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Ligand sarcosine

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

creatinine degradation, glycine betaine biosynthesis

KEGG

Arginine and proline metabolism, Glycine, serine and threonine metabolism

MetaCyc

creatinine degradation I, creatinine degradation II, 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, glyphosate degradation III more

Show all BRENDA pathways known for sarcosine

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Roles as Enzyme Ligand

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

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Show Natural Substrate (16 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.21.4.3

N-methylglycine + phosphate + thioredoxin = acetyl phosphate + methylamine + thioredoxin disulfide

636282, 636281, 636280

-

1.4.3.19

sarcosine + H2O + O2 = ?

725913

-

1.4.3.19

sarcosine + H2O + O2 = glyoxylate + methylamine + H2O2

672771

-

1.5.3.1

sarcosine + 5,6,7,8-tetrahydrofolate + O2 = glycine + formaldehyde + H2O2

764062, 764119, 764037

3qse, 3D-view

1.5.3.1

sarcosine + H2O + O2 = ?

392390, 392393, 392380, 392376

3qse, 3D-view

1.5.3.1

sarcosine + H2O + O2 = glycine + formaldehyde + H2O2

724775, 725124, 724937, 764086, 764208, 742088, 742299, 742678

3qse, 3D-view

1.5.3.1

sarcosine + H2O2 + O2 = glycine + formaldehyde + H2O2

741596

3qse, 3D-view

1.5.3.1

sarcosine + O2 + H2O = formaldehyde + glycine + H2O2

685282, 687443, 685219

3qse, 3D-view

1.4.3.19

2 entries

1.5.3.1

5 entries

1.5.3.24

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

765237, 765016, 765017, 765018, 765019, 765024, 765025, 765026, 765738, 765715, 764120, 764122, 764123, 764124, 764129, 764125

-

1.5.8.3

sarcosine + acceptor + H2O = glycine + formaldehyde + reduced acceptor

392511, 390333, 392509, 392494, 392496, 392497, 392499, 392500, 392501, 392506, 392507, 392508, 392498, 389889, 392505, 172080, 289023, 392502, 392510

-

1.5.8.3

sarcosine + H2O + electron-transfer flavoprotein = glycine + formaldehyde + reduced electron-transfer flavoprotein

725421, 742694, 743612, 743719

-

2.1.1.156

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

659286, 671647

5hil, 3D-view

2.1.1.156

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

719715, 734671, 657578, 659145, 659286, 733736, 720836, 734932

5hil, 3D-view

2.1.1.157

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

677087

-

2.1.1.157

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

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

-

1.5.8.3

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

677087

-

In Vivo Product in Enzyme-catalyzed Reactions (13 results)

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Show Natural Product (13 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

0, 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

0

-

1.5.8.4

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

0

-

1.5.8.4

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

0

-

1.5.8.4

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

0

-

1.5.8.4

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

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

-

2.1.1.156

S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + N-methylglycine

0

5hil, 3D-view

2.1.1.156

S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine

0

5hil, 3D-view

1.5.8.4

5 entries

2.1.1.156

2 entries

2.1.1.162

S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + N-methylglycine

0

-

2.1.1.20

S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + N-methylglycine

0

-

2.1.1.20

S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine

0

-

2.1.1.20

2 entries

3.5.1.59

N-carbamoylsarcosine + H2O = sarcosine + CO2 + NH3

209210, 209212, 209207

-

3.5.3.3

creatine + H2O = sarcosine + urea

0

-

Substrate in Enzyme-catalyzed Reactions (43 results)

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Show Substrate (43 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.21.4.3

N-methylglycine + phosphate + dithioerythritol = acetyl phosphate + methylamine + dithioerythritol disulfide

636280

-

1.21.4.3

N-methylglycine + phosphate + thioredoxin = acetyl phosphate + methylamine + thioredoxin disulfide

636282, 636280, 636281

-

1.4.3.19

sarcosine + H2O + O2 = ?

742365, 743136, 725913

-

1.4.3.19

sarcosine + H2O + O2 = glyoxylate + methylamine + H2O2

440361, 440362, 655429, 672771, 685414, 689934, 701114, 656226, 687878, 696494, 698957, 742488, 742686

-

1.5.3.1

sarcosine + 5,6,7,8-tetrahydrofolate + O2 = glycine + formaldehyde + H2O2

764062, 764119, 764037

3qse, 3D-view

1.5.3.1

sarcosine + H2O + 2,6-dichlorophenolindophenol = glycine + formaldehyde + reduced 2,6-dichlorophenolindophenol

392382

3qse, 3D-view

1.5.3.1

sarcosine + H2O + O2 = ?

392390, 392393, 392380, 392376

3qse, 3D-view

1.5.3.1

sarcosine + H2O + O2 = glycine + formaldehyde + H2O2

654459, 672027, 672210, 724775, 743119, 725124, 724937, 742952, 671547, 743892, 764086, 764208, 742088, 741596, 742299, 742678, 743178, 765378, 742252, 742971

3qse, 3D-view

1.5.3.1

sarcosine + H2O + phenazine methosulfate = glycine + formaldehyde + reduced phenazine methosulfate

392382

3qse, 3D-view

1.5.3.1

sarcosine + H2O + potassium ferricyanide = glycine + formaldehyde + potassium ferrocyanide

392382

3qse, 3D-view

1.5.3.1

sarcosine + H2O2 + O2 = glycine + formaldehyde + H2O2

741596

3qse, 3D-view

1.5.3.1

sarcosine + O2 + H2O = formaldehyde + glycine + H2O2

685282, 687443, 685219, 765379

3qse, 3D-view

1.5.3.1

sarcosine + O2 + H2O = glycine + formaldehyde + H2O2

392398, 392390, 392385, 392381, 392382, 392383, 392386, 392387, 392388, 392389, 392391, 392378, 392380, 392376, 392377, 392379, 392384

3qse, 3D-view

1.21.4.3

2 entries

1.4.3.19

2 entries

1.5.3.1

9 entries

1.5.3.19

sarcosine + O2 + H2O = glycine + formaldehyde + H2O2

719401

-

1.5.3.20

sarcosine + H2O + O2 = methylamine + glyoxalate + H2O2

762741

-

1.5.3.24

sarcosine + 5,6,7,8-tetrahydrofolate + 2,6-dichlorophenolindophenol = ?

765024

-

1.5.3.24

sarcosine + 5,6,7,8-tetrahydrofolate + ferricyanide = ?

765024

-

1.5.3.24

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

765237, 765016, 765017, 765018, 765019, 765024, 765025, 765026, 765738, 765715, 764120, 764121, 764122, 764123, 764124, 764129, 764125

-

1.5.3.24

sarcosine + 5,6,7,8-tetrahydrofolate + phenazine methosulfate = ?

765024

-

1.5.3.24

sarcosine + 5-formyltetrahydrofolate + O2 = ?

764121

-

1.5.3.24

sarcosine + pteroyltetraglutamate + O2 = ?

764121

-

1.5.3.24

sarcosine + tetrahydropteroyltetraglutamate + O2 = ?

764121

-

1.5.3.24

7 entries

1.5.7.3

sarcosine + 2 oxidized ferredoxin + H2O = glycine + formaldehyde + 2 reduced ferredoxin + 2 H+

763964

-

1.5.8.3

N-methylglycine + acceptor + H2O = glycine + formaldehyde + reduced acceptor

392502

-

1.5.8.3

sarcosine + acceptor + H2O = glycine + formaldehyde + reduced acceptor

392511, 390333, 392509, 392494, 392496, 392497, 392499, 392500, 392501, 392506, 392507, 392508, 392498, 389889, 392505, 172080, 289023, 392502, 392510

-

1.5.8.3

sarcosine + H2O + electron-transfer flavoprotein = glycine + formaldehyde + reduced electron-transfer flavoprotein

725421, 742694, 743612, 743719

-

1.5.8.3

sarcosine + H2O + phenazine methosulfate = glycine + formaldehyde + reduced phenazine methosulfate

392502

-

1.5.8.3

sarcosine + H2O + potassium ferricyanide = glycine + formaldehyde + potassium ferrocyanide

392502

-

1.5.8.3

sarcosine + oxidized 1-methoxy-5-methylphenazinium methylsulfate = glycine + formaldehyde + reduced 1-methoxy-5-methylphenazinium methylsulfate

655081

-

1.5.8.4

sarcosine + acceptor + H2O = glycine + formaldehyde + reduced acceptor

392499

-

1.5.8.4

sarcosine + electron-transfer flavoprotein + H2O = glycine + formaldehyde + reduced electron-transfer flavoprotein + H2O2

763963

-

1.5.99.5

N-methyl-glycine + 2,6-dichlorophenolindophenol + H2O = glycine + formaldehyde + reduced 2,6-dichlorophenolindophenol

437743

-

1.5.99.5

sarcosine + 2,6-dichlorophenolindophenol + H2O = aminoacetate + formaldehyde + reduced 2,6-dichlorophenolindophenol

437743, 437744, 437748, 437745, 437747

-

1.5.8.3

6 entries

1.5.8.4

2 entries

1.5.99.5

2 entries

1.5.99.B2

sarcosine + acceptor + H2O = ? + reduced acceptor

686651

-

2.1.1.156

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

659286, 671647

5hil, 3D-view

2.1.1.156

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

719715, 734671, 657578, 659145, 659286, 733736, 720836, 734932

5hil, 3D-view

2.1.1.157

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

677087

-

2.1.1.157

2 S-adenosyl-L-methionine + sarcosine = 2 S-adenosyl-L-homocysteine + betaine

659145

-

2.1.1.157

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

719715, 689964, 734643, 734671, 657578, 659145, 659286, 733736, 720836, 695924

-

2.1.1.162

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

677087

-

2.1.1.162

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

758064, 677087

-

2.1.1.156

2 entries

2.1.1.157

3 entries

2.1.1.162

2 entries

6.1.1.15

ATP + N-methylglycine + tRNAPro = ?

174

-

6.3.4.13

ATP + 5-phosphoribosylamine + sarcosine = ?

1412

-

Product in Enzyme-catalyzed Reactions (28 results)

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Show Product (28 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.1.25

glyocylate + methylamine + NADPH + H+ = sarcosine + NADP+

0

-

1.5.3.10

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

0

-

1.5.3.10

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

0, 394961, 394957

-

1.5.3.10

2 entries

1.5.7.3

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

0

-

1.5.8.4

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

0

-

1.5.8.4

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

0, 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

0

-

1.5.8.4

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

0

-

1.5.8.4

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

0

-

1.5.8.4

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

0

-

1.5.8.4

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

0

-

1.5.8.4

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

0

-

1.5.8.4

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

0

-

1.5.8.4

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

0

-

1.5.8.4

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

0

-

1.5.8.4

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

0

-

1.5.8.4

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

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

-

2.1.1.156

S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + N-methylglycine

0

5hil, 3D-view

2.1.1.156

S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine

0

5hil, 3D-view

1.5.8.4

13 entries

2.1.1.156

2 entries

2.1.1.157

S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine

0

-

2.1.1.162

S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + N-methylglycine

0

-

2.1.1.162

S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine

0

-

2.1.1.20

S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + N-methylglycine

0

-

2.1.1.20

S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine

0, 485214, 485215, 485216, 485217, 485218, 485213, 485212

-

3.5.1.24

3alpha,7alpha-dihydroxy-5beta-cholanoylsarcosine + H2O = 3alpha,7alpha-dihydroxy-5beta-cholanate + sarcosine

0

-

3.5.1.24

cholylsarcosine + H2O = cholic acid + sarcosine

0

-

2.1.1.162

2 entries

2.1.1.20

2 entries

3.5.1.24

2 entries

3.5.1.59

N-carbamoylsarcosine + H2O = sarcosine + CO2 + NH3

0, 209208, 209211, 209213, 209207, 209210, 209212

-

3.5.3.3

creatine + H2O = sarcosine + urea

209210, 288979, 288984, 209434, 288980, 288985, 288989, 288990, 288992, 288994, 288995, 288996, 288981, 392380, 288982, 288986, 288977, 288978, 288991, 288983, 288993, 0

-

Inhibitor in Enzyme-catalyzed Reactions (11 results)

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Show Inhibitors (11 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.17

-

654371

-

1.2.1.8

1 mM, 24% inhibition

390329

-

2.1.1.156

competitive inhibition, versus glycine, 70% inhibition at 250 mM

659286

5hil, 3D-view

2.1.1.157

slight competitive inhibition, versus dimethylglycine, 20% inhibition at 250 mM

659286

-

2.1.1.161

slight inhibition

659286

-

2.1.1.20

weak

485212

-

3.5.3.3

-

288985, 288993

-

5.1.1.4

-

2122

-

5.1.1.8

-

2158, 2159

-

6.1.1.15

-

174

-

6.1.1.15

weak

174

-

6.1.1.15

2 entries

3D Structure of Enzyme-Ligand-Complex (PDB) (196 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (196 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.5.3.1

3qse, 3D-view

2.1.1.156

5hil, 3D-view

2.1.1.244

6kdq, 3D-view

2.1.1.299

6kds, 3D-view

3.1.3.16

1m63, 3D-view

3.1.3.16

1mf8, 3D-view

3.1.3.16

1m63, 3D-view

3.1.3.16

1mf8, 3D-view

3.1.3.16

1m63, 3D-view

3.1.3.16

1mf8, 3D-view

3.1.3.16

1m63, 3D-view

3.1.3.16

1mf8, 3D-view

3.1.3.16

1m63, 3D-view

3.1.3.16

1mf8, 3D-view

3.1.3.16

10 entries

3.4.21.4

3t26, 3D-view

3.4.24.27

3t2i, 3D-view

5.2.1.8

1bck, 3D-view

5.2.1.8

1c5f, 3D-view

5.2.1.8

1cwa, 3D-view

5.2.1.8

1cwb, 3D-view

5.2.1.8

1cwc, 3D-view

5.2.1.8

1cwf, 3D-view

5.2.1.8

1cwl, 3D-view

5.2.1.8

1cwm, 3D-view

5.2.1.8

1cwo, 3D-view

5.2.1.8

1cyn, 3D-view

5.2.1.8

1m63, 3D-view

5.2.1.8

1mf8, 3D-view

5.2.1.8

1mik, 3D-view

5.2.1.8

1qng, 3D-view

5.2.1.8

1qnh, 3D-view

5.2.1.8

1xq7, 3D-view

5.2.1.8

2esl, 3D-view

5.2.1.8

2oju, 3D-view

5.2.1.8

2rma, 3D-view

5.2.1.8

2rmb, 3D-view

5.2.1.8

2rmc, 3D-view

5.2.1.8

2wfj, 3D-view

5.2.1.8

2x2c, 3D-view

5.2.1.8

2x7k, 3D-view

5.2.1.8

2z6w, 3D-view

5.2.1.8

3cys, 3D-view

5.2.1.8

3eov, 3D-view

5.2.1.8

3odi, 3D-view

5.2.1.8

3odl, 3D-view

5.2.1.8

3pmp, 3D-view

5.2.1.8

4dgc, 3D-view

5.2.1.8

4hy7, 3D-view

5.2.1.8

4jjm, 3D-view

5.2.1.8

5a0e, 3D-view

5.2.1.8

6hmz, 3D-view

5.2.1.8

7pcj, 3D-view

5.2.1.8

1bck, 3D-view

5.2.1.8

1c5f, 3D-view

5.2.1.8

1cwa, 3D-view

5.2.1.8

1cwb, 3D-view

5.2.1.8

1cwc, 3D-view

5.2.1.8

1cwf, 3D-view

5.2.1.8

1cwl, 3D-view

5.2.1.8

1cwm, 3D-view

5.2.1.8

1cwo, 3D-view

5.2.1.8

1cyn, 3D-view

5.2.1.8

1m63, 3D-view

5.2.1.8

1mf8, 3D-view

5.2.1.8

1mik, 3D-view

5.2.1.8

1qng, 3D-view

5.2.1.8

1qnh, 3D-view

5.2.1.8

1xq7, 3D-view

5.2.1.8

2esl, 3D-view

5.2.1.8

2oju, 3D-view

5.2.1.8

2rma, 3D-view

5.2.1.8

2rmb, 3D-view

5.2.1.8

2rmc, 3D-view

5.2.1.8

2wfj, 3D-view

5.2.1.8

2x2c, 3D-view

5.2.1.8

2x7k, 3D-view

5.2.1.8

2z6w, 3D-view

5.2.1.8

3cys, 3D-view

5.2.1.8

3eov, 3D-view

5.2.1.8

3odi, 3D-view

5.2.1.8

3odl, 3D-view

5.2.1.8

3pmp, 3D-view

5.2.1.8

4dgc, 3D-view

5.2.1.8

4hy7, 3D-view

5.2.1.8

4jjm, 3D-view

5.2.1.8

5a0e, 3D-view

5.2.1.8

6hmz, 3D-view

5.2.1.8

7pcj, 3D-view

5.2.1.8

1bck, 3D-view

5.2.1.8

1c5f, 3D-view

5.2.1.8

1cwa, 3D-view

5.2.1.8

1cwb, 3D-view

5.2.1.8

1cwc, 3D-view

5.2.1.8

1cwf, 3D-view

5.2.1.8

1cwl, 3D-view

5.2.1.8

1cwm, 3D-view

5.2.1.8

1cwo, 3D-view

5.2.1.8

1cyn, 3D-view

5.2.1.8

1m63, 3D-view

5.2.1.8

1mf8, 3D-view

5.2.1.8

1mik, 3D-view

5.2.1.8

1qng, 3D-view

5.2.1.8

1qnh, 3D-view

5.2.1.8

1xq7, 3D-view

5.2.1.8

2esl, 3D-view

5.2.1.8

2oju, 3D-view

5.2.1.8

2rma, 3D-view

5.2.1.8

2rmb, 3D-view

5.2.1.8

2rmc, 3D-view

5.2.1.8

2wfj, 3D-view

5.2.1.8

2x2c, 3D-view

5.2.1.8

2x7k, 3D-view

5.2.1.8

2z6w, 3D-view

5.2.1.8

3cys, 3D-view

5.2.1.8

3eov, 3D-view

5.2.1.8

3odi, 3D-view

5.2.1.8

3odl, 3D-view

5.2.1.8

3pmp, 3D-view

5.2.1.8

4dgc, 3D-view

5.2.1.8

4hy7, 3D-view

5.2.1.8

4jjm, 3D-view

5.2.1.8

5a0e, 3D-view

5.2.1.8

6hmz, 3D-view

5.2.1.8

7pcj, 3D-view

5.2.1.8

1bck, 3D-view

5.2.1.8

1c5f, 3D-view

5.2.1.8

1cwa, 3D-view

5.2.1.8

1cwb, 3D-view

5.2.1.8

1cwc, 3D-view

5.2.1.8

1cwf, 3D-view

5.2.1.8

1cwl, 3D-view

5.2.1.8

1cwm, 3D-view

5.2.1.8

1cwo, 3D-view

5.2.1.8

1cyn, 3D-view

5.2.1.8

1m63, 3D-view

5.2.1.8

1mf8, 3D-view

5.2.1.8

1mik, 3D-view

5.2.1.8

1qng, 3D-view

5.2.1.8

1qnh, 3D-view

5.2.1.8

1xq7, 3D-view

5.2.1.8

2esl, 3D-view

5.2.1.8

2oju, 3D-view

5.2.1.8

2rma, 3D-view

5.2.1.8

2rmb, 3D-view

5.2.1.8

2rmc, 3D-view

5.2.1.8

2wfj, 3D-view

5.2.1.8

2x2c, 3D-view

5.2.1.8

2x7k, 3D-view

5.2.1.8

2z6w, 3D-view

5.2.1.8

3cys, 3D-view

5.2.1.8

3eov, 3D-view

5.2.1.8

3odi, 3D-view

5.2.1.8

3odl, 3D-view

5.2.1.8

3pmp, 3D-view

5.2.1.8

4dgc, 3D-view

5.2.1.8

4hy7, 3D-view

5.2.1.8

4jjm, 3D-view

5.2.1.8

5a0e, 3D-view

5.2.1.8

6hmz, 3D-view

5.2.1.8

7pcj, 3D-view

5.2.1.8

1bck, 3D-view

5.2.1.8

1c5f, 3D-view

5.2.1.8

1cwa, 3D-view

5.2.1.8

1cwb, 3D-view

5.2.1.8

1cwc, 3D-view

5.2.1.8

1cwf, 3D-view

5.2.1.8

1cwl, 3D-view

5.2.1.8

1cwm, 3D-view

5.2.1.8

1cwo, 3D-view

5.2.1.8

1cyn, 3D-view

5.2.1.8

1m63, 3D-view

5.2.1.8

1mf8, 3D-view

5.2.1.8

1mik, 3D-view

5.2.1.8

1qng, 3D-view

5.2.1.8

1qnh, 3D-view

5.2.1.8

1xq7, 3D-view

5.2.1.8

2esl, 3D-view

5.2.1.8

2oju, 3D-view

5.2.1.8

2rma, 3D-view

5.2.1.8

2rmb, 3D-view

5.2.1.8

2rmc, 3D-view

5.2.1.8

2wfj, 3D-view

5.2.1.8

2x2c, 3D-view

5.2.1.8

2x7k, 3D-view

5.2.1.8

2z6w, 3D-view

5.2.1.8

3cys, 3D-view

5.2.1.8

3eov, 3D-view

5.2.1.8

3odi, 3D-view

5.2.1.8

3odl, 3D-view

5.2.1.8

3pmp, 3D-view

5.2.1.8

4dgc, 3D-view

5.2.1.8

4hy7, 3D-view

5.2.1.8

4jjm, 3D-view

5.2.1.8

5a0e, 3D-view

5.2.1.8

6hmz, 3D-view

5.2.1.8

7pcj, 3D-view

5.2.1.8

180 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (49 results)

top print hide

Show Turnover Number (49 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.4.3.19

0.47

-

apparent value for mutant enzyme M261Y, at 25°C and pH 8.5

685414

1.4.3.19

0.6

-

apparent value for wild type enzyme, at 25°C and pH 8.5

685414

1.4.3.19

0.6

-

wild type enzyme, at pH 8.5 and 25°C

742488

1.4.3.19

0.73

-

apparent value for mutant enzyme M261H, at 25°C and pH 8.5

685414

1.4.3.19

0.98

-

wild type enzyme, at pH 7.5, temperature not specified in the publication

742365

1.4.3.19

1.08

-

apparent value for mutant enzyme H244F, at 25°C and pH 8.5

685414

1.4.3.19

1.12

-

apparent value for mutant enzyme H244Q, at 25°C and pH 8.5

685414

1.4.3.19

1.33

-

apparent value for mutant enzyme H244N, at 25°C and pH 8.5

685414

1.4.3.19

1.6

-

-

440361

1.4.3.19

4.2

-

-

440362

1.5.3.1

0.001

-

mutant F235V/F339L, pH not specified in the publication, 37°C

765378

1.5.3.1

0.001

-

wild-type, reconstituted in presence of 7,8-diethyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C

765378

1.5.3.1

0.001

-

wild-type, reconstituted in presence of 7-methyl-8-bromo-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C

765378

1.5.3.1

0.001

-

wild-type, reconstituted in presence of FAD, pH not specified in the publication, 37°C

765378

1.5.3.1

0.0011

-

wild-type, reconstituted in presence of 7-methyl-8-chloro-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C

765378

1.5.3.1

0.0011

-

wild-type, reconstituted in presence of isoalloxazine, pH not specified in the publication, 37°C

765378

1.5.3.1

0.0013

-

wild-type, reconstituted in presence of 7-bromo-8-methyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C

765378

1.5.3.1

0.0013

-

wild-type, reconstituted in presence of 7-chloro-8-ethyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C

765378

1.5.3.1

0.0013

-

wild-type, reconstituted in presence of FMN, pH not specified in the publication, 37°C

765378

1.5.3.1

0.0015

-

wild-type, reconstituted in presence of 3-methyl-7,8-dimethyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C

765378

1.5.3.1

0.0049

-

K265Q mutant, pH 8.0, 25°C

685282

1.5.3.1

0.0066

-

K265A mutant, pH 8.0, 25°C

685282

1.5.3.1

0.0076

-

K265M mutant, pH 8.0, 25°C

685282

1.5.3.1

0.0113

-

K358R mutant enzyme, pH 8.0, 25°C

687443

1.5.3.1

0.053

-

wild-type, 37°C, pH not specified in the publication

765379

1.5.3.1

0.115

-

native enzyme, reconstructed with 20% dimethyl sulfoxide, pH 8.0, 37°C

743119

1.5.3.1

0.204

-

native enzyme, reconstructed in aqueous, pH 8.0, 37°C

743119

1.5.3.1

0.272

-

K265R mutant, pH 8.0, 25°C

685282

1.5.3.1

2.25

-

K171A mutant enzyme, pH 8.0, 25°C

687443

1.5.3.1

2.64

-

K171D mutant enzyme, pH 8.0, 25°C

687443

1.5.3.1

2.7

-

R49K mutant, pH 8.0, 25°C

685219

1.5.3.1

5.8

-

-

392382, 392377

1.5.3.1

9.23

-

K171R mutant enzyme, pH 8.0, 25°C

687443

1.5.3.1

18.5

-

wild-type enzyme, pH 8.0, 25°C

687443

1.5.3.1

20.3

-

pH 8.5, 60°C

671547

1.5.3.1

45.8

-

native protein, pH 8.0, 25°C

685282

1.5.3.1

101

-

native enzyme, pH 8.0, 25°C

685219

1.4.3.19

10 entries

1.5.3.1

27 entries

1.5.3.19

4

-

pH 10, temperature not specified in the publication

719401

1.5.3.24

1.65

-

mutant enzyme Y271A, at pH 8.0 and 25°C

765018

1.5.3.24

5.8

-

at pH 8.3 and 37°C

765024

1.5.3.24

7.15

-

mutant enzyme Y271F, at pH 8.0 and 25°C

765018

1.5.3.24

14.5

-

mutant enzyme Y269A, at pH 8.0 and 25°C

765018

1.5.3.24

17.5

-

wild type enzyme, at pH 8.0 and 25°C

765018

1.5.3.24

5 entries

1.5.7.3

0.28

-

pH 7.5, 60°C

763964

1.5.8.3

0.065

-

-

392496

1.5.8.4

0.28

-

pH 7.5, 60°C

763963

2.1.1.157

0.44

-

pH 7.2, 37°C

695924

2.1.1.157

1.07

-

-

689964

2.1.1.157

2 entries

6.3.4.13

3.6

-

-

1412

K_M Value (97 results)

top print hide

Show KM Value (97 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.21.4.3

3.7

-

pH 7.7, 37°C

636280

1.4.3.19

0.22

-

-

440361

1.4.3.19

0.23

-

M261Y mutant

672771

1.4.3.19

0.45

-

in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate, at pH 8.5 and 37°C

689934

1.4.3.19

0.45

-

pH 8.5, 37°C

701114

1.4.3.19

0.51

-

mutant enzyme I15V, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C

687878

1.4.3.19

0.57

-

M261 wild type

672771

1.4.3.19

0.58

-

M261H mutant

672771

1.4.3.19

0.6

-

wild type enzyme, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C

687878

1.4.3.19

0.7

-

apparent value for wild type enzyme, at 25°C and pH 8.5

685414

1.4.3.19

0.7

-

wild type enzyme, at pH 8.5 and 25°C

742488

1.4.3.19

1.4

-

apparent value for mutant enzyme H244F, at 25°C and pH 8.5

685414

1.4.3.19

1.51

-

wild type enzyme, at pH 7.5, temperature not specified in the publication

742365

1.4.3.19

2.1

-

apparent value for mutant enzyme H244N, at 25°C and pH 8.5

685414

1.4.3.19

2.6

-

-

440362

1.4.3.19

2.8

-

apparent value for mutant enzyme H244Q, at 25°C and pH 8.5

685414

1.4.3.19

4.86

-

at pH 8.5 and 40°C

743136

1.4.3.19

11

-

apparent value for mutant enzyme M261H, at 25°C and pH 8.5

685414

1.4.3.19

11

-

apparent value for mutant enzyme M261Y, at 25°C and pH 8.5

685414

1.5.3.1

0.01

-

R49K mutant, pH 8.0, 25°C

685219

1.5.3.1

0.285

-

immobilized enzyme on alkylamine glass beads, pH 7.8, 37°C

725124

1.5.3.1

0.29

-

native enzyme, pH 8.0, 25°C

685219

1.5.3.1

0.91

-

-

392376

1.5.3.1

1.379

-

immobilized enzyme on arylamine glass beads, pH 7.8, 37°C

725124

1.5.3.1

1.47

-

K171A mutant enzyme, pH 8.0, 25°C

687443

1.5.3.1

1.72

-

K171R mutant enzyme, pH 8.0, 25°C

687443

1.5.3.1

2.75

-

K171D mutant enzyme, pH 8.0, 25°C

687443

1.5.3.1

2.76

-

wild-type enzyme, pH 8.0, 25°C

687443

1.5.3.1

3.1

-

pH 8.5, 60°C

724775, 671547

1.5.3.1

3.4

-

-

392382

1.5.3.1

4.2

-

-

392379

1.5.3.1

6.4

-

-

392377

1.5.3.1

7.6

-

native enzyme, pH 8.0, 25°C

685219

1.5.3.1

12.2

-

-

392378

1.5.3.1

17.4

-

K358R mutant enzyme, pH 8.0, 25°C

687443

1.5.3.1

19.7

-

wild-type, reconstituted in presence of 7-chloro-8-ethyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C

765378

1.5.3.1

21

-

at pH 8.0 and 30°C

764208

1.5.3.1

28.8

-

R49K mutant, pH 8.0, 25°C

685219

1.5.3.1

47.2

-

wild-type, reconstituted in presence of 3-methyl-7,8-dimethyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C

765378

1.5.3.1

47.94

-

37°C, pH 8.0, poly-lysine modified enzyme

742678

1.5.3.1

50

-

free enzyme, pH 7.8, 37°C

725124

1.5.3.1

61.2

-

wild-type, 37°C, pH not specified in the publication

765379

1.5.3.1

81.9

-

wild-type, reconstituted in presence of FMN, pH not specified in the publication, 37°C

765378

1.5.3.1

85.9

-

wild-type, reconstituted in presence of 7-methyl-8-bromo-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C

765378

1.5.3.1

112.5

-

wild-type, reconstituted in presence of 7-methyl-8-chloro-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C

765378

1.5.3.1

128.9

-

mutant F235V/F339L, pH not specified in the publication, 37°C

765378

1.5.3.1

134.7

-

wild-type, reconstituted in presence of 7,8-diethyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C

765378

1.5.3.1

137.2

-

wild-type, reconstituted in presence of FAD, pH not specified in the publication, 37°C

765378

1.5.3.1

141.6

-

native enzyme, reconstructed in aqueous, pH 8.0, 37°C

743119

1.5.3.1

141.65

-

37°C, pH 8.0, soluble enzyme

742678

1.5.3.1

142.3

-

native enzyme, reconstructed with 20% dimethyl sulfoxide, pH 8.0, 37°C

743119

1.5.3.1

153.6

-

wild-type, reconstituted in presence of isoalloxazine, pH not specified in the publication, 37°C

765378

1.5.3.1

183.1

-

wild-type, reconstituted in presence of 7-bromo-8-methyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C

765378

1.4.3.19

18 entries

1.5.3.1

34 entries

1.5.3.19

25

-

pH 10, temperature not specified in the publication

719401

1.5.3.20

0.97

-

pH 8.0, 30°C

762741

1.5.3.24

1.4

-

wild type enzyme, at pH 8.0 and 25°C

765018

1.5.3.24

1.47

-

mutant enzyme K171A, at pH 8.0 and 25°C

765017

1.5.3.24

1.72

-

mutant enzyme K171R, at pH 8.0 and 25°C

765017

1.5.3.24

2.75

-

mutant enzyme K171D, at pH 8.0 and 25°C

765017

1.5.3.24

2.76

-

wild type enzyme, at pH 8.0 and 25°C

765017

1.5.3.24

3.4

-

at pH 8.3 and 37°C

765024

1.5.3.24

3.8

-

at pH 7.0 and 37°C

765024

1.5.3.24

11.3

-

mutant enzyme Y269A, at pH 8.0 and 25°C

765018

1.5.3.24

17.4

-

mutant enzyme K358R, at pH 8.0 and 25°C

765017

1.5.3.24

72.6

-

mutant enzyme Y271F, at pH 8.0 and 25°C

765018

1.5.3.24

1730

-

mutant enzyme Y271A, at pH 8.0 and 25°C

765018

1.5.3.24

11 entries

1.5.7.3

14.85

-

pH 7.5, 60°C

763964

1.5.8.3

0.32

1

-

392494, 392496, 392499, 392507

1.5.8.3

1.3

-

pH 7.5, 37°C, immobilized enzyme

655081

1.5.8.3

1.9

-

pH 7.5, 37°C, non-immobilized enzyme

655081

1.5.8.3

3.9

-

-

392510

1.5.8.3

6.1

-

-

390333

1.5.8.3

29

-

-

392502

1.5.8.3

6 entries

1.5.8.4

14.65

-

pH 7.5, 60°C

763963

1.5.99.5

0.1

-

-

437743

1.5.99.5

90.9

-

-

437744, 437745

1.5.99.5

200

-

-

437743

2.1.1.156

0.8

-

pH 8.8, 37°C

659286

2.1.1.156

0.8

-

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

659286

2.1.1.156

1.1

-

pH 8.8, 37°C, recombinant mutant R169K

659286

2.1.1.156

2.3

-

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

657578

2.1.1.156

2.94

-

pH 8.2, 37°C

671647

2.1.1.156

3020

-

pH 7.3, 37°C, recombinant enzyme

720836

2.1.1.157

0.8

-

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

659286

2.1.1.157

2

-

-

689964

2.1.1.157

2.29

-

pH 7.2, 37°C

695924

2.1.1.157

2.29

-

pH 7.3, 37°C, recombinant enzyme

720836

2.1.1.157

6.1

-

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

657578

2.1.1.162

0.73

-

wild-type, pH 8.0, 25°C

758064

2.1.1.162

1.5

-

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

758064

2.1.1.162

3.14

-

pH 7.2, 37°C

677087

6.1.1.15

45

-

ATP-diphosphate exchange

174

6.1.1.15

67

-

ATP-diphosphate exchange

174

6.1.1.15

100

-

ATP-diphosphate exchange

174

6.1.1.15

140

-

ATP-diphosphate exchange

174

6.1.1.15

300

-

approximate value, , ATP-diphosphate exchange

174

1.5.99.5

3 entries

2.1.1.156

6 entries

2.1.1.157

5 entries

2.1.1.162

3 entries

6.1.1.15

5 entries

6.3.4.13

1.2

-

-

1412

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

405

-

pH 8.0, 25°C

654371

1.2.1.8

130

-

-

390329

References & Links

Literature References (173)

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Show Reference (173 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

174

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Purification and characterization of a novel enzyme, N-carbamoylsarcosine amidohydrolase, from Pseudomonas putida 77

1986

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261

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Reagent and methods for determining N-carbamoylsarcosine and a new enzyme suitable for this method

1984

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Ger. Offen. DE3248145

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1986

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Crystal structure analysis, refinement and enzymatic reaction mechanism of N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. at 2.0 A resolution

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1950

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288977

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Manufacture of creatine amidinohydrolase with Acinetobacter

1986

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1984

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1993

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1981

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Creatinineamide hydrolase and creatineamidino hydrolase

1980

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Jpn. Kokai Tokkyo Koho JP55/34029 [80/34029]

6 pp.

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288983

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Creatine amidinohydrolase

1977

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614

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288984

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Creatine and creatine hydrolase

1977

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288985

1696320

Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures

1990

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288986

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Purification and characterization of creatine amidinohydrolase of Alcaligenes origin

1986

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288989

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Creatine amidinohydrolase of Pseudomonas putida: crystallization and some properties

1976

Yoshimoto, T.; Oka, I.; Tsuru, D.

Arch. Biochem. Biophys.

177

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288990

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1976

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1974

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3

9-15

288992

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Sequence and structure comparison suggests that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold

1994

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Proc. Natl. Acad. Sci. USA

91

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288993

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Effects of pH, temperature and reaction products on the performance of an immobilized creatininase-creatinase-sarcosine oxidase enzyme system for creatinine determination

1992

Sakslund, H.; Hammerich, O.

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268

331-345

288994

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Intrinsic stability and extrinsic stabilization of creatinase from Pseudomonas putida

1993

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288995

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Cloning of creatinase gene from Pseudomonas putida, in Escherichia coli by using an indicator plate

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1998

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The characterisation of inducible dehydrogenases specific for the oxidation of D-alanine, allohydroxy-D-proline, choline and sarcosine as peripheral membrane proteins in Pseudomonas aeruginosa

1977

Bater, A.J.; Venables, W.A.

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468

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Purification and characterization of osmoregulatory betaine aldehyde dehydrogenase of Escherichia coli

1990

Falkenberg, P.; Strom, A.R.

Biochim. Biophys. Acta

1034

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Osmotic control of glycine betaine biosynthesis and degradation in Rhizobium meliloti

1988

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

J. Bacteriol.

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392376

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Purification and characterization of sarcosine oxidase of Streptomyces origin

1987

Inouye, Y.; Nishimura, M.; Matsuda, Y.; Hoshika, H.; Iwasaki, H.; Hujimura, K.; Asano, K.; Nakamura, S.

Chem. Pharm. Bull.

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392377

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Sarcosine oxidase from Arthrobacter urefaciens: Purification and some properties

1988

Ogushi, S.; Nagao, K.; Emi, S.; Ando, M.; Tsuru, D.

Chem. Pharm. Bull.

36

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392378

3594681

Purification and characterization of sarcosine oxidase of Bacillus origin

1987

Matsuda, Y.; Hoshika, H.; Inouye, Y.; Ikuta, S.; Matsuura, K.; Nakamura, S.

Chem. Pharm. Bull.

35

711-717

392379

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Crystallization and characterization of sarcosine oxidase from Alcaligenes denitrificans subsp. denitrificans

1987

Kim, J.M.; Shimizu, S.; Yamada, H.

Agric. Biol. Chem.

51

1167-1168

392380

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Sarcosine oxidase involved in creatinine degradation in Alcaligenes denitrificans subsp. denitrificans J9 and Arthrobacter spp. J5 and J11

1986

Kim, J.M.; Shimizu, S.; Yamada, H.

Agric. Biol. Chem.

50

2811-2816

392381

4027239

Properties and catalytic function of the two nonequivalent flavins in sarcosine oxidase

1985

Schuman Jorns, M.

Biochemistry

24

3189-3194

392382

7240129

Purification and some properties of sarcosine oxidase from Corynebacterium sp. U-96

1981

Suzuki, M.

J. Biochem.

89

599-607

392383

6158947

Corynebacterium sarcosine oxidase: a unique enzyme having covalently-bound and noncovalently-bound flavins

1980

Hayashi, S.; Nakamura, S.; Suzuki, M.

Biochem. Biophys. Res. Commun.

96

924-930

392384

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Purification and properties of sarcosine oxidase from Cylindrocarpum didymum M-1

1980

Mori, N.; Sano, M.; Tani, Y.; Yamada, H.

Agric. Biol. Chem.

44

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392385

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Isolation of acid-nonextractable flavins from a bacterial sarcosine oxidase

1972

Patek, D.R.; Dahl, C.R.; Frisell, W.R.

Biochem. Biophys. Res. Commun.

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392386

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Mechanism of reduction of Corynebacterium sarcosine oxidase by dithiothreitol

1984

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1983

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392388

6188492

Steady-state kinetics and spectral properties of Corynebacterium sarcosine oxidase

1983

Hayashi, S.; Suzuki, M.; Nakamura, S.

Biochim. Biophys. Acta

742

630-636

392389

2443179

Kinetic studies on the reaction mechanism of sarcosine oxidase

1987

Kawamura-Konishi, Y.; Suzuki, H.

Biochim. Biophys. Acta

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392390

5545477

One-carbon metabolism in microorganisms. I. Oxidative demethylation in a sarcosine-utilizing bacterium

1971

Frisell, W.R.

Arch. Biochem. Biophys.

142

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392391

3790506

Bacterial sarcosine oxidase: Comparison of two multisubunit enzymes containing both covalent and noncovalent flavin

1986

Kvalnes-Krick, K.; Schuman Jorns, M.

Biochemistry

25

6061-6069

392393

2430939

Glyphosate catabolism by Pseudomonas Sp. strain PG2982

1986

Shinabarger, D.L.; Braymer, H.D.

J. Bacteriol.

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392398

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Enzyme cytochemical localization of sarcosine oxidase activity in the liver and kidney of several mammals

2000

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Dimethylglycine dehydrogenase and sarcosine dehydrogenase: mitochondrial folate-binding proteins from rat liver

1986

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392496

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Enzymatic properties of dimethylglycine dehydrogenase and sarcosine dehydrogenase from rat liver

1985

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392497

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

1985

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J. Biol. Chem.

260

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392498

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

1982

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Biochem. J.

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392499

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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

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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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392501

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Identification of the covalently bound flavin of dimethylglycine dehydrogenase and sarcosine dehydrogenase from rat liver mitochondria

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392502

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Sarcosine dehydrogenase from Pseudomonas putida: purification and some properties

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392506

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Purification and characterization of the flavin prosthetic group of sarcosine dehydrogenase

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392507

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Sarcosine dehydrogenase and dimethylglycine dehydrogenase (rat liver, monkey liver)

1970

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392508

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Separation and purification of sarcosine dehydrogenase and dimethylglycine dehydrogenase

1962

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392509

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Cloning and mapping of the cDNA for human sarcosine dehydrogenase, a flavoenzyme defective in patients with sarcosinemia

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392510

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Purification and some properties of sarcosine dehydrogenase from Pseudomonas putida RS65

2001

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Food Sci. Agric. Chem.

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392511

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Molecular cloning and tissue distribution of rat sarcosine dehydrogenase

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392516

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Covalent binding of folic acid to dimethylglycine dehydrogenase

1984

Wagner, C.; Briggs, W.T.; Cook, R.J.

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392520

6159630

Identification of folate binding protein of mitochondria as dimethylglycine dehydrogenase

1980

Wittwer, A.J.; Wagner, C.

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392524

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Rat liver dimethylglycine dehydrogenase. Flavinylation of the enzyme in hepatocytes in primary culture and characterization of a cDNA clone

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437743

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1972

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437744

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437745

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437748

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485212

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485213

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Reductive cleavage of sarcosine and betaine by Eubacterium acidaminophilum via enzyme systems different from glycine reductase

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Purification and characterization of protein PB of betaine reductase and its relationship to the corresponding proteins glycine reductase and sarcosine reductase from Eubacterium acidaminophilum

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1998

Harms, C.; Ludwig, U.; Andressen, J.R.

Arch. Microbiol.

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The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase

2004

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654459

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Low pKa lysine residues at the active site of sarcosine oxidase from Corynebacterium sp. U-96

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Enzymatic activity and stability of D-fructose dehydrogenase and sarcosine dehydrogenase immobilized onto giant vesicles

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Structure-function correlation in glycine oxidase from Bacillus subtilis

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Characterization of glycine sarcosine N-methyltransferase and sarcosine dimethylglycine N-methyltransferase

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Appl. Environ. Microbiol.

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Extreme halophiles synthesize betaine from glycine by methylation

2000

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Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica

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Expression and characterization of a thermostable sarcosine oxidase (SOX) from Bacillus sp. in Escherichia coli

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Guo, K.; Ma, X.; Sun, G.; Zhao, Y.; Li, X.; Zhao, W.; Kai, L.

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671647

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Identification of glycine betaine as compatible solute in Synechococcus sp. WH8102 and characterization of its N-methyltransferase genes involved in betaine synthesis

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Biochemistry

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Role of the covalent flavin linkage in monomeric sarcosine oxidase

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Hassan-Abdallah, A.; Zhao, G.; Jorns, M.S.

Biochemistry

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672771

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Maximization of production of his-tagged glycine oxidase and its M261 mutant proteins

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Martinez-Martinez, I.; Navarro-Fernandez, J.; Lozada-Ramirez, J.D.; Garcia-Carmona, F.; Sanchez-Ferrer, A.

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Effects of substrate and potassium on the betaine-synthesizing enzyme glycine sarcosine dimethylglycine N-methyltransferase from a halophilic methanoarchaeon Methanohalophilus portucalensis

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Identification of the oxygen activation site in monomeric sarcosine oxidase: role of lys265 in catalysis

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