; Scales, S.J.; Moreau, A.; Murley, L.L.; De Mey, J.; Kreis, T.E.

J. Biol. Chem.

273

19602-19611

34326

9837973

Molecular cloning, characterization, and dynamics of rat formiminotransferase cyclodeaminase, a Golgi-associated 58-kDa protein

1998

Gao, Y.S.; Alvarez, C.; Nelson, D.S.; Sztul, E.

J. Biol. Chem.

273

33825-33834

34328

10029623

Formiminotransferase cyclodeaminase is an organ-specific autoantigen recognized by sera of patients with autoimmune hepatitis

1999

Lapierre, P.; Hajoui, O.; Homberg, J.C.; Alvarez, F.

Gastroenterology

116

643-649

172166

7354066

Purification of a complex catalizing folate cofactor synthesis and transformylation in de novo purine biosynthesis

1980

Caperelli, C.A.; Benkovic, P.A.; Chettur, G.; Benkovic, S.J

J. Biol. Chem.

255

1885-1890

209718

3316188

Catabolic enzymes of the acetogen Butyribacterium methylotrophicum grown on single-carbon substrates

1987

Kerby, R.; Zeikus, J.G.

J. Bacteriol.

169

5605-5609

209719

3702702

Purification of 5,10-methenyltetrahydrofolate cyclohydrolase from Clostridium formicoaceticum

1986

Ljungdahl, L.G.; Clark, J.E.

Methods Enzymol.

122

385-391

209720

6806250

Levels of enzymes involved in the synthesis of acetate from CO2 in Clostridium thermoautotrophicum

1982

Clark, J.E.; Ragsdale, S.W.; Ljungdahl, L.G.; Wiegel, J.

J. Bacteriol.

151

507-509

209721

7061514

Purification and properties of 5,10-methenyltetrahydrofolate cyclohydrolase from Clostridium formicoaceticum

1982

Clark, J.E.; Ljungdahl, L.G.

J. Biol. Chem.

257

3833-3836

209722

-

5,10-Methenyltetrahydrofolate cyclohydrolase and 5-formyltetrahydrofolate cyclodehydrase in Aedes aegypti

1980

Jaffe, J.J.; Chrin, L.R.; Smith, R.B.

Comp. Biochem. Physiol. B

66

597-600

209725

476523

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

1979

Tan, L.U.L.; MacKenzie, R.E.

Can. J. Biochem.

57

806-812

209726

23838

Methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase from porcine liver. Interaction between the dehydrogenase and cyclohydrolase activities of the multifunctional enzyme

1978

Cohen, L.; MacKenzie, R.E.

Biochim. Biophys. Acta

522

311-317

209727

838698

Methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase. A multifunctional protein from porcine liver

1977

Tan, L.U.L.; Drury, E.J.; MacKenzie, R.E.

J. Biol. Chem.

252

1117-1122

209728

-

The occurrence and properties of methenyltetrahydrofolate cyclohydrolase in plants

1973

Suzuki, N.; Iwai, K.

Plant Cell Physiol.

14

319-327

209729

13672973

The enzymatic formation of formiminotetrahydrofolic acid, 5,10-methenyltetrahydrofolic acid, and 10-formyltetrahydrofolic acid in the metabolism of formiminoglutamic acid

1959

Tabor, H.; Wyngarden, L.

J. Biol. Chem.

234

1830-1846

209730

-

The enzymatic synthesis of N10-formyltetrahydrofolic acid and its role in ATP formation during formiminoglycine degradation

1956

Schnell, E.; Rochow, E.G.

J. Am. Chem. Soc.

78

4176-4178

209731

1748668

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

1991

D'Ari, L.; Rabinowitz, J.C.

J. Biol. Chem.

266

23953-23958

209732

1569082

The NADP-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase is not expressed in Spodoptera frugiperda cells

1992

Tremblay, G.B.; Mejia, N.R.; MacKenzie, R.E.

J. Biol. Chem.

267

8281-8285

209734

1392622

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

1992

Xiao-Ming, Y.; MacKenzie, R.E.

Protein Expr. Purif.

3

256-262

209736

8110794

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

1994

Pelletier, J.N.; MacKenzie, R.E.

Biochemistry

33

1900-1906

209737

-

A 5,10-methylenetetrahydrofolate dehydrogenase: 5,10-methenyltetrahydrofolate cyclohydrolase protein from Pisum sativum

1995

Kirk, C.D.; Chen, L.; Imeson, H.C.; Cossins, E.A.

Phytochemistry

39

1309-1317

209738

8765228

Methylenetetrahydrofolate dehydrogenase-cyclohydrolase from Photobacterium phosphoreum shares properties with a mammalian mitochondrial homologue

1996

Pawelek, P.D.; MacKenzie, R.E.

Biochim. Biophys. Acta

1296

47-54

209739

9061797

Purification, crystallization, and preliminary X-ray studies of a bifunctional 5,10-methenyl/methylene tetrahydrofolate cyclohydrolase/dehydrogenase from Escherichia coli

1997

Cheung, E.; D'Ari, L.; Rabinowitz, J.C.; Dyer, D.H.; Huang, J.Y.; Stoddard, B.L.

Proteins

27

322-324

209740

10386884

The crystal structure of a bacterial, bifunctional 5,10 methylene-tetrahydrofolate dehydrogenase/cyclohydrolase

1999

Shen, B.W.; Dyer, D.H.; Huang, J.Y.; D'Ari, L.; Rabinowitz, J.; Stoddard, B.L.

Protein Sci.

8

1342-1349

209741

10215859

A methenyl tetrahydromethanopterin cyclohydrolase and a methenyl tetrahydrofolate cyclohydrolase in Methylobacterium extorquens AM1

1999

Pomper, B.K.; Vorholt, J.A.; Chistoserdova, L.; Lidstrom, M.E.; Thauer, R.K.

Eur. J. Biochem.

261

475-480

209742

10828945

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

2000

Schmidt, A.; Wu, H.; MacKenzie, R.E.; Chen, V.J.; Bewly, J.R.; Ray, J.E.; Toth, J.E; Cygler, M.

Biochemistry

39

6325-6335

392075

4153026

Purification and characterisation of nicotinamide adenine dinucleotide-dependent methylenetetrahydrofolate dehydrogenase from Clostridium formicoaceticum

1974

Moore, M.R.; O'Brien, W.E.; Ljungdahl, L.G.

J. Biol. Chem.

249

5250-5253

392076

6608524

Purification and properties of NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from Acetobacterium woodii

1984

Ragsdale, S.W.; Ljungdahl, L.G.

J. Biol. Chem.

259

3499-3503

392077

3877056

NAD-dependent methylenetetrahydrofolate dehydrogenase is expressed by immortal cells

1985

Mejia, N.; Mackenzie, R.E.

J. Biol. Chem.

260

14616-14620

392078

3487546

NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase from ascites tumor cells. Purification and properties

1986

Mejia, N.; Rios-Orlandi, E.M.; Mackenzie, R.E.

J. Biol. Chem.

261

9509-9513

392079

3074630

Methylenetetrahydrofolate dehydrogenases in normal and transformed mammalian cells

1988

Mackenzie, R.E.; Mejia, N.; Yang, X.M.

Adv. Enzyme Regul.

27

31-39

392080

3261979

NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase in transformed cells is a mitochondrial enzyme

1988

Mejia, N.; Mackenzie, R.E.

Biochem. Biophys. Res. Commun.

155

1-6

392081

3258307

The activities of the NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase from ascites tumor cells are kinetically independent

1988

Rios-Orlandi, E.M.; Mackenzie, R.E.

J. Biol. Chem.

263

4662-4667

392082

2647744

Isolation and characterization of cDNA clones encoding the murine NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase

1989

Belanger, C.; Mackenzie, R.E.

J. Biol. Chem.

264

4837-4843

392083

2223762

Isolation and characterization of a novel eukaryotic monofunctional NAD+-dependent 5,10-methylenetetrahydrofolate dehydrogenase

1990

Barlowe, C.K.; Appling, D.R.

Biochemistry

29

7089-7094

392084

2275549

Activity of an NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase in normal tissue, neoplastic cells, and oncogene-transformed cells

1990

Smith, G.K.; Banks, S.D.; Monaco, T.J.; Rigual, R.; Duch, D.S.; Mullin, R.J.; Huber, B.E.

Arch. Biochem. Biophys.

283

367-371

392085

8424951

NAD(+)-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase: detection of the mRNA in normal murine tissues and transcriptional regulation of the gene in cell lines

1993

Peri, K.G.; Mackenzie, R.E.

Biochim. Biophys. Acta

1171

281-287

392086

8485162

The isolation and characterization of a Drosophila gene encoding a putative NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase

1993

Price, B.D.; Laughon, A.

Biochim. Biophys. Acta

1173

94-98

392087

8218174

NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is the mammalian homolog of the mitochondrial enzyme encoded by the yeast MIS1 gene

1993

Yang, X.M.; Mackenzie, R.E.

Biochemistry

32

11118-11123

392088

7615077

NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is targeted to the cytoplasm in insect cell lines

1995

Tremblay, G.B.; Sohi, S.S.; Retnakaran, A.; Mackenzie, R.E.

FEBS Lett.

368

177-182

392089

8990502

Crystallization of the NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from Saccharomyces cerevisiae

1996

Monzingo, A.F.; West, M.G.; Schelp, E.; Appling, D.R.; Robertus, J.D.

Proteins

26

481-482

392090

9250982

Monofunctional NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase from Saccharomyces cerevisiae

1997

Appling, D.R.; West, M.G.

Methods Enzymol.

281

178-188

392091

9250981

Mitochondrial NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase

1997

Mackenzie, R.E.

Methods Enzymol.

281

171-177

392092

12024029

Mitochondrial NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is essential for embryonic development

2002

Di Pietro, E.; Sirois, J.; Trenblay, M.L.; Mackenzie, R.E.

Mol. Cell. Biol.

22

4158-4166

392093

12061812

Mammalian mitochondrial methylenetetrahydrofolate dehydrogenase-cyclohydrolase

2002

Patel, H.; Christensen, K.E.; Mejia, N.; Mackenzie, R.E.

Arch. Biochem. Biophys.

403

145-148

392306

4384970

Methylenetetrahydrofolate dehydrogenase of the amethopterin-resistant strain Streptococcus faecium var. durans A and its repressibility by serine

1968

Albrecht, A.M.; Pearce, F.K.; Hutchinson, D.J.

J. Bacteriol.

95

1779-1789

392309

6966369

Methylenetetrahydrofolate dehydrogenase from Clostridium formicoaceticum and methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase (combined) from Clostridium thermoaceticum

1980

Ljungdahl, L.G.; O'Brien, W.E.; Moore, M.R.; Liu, M.T.

Methods Enzymol.

66

599-609

392310

4383631

Enzymes of clostridial purine fermentation. Methylenetetrahydrofolate dehydrogenase

1967

Uyeda, K.; Rabinowitz, J.C.

J. Biol. Chem.

242

4378-4385

392313

14490085

5,10-Methylenetetrahydrofolic dehydrogenase from bakers'yeast

1962

Ramasastri, B.V.; Blakley, R.L.

J. Biol. Chem.

237

1982-1988

392316

4379024

Purification and properties of N5, N10-Methylenetetra-hydrofolate dehydrogenase of calf thymus

1965

Yeh, Y.C.; Greenberg, D.M.

Biochim. Biophys. Acta

105

279-291

392333

9454603

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

1998

Pawelek, P.D.; MacKenzie, R.E.

Biochemistry

37

1109-1115

441407

16664855

Serine hydroxymethyltransferase from soybean root nodules

1986

Mitchell, M.K.; Reynolds, P.H.S.; Blevins, D.G.

Plant Physiol.

81

553-557

485713

13502326

Biosynthesis of the purines. XIX. 2-Amino-N-ribosylacetamide 5'-phosphate(glycinamide ribotide) transformylase

1957

Warren, L.; Buchanan, J.M.

J. Biol. Chem.

229

613-626

485714

7284307

L(-)-10-formyltetrahydrofolate is the cofactor for glycinamide ribonucleotide transformylase from chicken liver

1981

Smith, G.K.; Benkovic, P.A.; Benkovic, S.J.

Biochemistry

20

4034-4036

485716

666851

Purification of glycineamide ribonucleotide transformylase

1978

Caperelli, C.A.; Chettur, G.; Lin, L.Y.; Benkovic, S.J.

Biochem. Biophys. Res. Commun.

82

403-410

485718

2185839

Subcloning, characterization, and affinity labeling of Escherichia coli glycinamide ribonucleotide transformylase

1990

Inglese, J.; Johnson, D.L.; Shiau, A.; Smith, J.M.; Benkovic, S.J.

Biochemistry

29

1436-1443

485727

350869

N10-Formyltetrahydrofolate is the formyl donor for glycinamide ribonucleotide transformylase in Escherichia coli

1978

Dev, I.K.; Harvey, R.J.

J. Biol. Chem.

253

4242-4244

485728

7417406

Characterization of the enzyme complex involving the folate-requiring enzymes of de novo purine biosynthesis

1980

Smith, G.K.; Mueller, W.T.; Wasserman, G.F.; Taylor, W.D.; Benkovic, S.J.

Biochemistry

19

4313-4321

485742

13672969

Biosynthesis of the purines. XXVI. The Identification of the formyl donors of the transformylation reactions

1959

Hartman, S.C.; Buchanan, J.M.

J. Biol. Chem.

234

1812-1816

485769

7901203

The nucleotide sequence of porcine formiminotransferase cyclodeaminase. Expression and purification from Escherichia coli

1993

Murley, L.L.; Mejia, N.R.; MacKenzie, R.E.

J. Biol. Chem.

268

22820-22824

485770

9677387

58K, a microtubule-binding Golgi protein, is a formiminotransferase cyclodeaminase

1998

Bashour, A.M.; Bloom, G.S.

J. Biol. Chem.

273

19612-19617

649293

11292595

Ontogeny of hepatic enzymes involved in serine- and folate-dependent one-carbon metabolism in rabbits

2001

Thompson, H.R.; Jones, G.M.; Narkewicz, M.R.

Am. J. Physiol.

280

G873-G878

652260

11923304

Cloning and characterization of methenyltetrahydrofolate synthetase from Saccharomyces cerevisiae

2002

Holmes, W.B.; Appling, D.R.

J. Biol. Chem.

277

20205-20213

652326

12207015

Cloning and characterization of mitochondrial 5-formyltetrahydrofolate cycloligase from higher plants

2002

Roje, S.; Janave, M.T.; Ziemak, M.J.; Hanson, A.D.

J. Biol. Chem.

277

42748-42754

652430

12764149

Methenyltetrahydrofolate synthetase regulates folate turnover and accumulation

2003

Anguera, M.C.; Suh, J.R.; Ghandour, H.; Nasrallah, I.M.; Selhub, J.; Stover, P.J.

J. Biol. Chem.

278

29856-29862

654529

12793858

5,10-methenyltetrahydrofolate cyclohydrolase, rat liver and chemically catalysed formation of 5-formyltetrahydrofolate

2003

Baggott, J.E.; MacKenzie, R.E.

Biochem. J.

374

773-778

654797

11004530

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

2000

Pawelek, P.D.; Allaire, M.; Cygler, M.; MacKenzie, R.E.

Biochim. Biophys. Acta

1479

59-68

656050

11904299

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

2002

Sundararajan, S.; MacKenzie, R.E.

J. Biol. Chem.

277

18703-18709

657277

15358367

Over-expression in Escherichia coli, functional characterization and refolding of rat dimethylglycine dehydrogenase

2004

Brizio, C.; Brandsch, R.; Bufano, D.; Pochini, L.; Indiveri, C.; Barile, M.

Protein Expr. Purif.

37

434-442

664598

15300832

Preliminary characterization of light harvesting in E. coli DNA photolyase

2004

Henry, A.A.; Jimenez, R.; Hanway, D.; Romesberg, F.E.

ChemBioChem

5

1088-1094

678403

16938496

Reversible resolution of flavin and pterin cofactors of His-tagged Escherichia coli DNA photolyase

2006

Xu, L.; Zhang, D.; Mu, W.; van Berkel, W.J.; Luo, Z.

Biochim. Biophys. Acta

1764

1454-1461

688294

18072727

Design, synthesis, and biological evaluation of classical and nonclassical 2-amino-4-oxo-5-substituted-6-methylpyrrolo[3,2-d]pyrimidines as dual thymidylate synthase and dihydrofolate reductase inhibitors

2008

Gangjee, A.; Li, W.; Yang, J.; Kisliuk, R.L.

J. Med. Chem.

51

68-76

688323

18309272

Crystallization and preliminary X-ray diffraction analysis of 5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase from Thermoplasma acidophilum DSM 1728

2008

Kim, J.H.; Sung, M.W.; Lee, E.H.; Nam, K.H.; Hwang, K.Y.

J. Microbiol. Biotechnol.

18

283-286

690897

18771290

Purification and characterization of a type III photolyase from Caulobacter crescentus

2008

Oztuerk, N.; Kao, Y.T.; Selby, C.P.; Kavakli, I.H.; Partch, C.L.; Zhong, D.; Sancar, A.

Biochemistry

47

10255-10261

692014

18547877

Active DNA photolyase encoded by a baculovirus from the insect Chrysodeixis chalcites

2008

van Oers, M.M.; Lampen, M.H.; Bajek, M.I.; Vlak, J.M.; Eker, A.P.

DNA Repair

7

1309-1318

692023

17951115

Repair of UV damage in bacteria

2008

Goosen, N.; Moolenaar, G.F.

DNA Repair

7

353-379

692639

18403248

Role of an invariant lysine residue in folate binding on Escherichia coli thymidylate synthase: calorimetric and crystallographic analysis of the K48Q mutant

2008

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Int. J. Biochem. Cell Biol.

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