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Ligand methylamine

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

methane metabolism

KEGG

Carbon metabolism, Methane metabolism, Microbial metabolism in diverse environments

MetaCyc

aromatic biogenic amine degradation (bacteria), carbaryl degradation, carbofuran degradation I, carbofuran degradation II, carbofuran degradation III, creatinine degradation III, methanogenesis from dimethylamine, methanogenesis from methylamine, methylamine degradation I, methylamine degradation II, N-methylpyrrolidone degradation, nicotine degradation I (pyridine pathway), nicotine degradation II (pyrrolidine pathway), nicotine degradation III (VPP pathway), nicotine degradation IV, noradrenaline and adrenaline degradation, trimethylamine degradation, viridicatin biosynthesis more

Show all BRENDA pathways known for methylamine

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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

1.4.1.17

pyruvate + methylamine + NADPH = N-methyl-L-alanine + H2O + NADP+

391526

-

1.4.3.21

methylamine + H2O + O2 = formaldehyde + NH3 + H2O2

701561, 703130

-

1.4.9.1

methylamine + amicyanin + H2O = formaldehyde + reduced amicyanin + NH3

396582

-

1.4.9.1

methylamine + H2O + 2 amicyanin = formaldehyde + NH3 + 2 reduced amicyanin

741759, 742302, 742338, 763938, 765329

-

1.4.9.1

methylamine + H2O + amicyanin = formaldehyde + NH3 + reduced amicyanin

723880

-

1.4.9.1

3 entries

2.1.1.21

methylamine + L-glutamate = NH3 + N-methyl-L-glutamate

485234, 485235, 485237, 700286, 485233, 485236

-

2.1.1.248

methylamine + a [Co(I) methylamine-specific corrinoid protein] = a [methyl-Co(III) methylamine-specific corrinoid protein] + ammonia

717757, 717723, 717525, 717771, 717781

-

3.5.1.36

alpha-ketoglutarate + methylamine = N-methyl-2-oxoglutaramate + H2O

209088

-

6.3.4.12

ATP + L-Glu + methylamine = ?

1399

-

6.3.4.12

ATP + L-glutamate + methylamine = ADP + phosphate + N5-methyl-L-glutamine

691369, 691366

-

6.3.4.12

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (18 results)

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Show Natural Product (18 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.238

dimethylamine + NADPH + H+ + O2 = methylamine + formaldehyde + NADP+ + H2O

0

-

1.21.4.3

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

0

-

1.4.3.1

N-methyl-D-Asp + H2O + O2 = oxaloacetate + methylamine + H2O2

0

-

1.4.3.1

N-methyl-D-aspartate + H2O + O2 = oxaloacetate + methylamine + H2O2

0

-

1.4.3.1

2 entries

1.4.3.12

N-methylcyclohexylamine + O2 + H2O = cyclohexanone + methylamine + H2O2

395988

-

1.4.3.19

sarcosine + H2O + O2 = glyoxylate + methylamine + H2O2

0

-

1.5.8.1

dimethylamine + H2O + electron-transfer flavoprotein = methylamine + formaldehyde + reduced electron-transferring flavoprotein

0

-

1.5.8.1

dimethylamine + H2O + electron-transferring flavoprotein = methylamine + formaldehyde + reduced electron-transferring flavoprotein

0

-

1.5.8.1

2 entries

1.5.99.14

6-hydroxypseudooxynicotine + EtfAB + H2O = 6-hydroxy-3-succinoylsemialdehyde-pyridine + methylamine + reduced EtfAB

0

-

2.1.1.249

dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein] = a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine

0

-

2.1.1.249

dimethylamine + a [Co(I) methylamine-specific corrinoid protein] = a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine

0

-

3.5.1.137

an N-methyl carbamate ester + H2O = an alcohol + methylamine + CO2

0

-

3.5.1.137

carbaryl + H2O = 1-naphthol + methylamine + CO2

0

-

3.5.1.137

carbofuran + H2O = 7-phenol + methylamine + CO2

0

-

3.5.1.4

N-methylacetamide + H2O = methylamine + acetate

209122

-

3.5.1.4

N-methylpropionamide + H2O = methylamine + propionate

209122

-

2.1.1.249

2 entries

3.5.1.137

3 entries

3.5.1.4

2 entries

3.5.3.16

methylguanidine + H2O = methylamine + urea

0

-

4.2.1.88

(+/-)-synephrine = 4-hydroxyphenylacetaldehyde + methylamine

0

-

Substrate in Enzyme-catalyzed Reactions (77 results)

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Show Substrate (77 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.25

methylamine + NADH + H+ + O2 = hydroxymethylamine + H2O + NAD+

711260

-

1.4.1.17

methylamine + alpha-ketobutyrate + NADPH = glutamic acid + H2O + NADP+

391526

-

1.4.1.17

methylamine + oxaloacetate + NADPH = aspartic acid + H2O + NADP+

391526

-

1.4.1.17

pyruvate + methylamine + NADPH = N-methyl-L-alanine + H2O + NADP+

391526

-

1.4.1.28

cyclohexanone + methylamine + NADH + H+ = N-methylcyclohexylamine + NAD+ + H2O

763489

-

1.4.1.28

cyclohexanone + methylamine + NADPH + H+ = N-methylcyclohexanamine + H2O + NADP+

765439

-

1.4.1.28

isobutanal + methylamine + NADH + H+ = N,2-dimethylpropan-1-amine + NAD+ + H2O

763489

-

1.4.3.21

methylamine + H2O + O2 = formaldehyde + NH3 + H2O2

701561, 725733, 703130, 724322, 726290, 724283

-

1.4.3.21

methylamine + H2O + O2 = methanal + NH3 + H2O2

688491, 391949, 391960, 654616, 672133, 672152

-

1.4.1.17

3 entries

1.4.1.28

3 entries

1.4.3.21

2 entries

1.4.3.4

methylamine + H2O + O2 = formaldehyde + NH3 + H2O2

724603

-

1.4.9.1

methylamine + acceptor + H2O = formaldehyde + NH3 + reduced acceptor

685218, 686104, 685296, 704815, 654628, 654676, 654866, 656086

-

1.4.9.1

methylamine + acceptor + H2O = methanal + NH3 + reduced acceptor

396581, 396585, 396578, 656282

-

1.4.9.1

methylamine + amicyanin + H2O = formaldehyde + NH3 + reduced amicyanin

685087, 688702

-

1.4.9.1

methylamine + amicyanin + H2O = formaldehyde + reduced amicyanin + NH3

396582, 685296

-

1.4.9.1

methylamine + H2O + 2 amicyanin = formaldehyde + NH3 + 2 reduced amicyanin

741759, 742302, 742338, 763938, 765329

-

1.4.9.1

methylamine + H2O + 2,6-dichloroindophenol + phenazine ethosulfate = formaldehyde + NH3 + reduced phenazine ethosulfate + ?

396585

-

1.4.9.1

methylamine + H2O + 2,6-dichloroindophenol = formaldehyde + NH3 + reduced 2,6-dichloroindophenol

396585

-

1.4.9.1

methylamine + H2O + amicyanin = formaldehyde + ammonia + reduced amicyanin

715266, 714231

-

1.4.9.1

methylamine + H2O + amicyanin = formaldehyde + NH3 + reduced amicyanin

723880

-

1.4.9.1

methylamine + H2O + cytochrome c-550 = formaldehyde + NH3 + reduced cytochrome c-550

396583

-

1.4.9.1

methylamine + H2O + K3Fe(CN)6 = formaldehyde + NH3 + reduced K3Fe(CN)6

396585

-

1.4.9.1

11 entries

1.4.9.2

methylamine + acceptor + H2O = formaldehyde + NH3 + reduced acceptor

685206

-

1.5.1.21

alpha-ketobutanoate + methylamine + NADPH = N-methyl-2-aminobutanoate + NADP+ + H2O

674509

-

1.5.1.21

alpha-ketohexanoate + methylamine + NADPH = N-methyl-2-aminohexanoate + NADP+ + H2O

674509

-

1.5.1.21

fluoropyruvate + methylamine + NADPH = N-methylfluoroalanine + NADP+ + H2O

674509

-

1.5.1.21

phenylpyruvate + methylamine + NADPH = N-methylphenylalanine + NADP+ + H2O

674509

-

1.5.1.21

pyruvate + methylamine = N-methylalanine

674509

-

1.5.1.25

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

741584

-

1.5.1.25

phenylpyruvate + methylamine + NADPH + H+ = N-methyl-L-phenylalanine + NADP+

741584

-

1.5.1.25

pyruvate + methylamine + NADPH + H+ = N-methyl-L-alanine + NADP+

741584

-

2.1.1.21

methylamine + L-glutamate = NH3 + N-methyl-L-glutamate

485233, 485234, 485235, 485236, 485237, 700286

-

2.1.1.21

methylamine + L-glutamate-gamma-methylester = NH3 + N-methyl-L-glutamate-gamma-methyl ester

485233

-

2.1.1.21

methylamine + L-glutamine = ?

485233

-

2.1.1.21

N-methyl-L-glutamate + methylamine = ?

485236

-

1.5.1.21

5 entries

1.5.1.25

3 entries

2.1.1.21

4 entries

2.1.1.248

methylamine + a [Co(I) methylamine-specific corrinoid protein] = a [methyl-Co(III) methylamine-specific corrinoid protein] + ammonia

717757, 717781, 717723, 717525, 717771

-

2.3.2.13

10-kDa heat shock protein-bound gamma-glutamine + methylamine = 10-kDa heat shock protein N5-methylglutamine + NH3

718564

-

2.3.2.13

60-kDa heat shock protein-bound gamma-glutamine + methylamine = 60-kDa heat shock protein N5-methylglutamine + NH3

718564

-

2.3.2.13

actin-bound gamma-glutamine + methylamine = actin N5-methylglutamine + NH3

718564

-

2.3.2.13

alpha-actin-bound gamma-glutamine + methylamine = alpha-actin N5-methylglutamine + NH3

718564

-

2.3.2.13

clathrin heavy chain-bound gamma-glutamine + methylamine = clathrin heavy chain N5-methylglutamine + NH3

718564

-

2.3.2.13

cytoskeletal 1 keratin type II-bound gamma-glutamine + methylamine = cytoskeletal 1 keratin type II N5-methylglutamine + NH3

718564

-

2.3.2.13

cytoskeletal 2 epidermal keratin type II-bound gamma-glutamine + methylamine = cytoskeletal 2 epidermal keratin type II N5-methylglutamine + NH3

718564

-

2.3.2.13

cytoskeletal 5 keratin type II-bound gamma-glutamine + methylamine = cytoskeletal 5 keratin type II N5-methylglutamine + NH3

718564

-

2.3.2.13

cytoskeletal 6A keratin type II-bound gamma-glutamine + methylamine = cytoskeletal 6A keratin type II N5-methylglutamine + NH3

718564

-

2.3.2.13

filamin A-bound gamma-glutamine + methylamine = filamin A N5-methylglutamine + NH3

718564

-

2.3.2.13

galectin-3-bound gamma-glutamine + methylamine = galectin-3 N5-methylglutamine + NH3

718564

-

2.3.2.13

H2A histone type 1-bound gamma-glutamine + methylamine = H2A histone type 1 N5-methylglutamine + NH3

718564

-

2.3.2.13

H2B histone type 1-bound gamma-glutamine + methylamine = H2B histone type 1 N5-methylglutamine + NH3

718564

-

2.3.2.13

H4 histone -bound gamma-glutamine + methylamine = H4 histone N5-methylglutamine + NH3

718564

-

2.3.2.13

methylamine + succinyl-beta-casein = ?

487845

-

2.3.2.13

methylamine + succinylated alpha-casein = ?

487845

-

2.3.2.13

nucleophosmin-bound gamma-glutamine + methylamine = nucleophosmin N5-methylglutamine + NH3

718564

-

2.3.2.13

protein-bound gamma-glutamine + methylamine = protein N5-methylglutamine + NH3

718564

-

2.3.2.13

spectrin alpha-bound gamma-glutamine + methylamine = spectrin alpha N5-methylglutamine + NH3

718564

-

2.3.2.13

vimentin-bound gamma-glutamine + methylamine = vimentin N5-methylglutamine + NH3

718564

-

2.3.2.13

20 entries

2.3.2.2

L-glutamylhydrazine + methylamine = gamma-L-glutamylmethylamide + hydrazine

755929

-

2.5.1.2

thiamine + methylamine = ?

636851

-

3.5.1.3

2-oxoglutaramate + methylamine = ?

288892

-

3.5.1.3

ethyl glutarate + methylamine = ?

288892, 288893

-

3.5.1.3

ethyl succinate + methylamine = ?

288892, 288893

-

3.5.1.3

gamma-ethyl 2-oxoglutarate + methylamine = ?

288893, 288892

-

3.5.1.3

gamma-methyl 2-oxoglutarate + methylamine = ?

288893, 288892

-

3.5.1.3

glutaramate + methylamine = ?

288888, 288892

-

3.5.1.3

methyl glutarate + methylamine = ?

288888, 288892, 288893

-

3.5.1.3

methyl succinate + methylamine = ?

288892, 288893

-

3.5.1.3

p-methylphenyl glutarate + methylamine = ?

288888

-

3.5.1.3

succinamate + methylamine = ?

288892

-

3.5.1.3

10 entries

3.5.1.36

alpha-ketoglutarate + methylamine = N-methyl-2-oxoglutaramate + H2O

209088

-

4.3.1.1

methylamine + fumarate = N-methylaspartic acid

691802

-

4.3.1.2

mesaconate + methanamine = ?

729599, 730442

-

4.3.1.2

mesaconate + methylamine = ?

729057

-

6.3.1.2

ATP + L-Glu + methylamine = ADP + phosphate + ?

37488

-

6.3.1.2

ATP + L-Glu + methylamine = ADP + phosphate + L-Gln + ?

661360

-

4.3.1.2

2 entries

6.3.1.2

2 entries

6.3.2.2

ATP + L-Glu + methylamine = ADP + phosphate + N-methyl-L-glutamine

702759

-

6.3.4.12

ATP + L-Glu + methylamine = ?

1399

-

6.3.4.12

ATP + L-Glu + methylamine = ADP + phosphate + N5-methyl-L-glutamine

1399, 1400, 1401

-

6.3.4.12

ATP + L-glutamate + methylamine = ADP + phosphate + N5-methyl-L-glutamine

691369, 691366

-

6.3.4.12

3 entries

Product in Enzyme-catalyzed Reactions (90 results)

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Show Product (90 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.238

dimethylamine + NADH + H+ + O2 = methylamine + formaldehyde + NAD+ + H2O

0

-

1.14.13.238

dimethylamine + NADPH + H+ + O2 = methylamine + formaldehyde + NADP+ + H2O

0

-

1.14.13.238

2 entries

1.18.6.1

reduced ferredoxin + H+ + CH3NC + ATP = oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate

440145, 0, 440154, 440158

-

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

0, 636282, 636280, 636281

-

1.4.3.1

N-methyl-D-aspartate + H2O + O2 = oxaloacetate + CH3NH2 + H2O2

391706, 391712, 391705, 391707, 391717, 391710, 391713, 391714, 0, 391715

-

1.4.3.1

N-methyl-D-Asp + H2O + O2 = oxaloacetate + methylamine + H2O2

0

-

1.4.3.1

N-methyl-D-aspartate + H2O + O2 = oxaloacetate + methylamine + H2O2

0

-

1.4.3.1

N-methyl-D-Glu + H2O + O2 = 2-oxoglutarate + methylamine + H2O2

0

-

1.4.3.1

N-methyl-L-Asp + H2O + O2 = oxaloacetate + methylamine + H2O2

0

-

1.21.4.3

2 entries

1.4.3.1

5 entries

1.4.3.12

N-methylcyclohexylamine + O2 + H2O = cyclohexanone + methylamine + H2O2

395988

-

1.4.3.19

N-methyl-D-Ala + H2O + O2 = pyruvate + methylamine + H2O2

0

-

1.4.3.19

sarcosine + H2O + O2 = glyoxylate + methylamine + H2O2

0

-

1.4.3.19

2 entries

1.4.3.24

4-(methylamino)-1-(pyridin-3-yl)butan-1-one + H2O + O2 = 4-oxo-4-(pyridin-3-yl)butanal + methylamine + H2O2

0

-

1.4.3.3

N-methyl-D-aspartate + H2O + O2 = oxaloacetate + methylamine + H2O2

0

-

1.4.3.3

N-methyl-DL-Leu + H2O + O2 = 4-methyl-2-oxopentanoate + methylamine + H2O2

0

-

1.4.3.4

5-methyl-6,7,8,9-tetrahydro-5H-benzo[7]annulene + H2O + O2 = 6,7,8,9-tetrahydro-5H-benzo[7]annulen-5-one + methylamine + H2O2

0

-

1.4.3.4

N-methyl-1-phenylethan-1-amine + H2O + O2 = 1-phenylethan-1-one + methylamine + H2O2

0

-

1.4.3.4

N-methylhistamine + H2O + O2 = 1H-imidazol-4-ylacetaldehyde + methylamine + H2O2

0

-

1.4.3.3

2 entries

1.4.3.4

3 entries

1.4.3.7

N-methyl-D-aspartate + H2O + O2 = oxaloacetate + methylamine + H2O2

395286

-

1.4.99.2

N-methyltaurine + H2O + acceptor = sulfoacetaldehyde + N-methylamine + reduced acceptor

0

-

1.5.3.20

N-methylalanine + H2O + O2 = methylamine + 2-oxo-propanoic acid + H2O2

0

-

1.5.3.20

sarcosine + H2O + O2 = methylamine + glyoxalate + H2O2

0

-

1.5.3.20

2 entries

1.5.3.21

4-methylaminobutanoate + O2 + H2O = succinate semialdehyde + methylamine + H2O2

0

-

1.5.8.1

dimethylamine + H2O + 2,6-dichlorophenolindophenol = methylamine + formaldehyde + reduced 2,6-dichlorophenolindophenol

0

-

1.5.8.1

dimethylamine + H2O + acceptor = methylamine + formaldehyde + reduced acceptor

393880

-

1.5.8.1

dimethylamine + H2O + electron-transfer flavoprotein = methylamine + formaldehyde + reduced electron-transferring flavoprotein

0

-

1.5.8.1

dimethylamine + H2O + electron-transferring flavoprotein = methylamine + formaldehyde + reduced electron-transferring flavoprotein

0

-

1.5.8.1

dimethylamine + H2O + phenazine methosulfate = methylamine + formaldehyde + reduced phenazine methosulfate

0

-

1.5.99.14

6-hydroxypseudooxynicotine + 2,6-dichlorophenolindophenol + H2O = 6-hydroxy-3-succinoylsemialdehyde-pyridine + methylamine + reduced 2,6-dichlorophenolindophenol

0

-

1.5.99.14

6-hydroxypseudooxynicotine + EtfAB + H2O = 6-hydroxy-3-succinoylsemialdehyde-pyridine + methylamine + reduced EtfAB

0

-

1.5.8.1

5 entries

1.5.99.14

2 entries

1.7.1.10

N-methylhydroxylamine + NADH = methylamine + NAD+ + H2O

394436, 394435

-

2.1.1.249

dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein] = a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine

0

-

2.1.1.249

dimethylamine + a [Co(I) methylamine-specific corrinoid protein] = a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine

0

-

2.1.1.249

2 entries

2.6.1.77

taurine + methanal = 2-sulfoacetaldehyde + methylamine

0

-

3.5.1.1

N4-methyl-L-asparagine = L-Asp + methylamine

0

-

3.5.1.137

2-nitrophenyl dimethylcarbamate + H2O = ? + methylamine + CO2

0

-

3.5.1.137

3,5-dimethylphenyl N-methylcarbamate + H2O = ? + methylamine + CO2

0

-

3.5.1.137

aldicarb + H2O = ? + methylamine + CO2

0

-

3.5.1.137

an N-methyl carbamate ester + H2O = an alcohol + methylamine + CO2

0

-

3.5.1.137

carbaryl + H2O = 1-naphthol + methylamine + CO2

0

-

3.5.1.137

carbofuran + H2O = 2,3-dihydro-2,2-dimethyl-7-benzofuranol + methylamine + CO2

0

-

3.5.1.137

carbofuran + H2O = 7-phenol + methylamine + CO2

0

-

3.5.1.137

carbofuran + H2O = ? + methylamine + CO2

0

-

3.5.1.137

carbofuran + H2O = carbofuran phenol + methylamine + CO2

0

-

3.5.1.137

fenobucarb + H2O = ? + methylamine + CO2

0

-

3.5.1.137

iprovalicarb + H2O = ? + methylamine + CO2

0

-

3.5.1.137

isoprocarb + H2O = ? + methylamine + CO2

0

-

3.5.1.137

methomyl + H2O = methyl (1E)-N-hydroxyethanimidothioate + methylamine + CO2

0

-

3.5.1.137

metolcarb + H2O = ? + methylamine + CO2

0

-

3.5.1.137

oxamyl + H2O = ? + methylamine + CO2

0

-

3.5.1.137

oxamyl oxime + H2O = ? + methylamine + CO2

0

-

3.5.1.137

pirimicarb + H2O = ? + methylamine + CO2

0

-

3.5.1.137

propoxur + H2O = ? + methylamine + CO2

0

-

3.5.1.137

prosulfocarb + H2O = ? + methylamine + CO2

0

-

3.5.1.137

xylylcarb + H2O = ? + methylamine + CO2

0

-

3.5.1.137

20 entries

3.5.1.3

N-methyl-2-oxoglutaramate + H2O = 2-oxoglutarate + methylamine

288893

-

3.5.1.39

N-methylbutyramide + H2O = methylamine + butyric acid

209104

-

3.5.1.39

N-methylcaproamide + H2O = methylamine + hexanoate

209104

-

3.5.1.39

N-methylcaprylamide + H2O = methylamine + octanoate

209104

-

3.5.1.39

N-methylheptylamide + H2O = methylamine + heptanoate

209104

-

3.5.1.39

N-methylvaleramide + H2O = methylamine + pentanoate

209104

-

3.5.1.4

N-methylacetamide + H2O = acetic acid + methaneamine

0

-

3.5.1.4

N-methylacetamide + H2O = methylamine + acetate

209122

-

3.5.1.4

N-methylpropionamide + H2O = methylamine + propionate

209122

-

3.5.1.39

5 entries

3.5.1.4

3 entries

3.5.1.56

N-methylformamide + H2O = methylamine + formate

209200

-

3.5.1.65

N5-methyl-L-glutamine + H2O = L-glutamate + methylamine

0

-

3.5.3.16

methylguanidine + H2O = methylamine + urea

0

-

3.5.3.18

N-monomethyl-L-arginine + H2O = L-citrulline + methylamine

0

-

3.5.3.18

NG-methyl arginine + H2O = L-citrulline + methylamine

0

-

3.5.3.18

NG-methyl-L-arginine + H2O = L-citrulline + methylamine

0

-

3.5.3.18

NG-monomethyl-L-arginine + H2O = citrulline + methylamine

0

-

3.5.3.18

Ngamma-monomethyl-L-arginine + H2O = L-citrulline + methylamine

0

-

3.5.3.18

Nomega-monomethyl-L-arginine + H2O = L-citrulline + methylamine

0

-

3.5.3.6

Nomega-methyl-Arg + H2O = L-citrulline + methylamine

0

-

3.5.3.6

Nomega-methyl-L-arginine + H2O = L-citrulline + methylamine

0

-

3.5.3.18

6 entries

3.5.3.6

2 entries

3.5.4.4

6-methylaminopurine ribonucleoside + H2O = inosine + methylamine

0

-

3.5.4.42

N-methylammelide + H2O = cyanuric acid + methylamine

651707

-

3.5.4.5

N4-methylcytidine + H2O = uridine + methylamine

0

-

3.8.1.8

2,4-dimethylamino-6-hydroxy-1,3,5-triazine + H2O = 6-(methylamino)-1,3,5-triazine-2,4-diol + methylamine

0

-

3.8.1.8

6-(ethylamino)-4-(methylamino)-1,3,5-triazin-2-ol + H2O = 6-(ethylamino)-1,3,5-triazine-2,4-diol + methylamine

0

-

3.8.1.8

6-hydroxy-4-(N-isopropylamino)-2-(N-methylamino)-1,3,5-triazine + H2O = 6-[(1-methylethyl)amino]-1,3,5-triazine-2,4-diol + methylamine

0

-

4.2.1.88

(+/-)-synephrine = 4-hydroxyphenylacetaldehyde + methylamine

648463, 0

-

4.2.1.88

(R)-synephrine = (4-hydroxyphenyl)acetaldehyde + methylamine

648464

-

4.3.1.2

(2S)-N-methylaspartic acid = fumarate + methylamine

6061

-

4.3.1.2

N,3-dimethylaspartic acid = methylfumarate + methylamine

6061

-

4.3.1.2

N-methyl-3-ethylaspartic acid = ethylfumarate + methylamine

6061

-

3.8.1.8

3 entries

4.2.1.88

2 entries

4.3.1.2

3 entries

4.3.1.24

N-methyl-L-phenylalanine = trans-cinnamate + methylamine

651438

-

4.3.2.9

5-L-glutamyl-methylamine = 5-oxoproline + methylamine

0

-

4.4.1.11

DL-2-amino-3-(N-methylamino)propionic acid = methylamine + NH3 + pyruvate

34516

-

Activator in Enzyme-catalyzed Reactions (13 results)

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Show Activating Compound (13 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.169

activation of enzyme from K176A mutant

286109

-

1.1.2.7

can replace NH4+

687432

-

1.1.2.8

-

742110

-

1.1.2.8

methylamine is a 5fold better activator for enzyme ExaF in vitro than ammonium

742793

-

1.1.2.8

2 entries

1.1.5.5

-

740180

-

1.1.99.20

30% activation, Pseudomonas sp. strain No. 43

389907

-

1.14.14.3

alphaH44A mutant, works as catalytic base

348600

-

1.2.2.B2

can replace NH4+

687432

-

2.7.4.1

28% activation compared to NH4+

756630

-

3.6.1.11

28% activation compared to NH4+

756630

-

4.1.1.31

increases the PEPC activity and enhances the effect of abscisic acid

749266

-

5.4.3.2

saturating methylamine accelerates the L-2-aminobutyrate reaction 47fold

716011

-

5.4.3.8

stimulates activity of mutant enzyme Lys265Arg

3432

-

Inhibitor in Enzyme-catalyzed Reactions (23 results)

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Show Inhibitors (23 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.17

-

654371

-

1.14.13.25

slightly

438948

-

1.4.3.10

-

395447

-

1.5.8.1

above 6 mM, slight inhibition

393880

-

1.8.3.4

-

395101

-

2.1.1.249

competitive inhibitor

717558

-

2.1.1.249

MMA, acts as competitive inhibitor of the reaction. The methylation is specifically reversed by MMA

717560

-

2.1.1.249

2 entries

2.3.1.45

slightly

487042

-

2.3.2.13

1.8 mM, 50% inhibition

487840

-

2.5.1.61

-

489923

-

2.7.10.1

-

691283

-

3.4.14.1

-

36134

-

3.4.19.6

-

667505

-

3.4.21.50

-

36618

-

3.4.22.8

-

81588

-

3.4.24.20

-

31045

-

3.5.1.3

0.05 M methylamine: 62% inhibition

288892

-

3.5.1.3

competitve inhibition, inhibits hydroxaminolysis of glutaramate and alpha-ketoglutaramate hydrolysis

288888

-

3.5.1.3

2 entries

3.5.3.18

10 mM, 80% of activity

652188

-

4.1.3.27

reaction of component I with NH4+ as substrate

33277

-

4.3.1.15

-

6046

-

6.3.2.10

inhibition of wild-type enzyme

651110

-

6.3.2.13

500 mM, 80% inhibition

651110

-

3D Structure of Enzyme-Ligand-Complex (PDB) (32 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (32 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.14.14.1

7d1f, 3D-view

1.6.2.4

7d1f, 3D-view

2.3.2.27

6aaw, 3D-view

3.4.21.4

1v6d, 3D-view

3.4.23.20

1apv, 3D-view

3.4.23.20

1apw, 3D-view

3.4.23.20

1apv, 3D-view

3.4.23.20

1apw, 3D-view

3.4.23.20

1apv, 3D-view

3.4.23.20

1apw, 3D-view

3.4.23.20

1apv, 3D-view

3.4.23.20

1apw, 3D-view

3.4.23.20

1apv, 3D-view

3.4.23.20

1apw, 3D-view

3.4.23.20

1apv, 3D-view

3.4.23.20

1apw, 3D-view

3.4.23.20

1apv, 3D-view

3.4.23.20

1apw, 3D-view

4.1.1.39

3axk, 3D-view

4.1.1.39

3axm, 3D-view

4.1.1.39

3axk, 3D-view

4.1.1.39

3axm, 3D-view

4.1.1.39

3axk, 3D-view

4.1.1.39

3axm, 3D-view

4.1.1.39

3axk, 3D-view

4.1.1.39

3axm, 3D-view

4.1.1.39

3axk, 3D-view

4.1.1.39

3axm, 3D-view

4.1.1.39

3axk, 3D-view

4.1.1.39

3axm, 3D-view

4.1.1.39

3axk, 3D-view

4.1.1.39

3axm, 3D-view

3.4.23.20

14 entries

4.1.1.39

14 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (27 results)

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Show Turnover Number (27 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.4.3.21

0.4

-

isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C

725733

1.4.3.21

2.08

-

Co2+ reconstituted enzyme

391960

1.4.3.21

2.12

-

native enzyme

391960

1.4.3.21

2.18

-

isoform HPAO-2, at 25°C, in 100 mM potassium phosphate, pH 7.2

724283

1.4.3.21

5.6

-

at pH 7.4, 37°C

726290

1.4.3.21

6.2

-

isoform HPAO-1, at 25°C, in 100 mM potassium phosphate, pH 7.2

724283

1.4.9.1

0.14

-

pH 7.5, 30°C, mutant enzyme betaD32N, acceptor phenazine ethosulfate/2,6-dichlorophenolindophenol

656282

1.4.9.1

0.19

-

pH 8.5, 30°C, mutant enzyme betaD32N, acceptor phenazine ethosulfate/2,6-dichlorophenolindophenol

656282

1.4.9.1

0.47

-

pH 7.5, 30°C, mutant enzyme betaD32N, acceptor amicyanin

656282

1.4.9.1

1.2

-

pH 8.5, 30°C, mutant enzyme betaD32N, acceptor amicyanin

656282

1.4.9.1

2

-

pH 7.5, 30°C, mutant enzyme alphaF55I

656086

1.4.9.1

13.6

-

with phenylazine as electron acceptor

396581

1.4.9.1

14

-

-

396585

1.4.9.1

18

-

pH 8.5, 30°C, wild-type enzyme, acceptor phenazine ethosulfate/2,6-dichlorophenolindophenol

656282

1.4.9.1

20

-

pH 7.5, 30°C, mutant enzyme betaI107V

656086

1.4.9.1

23

-

pH 7.5, 30°C, wild-type enzyme, acceptor amicyanin

656282

1.4.9.1

26

-

pH 8.5, 30°C, wild-type enzyme, acceptor amicyanin

656282

1.4.9.1

30

-

pH 7.5, 30°C, wild-type enzyme

656086

1.4.9.1

30

-

with amicyanin as electron acceptor at pH 7

396582

1.4.9.1

34

-

pH 7.5, 30°C, mutant enzyme betaI107N

656086

1.4.9.1

35

-

pH 7.5, 30°C, wild-type enzyme, acceptor phenazine ethosulfate/2,6-dichlorophenolindophenol

656282

1.4.9.1

48.5

-

with amicyanin as electron acceptor

396581

1.4.9.1

55

-

with amicyanin as electron acceptor at pH 10

396582

1.4.9.1

77

-

pH 7.5, 30°C, mutant enzyme alphaF55A

656086

2.3.2.13

0.32

-

chondrosarcoma transglutaminase B

487845

2.3.2.13

0.467

-

transglutaminase C

487845

2.3.2.13

1.86

-

factor XIIIa

487845

1.4.3.21

6 entries

1.4.9.1

18 entries

2.3.2.13

3 entries

K_M Value (41 results)

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Show KM Value (41 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.4.1.17

75

-

-

391526

1.4.3.21

0.01

-

native enzyme

391960

1.4.3.21

0.146

-

recombinant enzyme

391949

1.4.3.21

0.18

-

isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C

725733

1.4.3.21

0.236

-

mutant enzyme L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C

724322

1.4.3.21

0.28

-

mutant enzyme M211V, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C

724322

1.4.3.21

0.331

-

wild type enzyme, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C

724322

1.4.3.21

0.502

-

mutant enzyme T212A, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C

724322

1.4.3.21

0.652

-

at pH 7.4, 37°C

726290

1.4.3.21

0.67

-

recombinant enzyme expressed in CHO cells

703130

1.4.3.21

0.68

-

Co2+ reconstituted enzyme

391960

1.4.3.21

1.26

-

mutant enzyme Y394N, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C

724322

1.4.3.21

1.7

-

recombinant enzyme expressed in CHO cells

703130

1.4.3.21

2.043

-

mutant enzyme M211V/Y394N/L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C

724322

1.4.3.21

13 entries

1.4.3.4

0.11

-

at pH 7.0 and 37°C

724603

1.4.9.1

0.004

-

pH 8.5, 30°C, wild-type enzyme, acceptor amicyanin

656282

1.4.9.1

0.005

-

pH 7.5, 30°C, wild-type enzyme, acceptor amicyanin

656282

1.4.9.1

0.0059

-

with amicyanin as electron acceptor

396581

1.4.9.1

0.0064

-

with phenylazine as electron acceptor

396581

1.4.9.1

0.009

-

pH 7.5, 30°C, wild-type enzyme

654866, 656086

1.4.9.1

0.015

-

pH 7.5, 30°C, wild-type enzyme, acceptor phenazine ethosulfate/2,6-dichlorophenolindophenol

656282

1.4.9.1

0.021

-

pH 8.5, 30°C, wild-type enzyme, acceptor phenazine ethosulfate/2,6-dichlorophenolindophenol

656282

1.4.9.1

0.06

-

pH 7.5, 30°C, mutant enzyme alphaF55I

654866, 656086

1.4.9.1

0.069

-

pH 7.5, 30°C, mutant enzyme betaI107V

654866, 656086

1.4.9.1

0.25

-

pH 7.5, 30°C, mutant enzyme betaI107N

654866, 656086

1.4.9.1

1.3

-

-

396585

1.4.9.1

12.2

-

pH 8.5, 30°C, mutant enzyme betaD32N, acceptor amicyanin

656282

1.4.9.1

14.9

-

pH 7.5, 30°C, mutant enzyme alphaF55A

654866, 656086

1.4.9.1

16.7

-

pH 7.5, 30°C, mutant enzyme betaD32N, acceptor phenazine ethosulfate/2,6-dichlorophenolindophenol

656282

1.4.9.1

19.6

-

pH 7.5, 30°C, mutant enzyme betaD32N, acceptor amicyanin

656282

1.4.9.1

22.4

-

pH 8.5, 30°C, mutant enzyme betaD32N, acceptor phenazine ethosulfate/2,6-dichlorophenolindophenol

656282

2.3.2.13

0.024

-

transglutaminase C

487845

2.3.2.13

0.051

-

chondrosarcoma transglutaminase B

487845

2.3.2.13

0.061

-

factor XIIIa

487845

1.4.9.1

16 entries

2.3.2.13

3 entries

2.5.1.2

32

-

-

636851

3.5.1.3

30

-

with substrate, acyl donor: methyl glutarate, Km for total methylamine, for free-base form of methylamine, Km is about 102 times smaller

288888

3.5.1.3

43

-

with substrate, acyl donor: glutaramate, Km for total methylamine, for free-base form of methylamine, Km is about 102 times smaller

288888

3.5.1.3

55

-

with substrate, acyl donor: p-methylphenyl glutarate, Km for total methylamine, for free-base form of methylamine, Km is about 102 times smaller

288888

3.5.1.3

3 entries

3.5.1.36

46

-

-

209088

6.3.1.2

20

-

pH 8.0, 3 mM Mn2+

661360

6.3.1.2

100

-

pH 8.5, 30 mM Mg2+

661360

6.3.1.2

2 entries

K_i Value (5 results)

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Show KI Value (5 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.3.17

26

-

pH 8.0, 25°C

654371

1.4.3.10

3.4

-

-

395447

1.8.3.4

1.4

-

-

395101

2.1.1.249

4.5

-

pH 7.0, 37°C

717558

3.4.19.6

0.01084

-

-

667505

IC₅₀ Value (2 results)

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Show IC50 Value (2 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

2.7.10.1

0.000104

-

-

691283

2.7.10.1

0.000189

-

-

691283

2.7.10.1

2 entries

References & Links

Literature References (134)

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Show Reference (134 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

1399

5800436

gamma-Glutamylamide. A new intermediate in the metabolism of methylamine

1969

Kung, H.F.; Wagner, C.

J. Biol. Chem.

244

4136-4140

1400

17409

The demonstration of two discrete enzymes catalyzing the synthesis of glutamine and gamma-glutamylmethylamide in the Pseudomonas MS

1977

Levitch, M.E.

Biochem. Biophys. Res. Commun.

76

609-614

1401

907146

An assay for the enzymatic synthesis of gamma-glutamylmethylamide

1977

Levitch, M.E.

Anal. Biochem.

82

463-467

3432

1643048

Activity and spectroscopic properties of the Escherichia coli glutamate 1-semialdehyde aminotransferase and the putative active site mutant K265R

1992

Ilag, L.L.; Jahn, D.

Biochemistry

31

7143-7151

6046

3275662

Diaminopropionate ammonia-lyase from Salmonella typhimurium. Purification and characterization of the crystalline enzyme and sequence determination of the pyridoxal 5'-phosphate binding peptide

1988

Nagasawa, T.; Tanizawa, K.; Satoda, T.; Yamada, H.

J. Biol. Chem.

263

958-964

6061

-

Preparation of N-substituted aspartic acids via enantiospecific conjugate addition of N-nucleophiles to fumaric acids using methylaspartase: synthetic utility and mechanistic implications

1997

Gulzar, M.S.; Akhtar, M.; Gani, D.

J. Chem. Soc. Perkin Trans. I

1197

649-655

31045

23849

Specificity and inhibition studies of Armillaria mellea protease

1978

Lewis, W.G.; Basford, J.M.; Wlatoon, P.L.

Biochim. Biophys. Acta

522

551-560

33277

4878701

Anthranilate synthetase. Purification and properties of component I from Salmonella typhimurium

1968

Zalkin, H.; Kling, D.

Biochemistry

7

3566-3573

34516

-

The C3-N bond cleavage of 2-amino-3-(N-substituted-amino)-propionic acids catalyzed by L-mehtionine gamma-lyase

1988

Takada, H.; Esaki, N.; Tanaka, H.; Soda, K.

Agric. Biol. Chem.

52

2897-2901

36134

1238111

The mechanism of action of dipeptidyl aminopeptidase. Inhibition by amino acid derivatives and amines; activation by aromatic compounds

1975

Metrione, R.M.; MacGeorge, N.L.

Biochemistry

14

5249-5252

36618

7845202

Lysyl endopeptidase of Achromobacter lyticus

1994

Sakiyama, F.; Masaki, T.

Methods Enzymol.

244

126-137

37488

-

Purification and some properties of glutamine synthetases from Bifidobacteria

1987

Hatanaka, M.; Tachiki, T.; Furukawa, R.; Tochikura, T.

Agric. Biol. Chem.

51

425-433

81588

5126938

Specificity and mechanism of clostripain catalysis

1971

Cole, P.W.; Murakami, K.; Inagami, T.

Biochemistry

10

4246-4252

209088

5808511

The enzymatic synthesis of 5-hydroxy-N-methylpyroglutamic acid

1969

Hersh, L.B.; Tsai, L.; Stadtman, E.R.

J. Biol. Chem.

244

4677-4683

209104

5141674

Alkylamidase of sheep liver

1971

Chen, P.R.S.; Dauterman, W.C.

Biochim. Biophys. Acta

250

216-223

209122

110350

Kinetic mechanismen of the aliphatic amidase from Pseudomonas aeruginosa

1979

Woods, M.J.; Findlater, J.D.; Orsi, B.A.

Biochim. Biophys. Acta

567

225-237

209200

3732281

Purification and characterization of N,N-dimethylformamidase from Pseudomonas DMF 3/3

1986

Schär, H.P.; Holzmann, W.; Ramos Tombo, G.M.; Ghisalba, O.

Eur. J. Biochem.

158

469-475

286109

11123955

Identification of active site residues in E. coli ketopantoate reductase by mutagenesis and chemical rescue

2000

Zheng, R.; Blanchard, J.S.

Biochemistry

39

16244-16251

288888

5028495

Rat liver omega-amidase. Kinetic evidence for an acyl-enzyme intermediate

1972

Hersh, L.B.

Biochemistry

11

2251-2256

288892

5114531

Rat liver omega-amidase. Purofication and properties

1971

Hersh, L.B.

Biochemistry

10

2884-2891

288893

319948

The glutamine transaminase-omega-amidase pathway

1977

Cooper, A.J.L.; Meister, A.

CRC Crit. Rev. Biochem.

4

281-303

348600

9402752

Identification and Characterization of a catalytic base in bacterial luciferase by chemical rescue of a dark mutant

1997

Huang, S.; Tu, S.C.

Biochemistry

36

14609-14615

389907

-

Inducible or constitutive polyethylene glycol dehydrogenase involved in the aerobic metabolism of polyethylene glycol

1989

Yamanaka, H.; Kawai, F.

J. Ferment. Bioeng.

67

300-302

391526

236301

Purification and characterization of N-methylalanine dehydrogenase

1975

Lin, M.C.M.; Wagner, C.

J. Biol. Chem.

250

3746-3751

391705

12021281

Engineering the substrate specificity of D-amino-acid oxidase

2002

Sacchi, S.; Lorenzi, S.; Molla, G.; Pilone, M.S.; Rossetti, C.; Pollegioni, L.

J. Biol. Chem.

277

27510-27516

391706

12209855

Cellular and subcellular distribution of D-aspartate oxidase in human and rat brain

2002

Zaar, K.; Kost, H.P.; Schad, A.; Volkl, A.; Baumgart, E.; Fahimi, H.D.

J. Comp. Neurol.

450

272-282

391707

10209293

Purification of beef kidney D-aspartate oxidase overexpressed in Escherichia coli and characterization of its redox potentials and oxidative activity towards agonists and antagonists of excitatory amino acid receptors

1999

Negri, A.; Tedeschi, G.; Ceciliani, F.; Ronchi, S.

Biochim. Biophys. Acta

1431

212-222

391710

-

D-Aspartate oxidase and free acidic D-amino acids in fish tissues

1998

Kera, Y.; Hasegawa, S.; Watanabe, T.; Segawa, H.; Yamada, R.H.

Comp. Biochem. Physiol. B

119

95-100

391712

9163533

Structural and functional characterization of the human brain D-aspartate oxidase

1997

Setoyama, C.; Miura, R.

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