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Ligand N,N-dimethylglycine

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

creatinine degradation, glycine betaine biosynthesis, methionine metabolism

KEGG

Glycine, serine and threonine metabolism

MetaCyc

glycine betaine biosynthesis IV (from glycine), glycine betaine biosynthesis V (from glycine), glycine betaine degradation I, glycine betaine degradation II (mammalian), glycine betaine degradation III, glycine betaine degradation IV, L-methionine salvage from L-homocysteine, methanogenesis from glycine betaine more

Show all BRENDA pathways known for N,N-dimethylglycine

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (10 results)

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Show Natural Substrate (10 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.3.10

N,N-dimethylglycine + H2O + O2 = sarcosine + formaldehyde + H2O2

724807, 394961, 394957

-

1.5.8.4

N,N-dimethylglycine + 5,6,7,8-tetrahydrofolate + electron-transfer flavoprotein = sarcosine + 5,10-methylenetetrahydrofolate + reduced electron-transfer flavoprotein

742499

-

1.5.8.4

N,N-dimethylglycine + electron-transfer flavoprotein + H2O = sarcosine + formaldehyde + reduced electron-transfer flavoprotein

743378, 741817

-

1.5.8.4

N,N-dimethylglycine + FAD + H2O = sarcosine + formaldehyde + FADH2

742499

-

1.5.8.4

N,N-dimethylglycine + H2O + FAD = sarcosine + formaldehyde + FADH2

657277

-

1.5.8.4

N,N-dimethylglycine + tetrahydropteroylpentaglutamate + acceptor = sarcosine + 5,10-methylene tetrahydropteroylpentaglutamate + reduced acceptor

392496, 392500, 392516, 392520, 392497, 392501, 392524

-

2.1.1.157

S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + betaine

719715, 734643, 734671, 657578, 659145, 733736, 720836, 659286

-

2.1.1.157

S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + N,N,N-trimethylglycine

677087

-

1.5.8.4

5 entries

2.1.1.157

2 entries

2.1.1.161

S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + N,N,N-trimethylglycine

659286, 671647

-

2.1.1.162

S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + N,N,N-trimethylglycine

677087

-

In Vivo Product in Enzyme-catalyzed Reactions (12 results)

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Show Natural Product (12 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.251

glycine betaine + NADH + H+ + O2 = N,N-dimethylglycine + formaldehyde + NAD+ + H2O

0

-

1.14.13.251

glycine betaine + NADPH + H+ + O2 = N,N-dimethylglycine + formaldehyde + NADP+ + H2O

0

-

2.1.1.156

S-adenosyl-L-methionine + N-methylglycine = S-adenosyl-L-homocysteine + N,N-dimethylglycine

0

5him, 3D-view

2.1.1.156

S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine + N,N-dimethylglycine

0

5him, 3D-view

2.1.1.157

S-adenosyl-L-methionine + N-methylglycine = S-adenosyl-L-homocysteine + N,N-dimethylglycine

0

-

2.1.1.157

S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine + N,N-dimethylglycine

0

-

1.14.13.251

2 entries

2.1.1.156

2 entries

2.1.1.157

2 entries

2.1.1.162

S-adenosyl-L-methionine + N-methylglycine = S-adenosyl-L-homocysteine + N,N-dimethylglycine

0

-

2.1.1.376

glycine betaine + a [Co(I) glycine betaine-specific corrinoid protein] = N,N-dimethylglycine + a [methyl-Co(III) glycine betaine-specific corrinoid protein]

0

-

2.1.1.376

glycine betaine + cob(I)alamin = N,N-dimethylglycine + methyl-cob(III)alamin

0

-

2.1.1.376

glycine betaine + [Co(I) glycine betaine-specific corrinoid protein MV8465] = N,N-dimethylglycine + [methyl-Co(III) glycine betaine-specific corrinoid protein MV8465]

0

-

2.1.1.5

L-homocysteine + betaine = L-methionine + dimethylglycine

0

-

2.1.1.5

N,N,N-trimethylglycine + L-homocysteine = N,N-dimethylglycine + L-methionine

0

-

2.1.1.376

3 entries

2.1.1.5

2 entries

Substrate in Enzyme-catalyzed Reactions (22 results)

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Show Substrate (22 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.3.10

N,N-dimethylglycine + 5,6,7,8-tetrahydrofolate + O2 = sarcosine + 5,10-methylenetetrahydrofolate + H2O2

655336

-

1.5.3.10

N,N-dimethylglycine + H2O + O2 = sarcosine + formaldehyde + H2O2

672060, 724807, 394961, 394957, 698911, 655336

-

1.5.3.10

2 entries

1.5.7.3

N,N-dimethylglycine + 2 oxidized ferredoxin + H2O = sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+

763964

-

1.5.8.4

N,N-dimethylglycine + 5,6,7,8-tetrahydrofolate + electron-transfer flavoprotein = sarcosine + 5,10-methylenetetrahydrofolate + reduced electron-transfer flavoprotein

742499

-

1.5.8.4

N,N-dimethylglycine + acceptor + H2O = sarcosine + formaldehyde + reduced acceptor

687135, 390333, 392496, 392497, 392499, 392500, 392501, 392507, 392508, 392516, 392520, 392498

-

1.5.8.4

N,N-dimethylglycine + electron-transfer flavoprotein + H2O = sarcosine + formaldehyde + reduced electron-transfer flavoprotein

743378, 741817

-

1.5.8.4

N,N-dimethylglycine + electron-transfer flavoprotein + H2O = sarcosine + formaldehyde + reduced electron-transfer flavoprotein + H2O2

763963

-

1.5.8.4

N,N-dimethylglycine + FAD + H2O = sarcosine + formaldehyde + FADH2

742499

-

1.5.8.4

N,N-dimethylglycine + ferricenium + H2O = sarcosine + formaldehyde + ferrocene

742499

-

1.5.8.4

N,N-dimethylglycine + ferricenium hexafluorophosphate + H2O = sarcosine + formaldehyde + reduced ferricenium hexafluorophosphate

699373

-

1.5.8.4

N,N-dimethylglycine + H2O + FAD = sarcosine + formaldehyde + FADH2

657277

-

1.5.8.4

N,N-dimethylglycine + H2O + ferrocene = sarcosine + formaldehyde + ?

742499

-

1.5.8.4

N,N-dimethylglycine + H2O + oxidized 1-methoxy-5-methylphenazinium methylsulfate = sarcosine + formaldehyde + reduced 1-methoxy-5-methylphenazinium methylsulfate

657277

-

1.5.8.4

N,N-dimethylglycine + H2O + oxidized 2,6-dichlorophenolindophenol = sarcosine + formaldehyde + reduced 2,6-dichlorophenolindophenol

657277, 742499

-

1.5.8.4

N,N-dimethylglycine + oxidized ferricenium hexafluorophosphate + H2O = sarcosine + formaldehyde + reduced ferricenium hexafluorophosphate + H2O2

741817

-

1.5.8.4

N,N-dimethylglycine + tetrahydropteroylpentaglutamate + acceptor = sarcosine + 5,10-methylene tetrahydropteroylpentaglutamate + reduced acceptor

392496, 392500, 392516, 392520, 392497, 392501, 392524

-

2.1.1.157

S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + betaine

719715, 689964, 734643, 734671, 657578, 659145, 733736, 720836, 659286

-

2.1.1.157

S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + betaine + H+

695924

-

2.1.1.157

S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + N,N,N-trimethylglycine

677087

-

1.5.8.4

13 entries

2.1.1.157

3 entries

2.1.1.161

S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + N,N,N-trimethylglycine

659286, 671647

-

2.1.1.162

S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + betaine

758064, 677087

-

2.1.1.162

S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + N,N,N-trimethylglycine

677087

-

2.1.1.162

2 entries

Product in Enzyme-catalyzed Reactions (18 results)

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Show Product (18 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.251

glycine betaine + NADH + H+ + O2 = N,N-dimethylglycine + formaldehyde + NAD+ + H2O

0

-

1.14.13.251

glycine betaine + NADPH + H+ + O2 = N,N-dimethylglycine + formaldehyde + NADP+ + H2O

0

-

1.14.13.251

2 entries

2.1.1.10

betaine + L-homocysteine = dimethylglycine + L-methionine

0

-

2.1.1.156

2 S-adenosyl-L-methionine + glycine = 2 S-adenosyl-L-homocysteine + N,N-dimethylglycine

0

5him, 3D-view

2.1.1.156

S-adenosyl-L-methionine + N-methylglycine = S-adenosyl-L-homocysteine + N,N-dimethylglycine

0

5him, 3D-view

2.1.1.156

S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine + N,N-dimethylglycine

0

5him, 3D-view

2.1.1.157

S-adenosyl-L-methionine + N-methylglycine = S-adenosyl-L-homocysteine + N,N-dimethylglycine

0

-

2.1.1.157

S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine + N,N-dimethylglycine

0

-

2.1.1.162

S-adenosyl-L-methionine + N-methylglycine = S-adenosyl-L-homocysteine + N,N-dimethylglycine

0

-

2.1.1.162

S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine + N,N-dimethylglycine

0

-

2.1.1.156

3 entries

2.1.1.157

2 entries

2.1.1.162

2 entries

2.1.1.250

glycine betaine + cob(I)alamin = dimethylglycine + methylcob(III)alamin

0

-

2.1.1.376

glycine betaine + a [Co(I) glycine betaine-specific corrinoid protein] = N,N-dimethylglycine + a [methyl-Co(III) glycine betaine-specific corrinoid protein]

0

-

2.1.1.376

glycine betaine + cob(I)alamin = N,N-dimethylglycine + methyl-cob(III)alamin

0

-

2.1.1.376

glycine betaine + [Co(I) glycine betaine-specific corrinoid protein MV8465] = N,N-dimethylglycine + [methyl-Co(III) glycine betaine-specific corrinoid protein MV8465]

0

-

2.1.1.5

betaine + DL-homocysteine = dimethylglycine + L-methionine

0

-

2.1.1.5

L-homocysteine + betaine = dimethylglycine + L-methionine

0

-

2.1.1.5

L-homocysteine + betaine = L-methionine + dimethylglycine

0

-

2.1.1.5

N,N,N-trimethylglycine + L-homocysteine = N,N-dimethylglycine + L-methionine

441232, 441234, 441233, 441235, 441236, 441237, 0

-

2.1.1.376

3 entries

2.1.1.5

4 entries

Inhibitor in Enzyme-catalyzed Reactions (10 results)

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Show Inhibitors (10 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.17

-

654371

-

1.1.99.1

slight

389887

-

1.2.1.8

1 mM, 24% inhibition

390329

-

2.1.1.156

versus glycine, 65% inhibition at 250 mM

659286

5him, 3D-view

2.1.1.156

-

659286

5him, 3D-view

2.1.1.156

recombinant enzyme: poor competitive product inhibition, 50% inhibition at 38 mM with glycine, and at 49 mM with sarcosine

657578

5him, 3D-view

2.1.1.156

3 entries

2.1.1.157

competitive inhibition, versus sarcosine, 40% inhibition at 250 mM

659286

-

2.1.1.5

at 0.2 mM: 80% inhibition, at 2 mM: 97% inhibition; weak inhibitor, at 2 mM: 11% inhibition

687808

-

2.1.1.5

at 0.25 mM: 64% inhibition, at 2.5 mM: 95% inhibition; weak inhibitor, at 2.5 mM: 19% inhibition

687808

-

2.1.1.5

70% inhibition at 5 mM

441247

-

2.1.1.5

3 entries

3D Structure of Enzyme-Ligand-Complex (PDB) (8 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (8 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.5.3.1

1el5, 3D-view

1.5.3.1

1vrq, 3D-view

1.5.3.1

1x31, 3D-view

1.5.3.1

1el5, 3D-view

1.5.3.1

1vrq, 3D-view

1.5.3.1

1x31, 3D-view

1.5.3.1

6 entries

2.1.1.156

5him, 3D-view

2.1.1.244

5cvd, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (23 results)

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Show Turnover Number (23 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.5.3.10

0.047

-

mutant Y259F

655336

1.5.3.10

0.047

-

mutant Y259F, pH 8.5, 25°C

672060

1.5.3.10

4.35

-

mutant H225Q

655336

1.5.3.10

10.6

-

wild-type enzyme

655336

1.5.3.10

10.6

-

wild-type, pH 8.5, 25°C

672060

1.5.3.10

13.6

-

mutant H225Q, pH 8.5, 25°C

672060

1.5.3.10

14.3

-

-

394957

1.5.3.10

7 entries

1.5.7.3

0.31

-

pH 7.5, 60°C

763964

1.5.8.4

0.01

-

mutant H109R, pH 7.5, 25°C

699373

1.5.8.4

0.14

-

-

392496

1.5.8.4

0.225

-

wild-type, presence of tetrahydrofolate, pH 7.5, 25°C

699373

1.5.8.4

0.3

-

wild-type, pH 7.5, 25°C

699373

1.5.8.4

0.32

-

pH 7.5, 60°C

763963

1.5.8.4

0.73

-

wild type enzyme, with 2,6-dichlorophenolindophenol as cosubstrate, at 25°C and pH 7.8 in 50 mM HEPES/NaOH with 150 mM NaCl

742499

1.5.8.4

0.733

-

25°C, pH 7.8, artificial electron acceptor: 2,6-dichlorophenolindophenol, wild-type enzyme

742499

1.5.8.4

1.5

-

25°C, pH 7.8, artificial electron acceptor: 2,6-dichlorophenolindophenol, mutant enzyme H109R

742499

1.5.8.4

1.52

-

mutant enzyme H109R, with 2,6-dichlorophenolindophenol as cosubstrate, at 25°C and pH 7.8 in 50 mM HEPES/NaOH with 150 mM NaCl

742499

1.5.8.4

3.55

-

25°C, pH 7.8, artificial electron acceptor: ferrocene, wild-type enzyme

742499

1.5.8.4

3.55

-

wild type enzyme, with ferrocene as cosubstrate, at 25°C and pH 7.8 in 50 mM HEPES/NaOH with 150 mM NaCl

742499

1.5.8.4

9.07

-

mutant enzyme H109R, with ferrocene as cosubstrate, at 25°C and pH 7.8 in 50 mM HEPES/NaOH with 150 mM NaCl

742499

1.5.8.4

9.1

-

25°C, pH 7.8, artificial electron acceptor: ferrocene, mutant enzyme H109R

742499

2.1.1.157

1.4

-

-

689964

2.1.1.157

2.68

-

pH 7.2, 37°C

695924

1.5.8.4

13 entries

2.1.1.157

2 entries

K_M Value (39 results)

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Show KM Value (39 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.5.3.10

1.39

-

DMGO1, pH 9.0, temperature not specified in the publication

724807

1.5.3.10

1.86

-

DMGO2, pH 9.0, temperature not specified in the publication

724807

1.5.3.10

2

-

-

394957

1.5.3.10

2.4

-

wild-type enzyme

655336

1.5.3.10

2.4

-

wild-type, pH 8.5, 25°C

672060

1.5.3.10

9.1

-

-

394961

1.5.3.10

47

-

mutant Y259F

655336

1.5.3.10

47

-

mutant Y259F, pH 8.5, 25°C

672060

1.5.3.10

59

-

mutant H225Q

655336

1.5.3.10

142

-

mutant H225Q, pH 8.5, 25°C

672060

1.5.3.10

10 entries

1.5.7.3

8.61

-

pH 7.5, 60°C

763964

1.5.8.4

0.039

-

and second value 15.4 mM, wild-type, pH 7.5, 25°C

699373

1.5.8.4

0.045

-

and second value 1.10 mM, wild-type, presence of tetrahydrofolate, pH 7.5, 25°C

699373

1.5.8.4

0.05

-

-

392496

1.5.8.4

0.05

-

pH 7.0, 30°C, recombinant holoenzyme, 2 Km-values

657277

1.5.8.4

0.3

-

25°C, pH 7.8, artificial electron acceptor: 2,6-dichlorophenolindophenol, wild-type enzyme

742499

1.5.8.4

0.3

-

wild type enzyme, with 2,6-dichlorophenolindophenol as cosubstrate, at 25°C and pH 7.8 in 50 mM HEPES/NaOH with 150 mM NaCl

742499

1.5.8.4

1.1

-

and first value 0.045 mM, wild-type, presence of tetrahydrofolate, pH 7.5, 25°C

699373

1.5.8.4

1.4

-

25°C, pH 7.8, artificial electron acceptor: ferrocene, wild-type enzyme

742499

1.5.8.4

1.4

-

wild type enzyme, with ferrocene as cosubstrate, at 25°C and pH 7.8 in 50 mM HEPES/NaOH with 150 mM NaCl

742499

1.5.8.4

2.5

5

mutant H109R, pH 7.5, 25°C

699373

1.5.8.4

4.7

-

25°C, pH 7.8, artificial electron acceptor: 2,6-dichlorophenolindophenol, mutant enzyme H109R

742499

1.5.8.4

4.7

-

mutant enzyme H109R, with 2,6-dichlorophenolindophenol as cosubstrate, at 25°C and pH 7.8 in 50 mM HEPES/NaOH with 150 mM NaCl

742499

1.5.8.4

8.6

-

pH 7.5, 60°C

763963

1.5.8.4

9.4

-

pH 7.0, 30°C, recombinant holoenzyme, 2 Km-values

657277

1.5.8.4

15.4

-

and first value 0.039 mM, wild-type, pH 7.5, 25°C

699373

1.5.8.4

32.2

-

25°C, pH 7.8, artificial electron acceptor: ferrocene, mutant enzyme H109R

742499

1.5.8.4

32.2

-

mutant enzyme H109R, with ferrocene as cosubstrate, at 25°C and pH 7.8 in 50 mM HEPES/NaOH with 150 mM NaCl

742499

2.1.1.157

0.5

-

pH 8.8, 37°C, recombinant wild-type enzyme

659286

2.1.1.157

2.8

-

-

689964

2.1.1.157

3.76

-

pH 7.2, 37°C

695924

2.1.1.157

3.76

-

pH 7.3, 37°C, recombinant enzyme

720836

2.1.1.157

4.9

-

recombinant enzyme, pH 7.4, 37°C, with S-adenosyl-L-methionine

657578

2.1.1.157

7.5

-

pH 8.8, 37°C, recombinant mutant P171Q

659286

2.1.1.161

0.5

-

pH 8.8, 37°C

659286

2.1.1.161

2.11

-

pH 8.2, 37°C

671647

2.1.1.162

1.1

-

wild-type, pH 8.0, 25°C

758064

2.1.1.162

1.2

-

truncation mutant carrying the C-terminal part, pH 8.0, 25°C

758064

2.1.1.162

2.45

-

pH 7.2, 37°C

677087

1.5.8.4

17 entries

2.1.1.157

6 entries

2.1.1.161

2 entries

2.1.1.162

3 entries

K_i Value (2 results)

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Show KI Value (2 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.3.17

57

-

pH 8.0, 25°C

654371

1.2.1.8

130

-

-

390329

References & Links

Literature References (50)

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Show Reference (50 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

389887

-

Characterization of choline dehydrogenase from Pseudomonas aeruginosa A-16

1976

Nagasawa, T.; Mori, N.; Tani, Y.; Ogata, K.

Agric. Biol. Chem.

40

2077-2084

390329

2194570

Purification and characterization of osmoregulatory betaine aldehyde dehydrogenase of Escherichia coli

1990

Falkenberg, P.; Strom, A.R.

Biochim. Biophys. Acta

1034

253-259

390333

3290197

Osmotic control of glycine betaine biosynthesis and degradation in Rhizobium meliloti

1988

Smith, L.T.; Pocard, J.A.; Bernard, T.; LeRudulier, D.

J. Bacteriol.

170

3142-3149

392496

2417560

Enzymatic properties of dimethylglycine dehydrogenase and sarcosine dehydrogenase from rat liver

1985

Porter, D.H.; Cook, R.J.; Wagner, C.

Arch. Biochem. Biophys.

243

396-407

392497

4055729

The amino acid sequences of the flavin-peptides of dimethylglycine dehydrogenase and sarcosine dehydrogenase from rat liver mitochondria

1985

Cook, R.J.; Misono, K.S.; Wagner, C.

J. Biol. Chem.

260

12998-13002

392498

6180732

The effect of tetrahydrofolate on the reduction of electron transfer flavoprotein by sarcosine and dimethylglycine dehydrogenases

1982

Steenkamp, D.J.; Husain, M.

Biochem. J.

203

707-715

392499

6163778

Identification of the folate-binding proteins of rat liver mitochondria as dimethylglycine dehydrogenase and sarcosine dehydrogenase. Flavoprotein nature and enzymatic properties of the purified proteins

1981

Wittwer, A.J.; Wagner, C.

J. Biol. Chem.

256

4109-4115

392500

6163777

Identification of the folate-binding proteins of rat liver mitochondria as dimethylglycine dehydrogenase and sarcosine dehydrogenase. Purification and folate-binding characteristics

1981

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