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Ligand S-methyl-L-cysteine

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.3.1.10

S-methyl-L-cysteine = ?

6035

-

Substrate in Enzyme-catalyzed Reactions (60 results)

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Show Substrate (60 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.11.45

(S)-methyl-L-cysteine + 2-oxoglutarate + O2 = S-methyl-L-cysteine (S)-sulfoxide + succinate + CO2

730987

-

1.14.16.1

(S)-methyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2 = (S)-methyl-L-cysteine S-oxide + dihydrobiopterin + H2O

699746

-

1.14.16.1

S-methyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2 = S-methyl-L-cysteine S-oxide + dihydrobiopterin + H2O

699235

-

1.14.16.1

S-methyl-L-cysteine + O2 = ?

697830

-

1.14.16.1

S-methyl-L-cysteine + tetrahydrobiopterin + O2 = ?

438714

-

1.14.16.1

S-methyl-L-cysteine + tetrahydrobiopterin + O2 = S-methyl-L-cysteine S-oxide + dihydrobiopterin + H2O

658533

-

1.4.1.9

L-S-methylcysteine + H2O + NAD+ = 3-methylthio-2-oxopropionate + NH3 + NADH

349682

-

1.4.1.9

S-methyl-L-cysteine + H2O + NAD+ = 3-methylthio-2-oxopropanoate + NH3 + NADH

656565

-

1.14.16.1

5 entries

1.4.1.9

2 entries

2.3.2.2

5-L-glutamylaniline + S-methyl-L-cysteine = aniline + 5-L-glutamyl-S-methyl-L-cysteine

487954

-

2.6.1.14

2-oxosuccinamic acid + L-methylcysteine = L-asparagine + ?

637253

-

2.6.1.15

glyoxylate + S-methyl-L-cysteine = glycine + 3-methylsulfanyl-2-oxopropanoate

639901, 639898

-

2.6.1.42

S-methyl-L-cysteine + 2-oxoglutarate = 3-(methylthio)-2-oxopropanoic acid + L-glutamate

639995

-

2.6.1.64

S-methyl-L-cysteine + glyoxylate = 3-methylsulfanyl-2-oxopropanoate + glycine

639901

-

2.6.1.64

S-methyl-L-cysteine + phenylpyruvate = 3-methylsulfanyl-2-oxopropanoate + L-phenylalanine

639901, 640172

-

2.6.1.64

2 entries

2.6.1.73

S-methyl-L-cysteine + glyoxylate = 3-methylsulfanyl-2-oxopropanoate + glycine

636989

-

4.1.1.57

S-Methyl-L-Cys = 2-Methylthioethanamine + CO2

4721

-

4.1.1.57

S-methyl-L-cysteine = 2-methylthioethanamine + CO2

748128

-

4.1.1.57

2 entries

4.1.1.64

2-Oxobutanoate + S-methyl-L-Cys = ?

4748

-

4.1.99.1

5-hydroxyindole + S-methyl-L-Cys = 5-hydroxy-L-Trp + ?

37352

-

4.1.99.1

5-methylindole + S-methyl-L-Cys = 5-methyl-L-Trp + ?

37352

-

4.1.99.1

indole + S-methyl-L-Cys = L-Trp + ?

37352, 37356

-

4.1.99.1

S-methyl-L-Cys + H2O = ?

37341, 37363, 37352, 37334, 37337, 37349

-

4.1.99.1

S-methyl-L-Cys + H2O = methanethiol + pyruvate + NH4+

713955

-

4.1.99.1

S-methyl-L-Cys + H2O = pyruvate + NH4+ + methanethiol

664234

-

4.1.99.1

S-methyl-L-Cys + indole = Trp + ?

37335, 37337, 37341

-

4.1.99.1

S-methyl-L-cysteine + H2O = ?

705579

-

4.1.99.1

S-methyl-L-cysteine + H2O = methanethiol + pyruvate + NH3

746742, 747245, 746778

-

4.1.99.1

S-methyl-L-cysteine + H2O = methanethiol + pyruvate + NH4+

715059

-

4.1.99.1

S-methyl-L-cysteine = ?

653815

-

4.1.99.2

S-methyl-L-Cys + H2O = ? + pyruvate + NH3

33465, 33458, 678401, 33462, 33471, 33454, 33456

-

4.1.99.2

S-methyl-L-cysteine + H2O = ?

651817

-

4.1.99.2

S-methyl-L-cysteine + H2O = methanethiol + pyruvate + NH3

746892

-

4.1.99.2

S-methyl-L-cysteine + H2O = methanthiol + pyruvate + NH3

747667

-

4.1.99.2

S-methyl-L-cysteine = ?

653702, 653815, 649731

-

4.1.99.2

S-methyl-L-cysteine = ? + pyruvate + NH3

678212

-

4.1.99.1

11 entries

4.1.99.2

6 entries

4.2.1.22

S-Methyl-L-cysteine + DL-homocysteine = ?

5594

-

4.3.1.10

S-methyl L-cysteine = ?

6035

-

4.3.1.10

S-methyl-L-cysteine = ?

6035

-

4.4.1.1

S-methyl-L-Cys = ?

34487, 586904

-

4.4.1.1

S-methyl-L-cysteine + H2O = NH3 + pyruvate + methyl mercaptan

653162

-

4.4.1.11

S-methyl-L-cysteine + 2-mercaptoethanol = ?

729426

-

4.4.1.11

S-methyl-L-cysteine + H2O = ?

701880

-

4.4.1.11

S-methyl-L-cysteine + H2O = methanethiol + NH3 + 2-oxopropanoate

678355, 662034, 747207, 747211, 691377

-

4.4.1.11

S-methyl-L-cysteine + H2O = pyruvate + NH3 + CH3SH

34518, 34520, 34534

-

4.4.1.11

S-methyl-L-cysteine = ?

650615

-

4.4.1.11

S-methylcysteine + H2O = ?

701880

-

4.4.1.13

(S)-methylcysteine + H2O = methanethiol + pyruvate + NH3

708804

-

4.4.1.13

S-methyl-L-Cys + H2O = ?

34712

-

4.4.1.13

S-methyl-L-cysteine + H2O = ?

713846, 651551

-

4.4.1.13

S-methyl-L-cysteine = methyl mercaptane + pyruvate + NH3

34681, 34679, 34678, 34677, 34685

-

4.4.1.13

S-methylcysteine + H2O = ?

664205

-

4.3.1.10

2 entries

4.4.1.1

2 entries

4.4.1.11

6 entries

4.4.1.13

5 entries

4.4.1.28

S-methyl-L-cysteine + H2O = sulfide + ?

730534

-

4.4.1.35

S-methyl L-cysteine + H2O = ?

651551

-

4.4.1.4

S-methyl-L-Cys = ?

34609

-

4.4.1.4

S-methyl-L-cysteine + H2O = methanethiol + NH3 + 2-oxopropanoate

747211

-

4.4.1.4

S-methyl-L-cysteine = ?

728940

-

4.4.1.4

3 entries

5.1.1.10

S-Methyl-L-Cys = S-Methyl-D-Cys

2047, 2045

-

6.3.2.2

ATP + L-Glu + S-methyl-L-Cys = ADP + phosphate + gamma-L-Glu-L-S-methyl-Cys

652341

-

6.3.2.2

ATP + L-Glu + S-methyl-L-Cys = ADP + phosphate + gamma-L-Glu-S-methyl-L-Cys

1118

-

6.3.2.2

ATP + L-Glu + S-methyl-L-cysteine = ADP + phosphate + gamma-L-Glu-S-methyl-L-cysteine

649263

-

6.3.2.2

3 entries

Product in Enzyme-catalyzed Reactions (12 results)

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Show Product (12 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.10

S-adenosyl-L-methionine + L-cysteine = S-adenosyl-L-homocysteine + S-methyl-L-cysteine

-

-

2.1.1.280

S-adenosyl-L-methionine + L-cysteine = S-adenosyl-L-homocysteine + S-methyl-L-cysteine

-

-

2.1.1.280

S-adenosyl-L-methionine + L-cysteine = S-methyl-L-cysteine + S-adenosyl-L-homocysteine

-

-

2.5.1.47

O3-acetyl-L-serine + methylmercaptan = S-methyl-L-cysteine + acetate

-

-

2.5.1.47

O-acetyl-L-Ser + methyl mercaptan = S-methylcysteine + acetate

637350, 637353, 637354, 637326, 637327, 637347

-

2.5.1.49

O-acetyl-L-serine + H2S = S-methylcysteine + ?

637329

-

2.5.1.49

O-acetyl-L-serine + methyl mercaptan = S-methylcysteine + ?

637329

-

2.1.1.280

2 entries

2.5.1.47

2 entries

2.5.1.49

2 entries

3.5.1.14

S-methyl-N-acetyl-L-cysteine + H2O = acetate + S-methyl-L-cysteine

-

-

4.3.2.9

5-L-glutamyl-S-methyl-L-cysteine = 5-oxoproline + S-methyl-L-cysteine

487982, 487975

-

4.4.1.9

L-cysteine + methanethiol = S-methyl-L-cysteine + ?

34716, 34718

-

4.4.1.9

O-acetyl-L-serine + methylmercaptan = S-methyl-L-cysteine + acetate

652590

-

4.4.1.9

2 entries

4.5.1.5

3-chloro-L-alanine + methylmercaptan = S-methyl-L-cysteine + Cl-

648766

-

Activator in Enzyme-catalyzed Reactions (2 results)

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Show Activating Compound (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.20

-

439548

-

1.13.11.20

at 10 mM, activation

439542

-

1.13.11.20

2 entries

Inhibitor in Enzyme-catalyzed Reactions (14 results)

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Show Inhibitors (14 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.20

34% inhibition at 1 mM

439542, 439548

-

1.14.16.1

6 mM, 55% inhibition

438714

-

1.14.16.1

competitive inhibitor of the C-oxidation of L-phenylalanine

699235

-

1.14.16.1

competitive to L-phenylalanine, 5 mM, 89% residual activity with substrate L-phenylalanine

658533

-

1.14.16.1

3 entries

2.1.1.228

-

721029

-

2.3.1.30

competitive against O-acetyl-L-serine, noncompetitive against CoA

486761

-

2.3.1.30

competitive versus O-acetyl-L-serine and competitive versus CoA

657672

-

2.3.1.30

2 entries

2.5.1.47

slight inhibition

637330

-

2.6.1.14

asparagine/pyruvate reaction

637253

-

4.4.1.13

substrate inhibition, when concentration exceeds 10 mM

34677

-

6.1.1.16

competitive

192

-

6.3.5.4

-

1713

-

7.4.2.12

enzyme YtmJKLMN shows 73% inhibition at 0.05 mM

750948

-

7.4.2.12

moderately inhibited by S-methyl-L-cysteine

750555

-

7.4.2.12

2 entries

3D Structure of Enzyme-Ligand-Complex (PDB) (281 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (281 entries)

EC NUMBER

ENZYME 3D STRUCTURE

2.1.1.192

3rfa, 3D-view

2.1.1.192

5hr7, 3D-view

2.1.1.192

6fz6, 3D-view

2.1.1.192

3rfa, 3D-view

2.1.1.192

5hr7, 3D-view

2.1.1.192

6fz6, 3D-view

2.1.1.192

3rfa, 3D-view

2.1.1.192

5hr7, 3D-view

2.1.1.192

6fz6, 3D-view

2.1.1.192

3rfa, 3D-view

2.1.1.192

5hr7, 3D-view

2.1.1.192

6fz6, 3D-view

2.1.1.192

3rfa, 3D-view

2.1.1.192

5hr7, 3D-view

2.1.1.192

6fz6, 3D-view

2.1.1.192

3rfa, 3D-view

2.1.1.192

5hr7, 3D-view

2.1.1.192

6fz6, 3D-view

2.1.1.192

3rfa, 3D-view

2.1.1.192

5hr7, 3D-view

2.1.1.192

6fz6, 3D-view

2.1.1.192

3rfa, 3D-view

2.1.1.192

5hr7, 3D-view

2.1.1.192

6fz6, 3D-view

2.1.1.63

1eh7, 3D-view

2.1.1.63

4zyg, 3D-view

2.1.1.63

1eh7, 3D-view

2.1.1.63

4zyg, 3D-view

2.1.1.63

1eh7, 3D-view

2.1.1.63

4zyg, 3D-view

2.1.1.63

1eh7, 3D-view

2.1.1.63

4zyg, 3D-view

2.1.1.63

1eh7, 3D-view

2.1.1.63

4zyg, 3D-view

2.1.1.63

1eh7, 3D-view

2.1.1.63

4zyg, 3D-view

2.1.1.63

1eh7, 3D-view

2.1.1.63

4zyg, 3D-view

2.1.1.63

1eh7, 3D-view

2.1.1.63

4zyg, 3D-view

2.8.4.1

1e6y, 3D-view

2.8.4.1

3m1v, 3D-view

2.8.4.1

3m2r, 3D-view

2.8.4.1

3m2u, 3D-view

2.8.4.1

3m2v, 3D-view

2.8.4.1

3m30, 3D-view

2.8.4.1

3m32, 3D-view

2.8.4.1

3pot, 3D-view

2.8.4.1

5a0y, 3D-view

2.8.4.1

5a8k, 3D-view

2.8.4.1

5a8r, 3D-view

2.8.4.1

5a8w, 3D-view

2.8.4.1

5g0r, 3D-view

2.8.4.1

7b2h, 3D-view

2.8.4.1

1e6y, 3D-view

2.8.4.1

3m1v, 3D-view

2.8.4.1

3m2r, 3D-view

2.8.4.1

3m2u, 3D-view

2.8.4.1

3m2v, 3D-view

2.8.4.1

3m30, 3D-view

2.8.4.1

3m32, 3D-view

2.8.4.1

3pot, 3D-view

2.8.4.1

5a0y, 3D-view

2.8.4.1

5a8k, 3D-view

2.8.4.1

5a8r, 3D-view

2.8.4.1

5a8w, 3D-view

2.8.4.1

5g0r, 3D-view

2.8.4.1

7b2h, 3D-view

2.8.4.1

1e6y, 3D-view

2.8.4.1

3m1v, 3D-view

2.8.4.1

3m2r, 3D-view

2.8.4.1

3m2u, 3D-view

2.8.4.1

3m2v, 3D-view

2.8.4.1

3m30, 3D-view

2.8.4.1

3m32, 3D-view

2.8.4.1

3pot, 3D-view

2.8.4.1

5a0y, 3D-view

2.8.4.1

5a8k, 3D-view

2.8.4.1

5a8r, 3D-view

2.8.4.1

5a8w, 3D-view

2.8.4.1

5g0r, 3D-view

2.8.4.1

7b2h, 3D-view

2.8.4.1

1e6y, 3D-view

2.8.4.1

3m1v, 3D-view

2.8.4.1

3m2r, 3D-view

2.8.4.1

3m2u, 3D-view

2.8.4.1

3m2v, 3D-view

2.8.4.1

3m30, 3D-view

2.8.4.1

3m32, 3D-view

2.8.4.1

3pot, 3D-view

2.8.4.1

5a0y, 3D-view

2.8.4.1

5a8k, 3D-view

2.8.4.1

5a8r, 3D-view

2.8.4.1

5a8w, 3D-view

2.8.4.1

5g0r, 3D-view

2.8.4.1

7b2h, 3D-view

2.8.4.1

1e6y, 3D-view

2.8.4.1

3m1v, 3D-view

2.8.4.1

3m2r, 3D-view

2.8.4.1

3m2u, 3D-view

2.8.4.1

3m2v, 3D-view

2.8.4.1

3m30, 3D-view

2.8.4.1

3m32, 3D-view

2.8.4.1

3pot, 3D-view

2.8.4.1

5a0y, 3D-view

2.8.4.1

5a8k, 3D-view

2.8.4.1

5a8r, 3D-view

2.8.4.1

5a8w, 3D-view

2.8.4.1

5g0r, 3D-view

2.8.4.1

7b2h, 3D-view

2.8.4.1

1e6y, 3D-view

2.8.4.1

3m1v, 3D-view

2.8.4.1

3m2r, 3D-view

2.8.4.1

3m2u, 3D-view

2.8.4.1

3m2v, 3D-view

2.8.4.1

3m30, 3D-view

2.8.4.1

3m32, 3D-view

2.8.4.1

3pot, 3D-view

2.8.4.1

5a0y, 3D-view

2.8.4.1

5a8k, 3D-view

2.8.4.1

5a8r, 3D-view

2.8.4.1

5a8w, 3D-view

2.8.4.1

5g0r, 3D-view

2.8.4.1

7b2h, 3D-view

2.8.4.1

1e6y, 3D-view

2.8.4.1

3m1v, 3D-view

2.8.4.1

3m2r, 3D-view

2.8.4.1

3m2u, 3D-view

2.8.4.1

3m2v, 3D-view

2.8.4.1

3m30, 3D-view

2.8.4.1

3m32, 3D-view

2.8.4.1

3pot, 3D-view

2.8.4.1

5a0y, 3D-view

2.8.4.1

5a8k, 3D-view

2.8.4.1

5a8r, 3D-view

2.8.4.1

5a8w, 3D-view

2.8.4.1

5g0r, 3D-view

2.8.4.1

7b2h, 3D-view

2.8.4.1

1e6y, 3D-view

2.8.4.1

3m1v, 3D-view

2.8.4.1

3m2r, 3D-view

2.8.4.1

3m2u, 3D-view

2.8.4.1

3m2v, 3D-view

2.8.4.1

3m30, 3D-view

2.8.4.1

3m32, 3D-view

2.8.4.1

3pot, 3D-view

2.8.4.1

5a0y, 3D-view

2.8.4.1

5a8k, 3D-view

2.8.4.1

5a8r, 3D-view

2.8.4.1

5a8w, 3D-view

2.8.4.1

5g0r, 3D-view

2.8.4.1

7b2h, 3D-view

2.1.1.192

24 entries

2.1.1.63

16 entries

2.8.4.1

112 entries

3.4.23.4

1czi, 3D-view

4.1.1.39

1gk8, 3D-view

4.1.1.39

1ir2, 3D-view

4.1.1.39

1uw9, 3D-view

4.1.1.39

1uwa, 3D-view

4.1.1.39

1uzd, 3D-view

4.1.1.39

1uzh, 3D-view

4.1.1.39

2v63, 3D-view

4.1.1.39

2v67, 3D-view

4.1.1.39

2v68, 3D-view

4.1.1.39

2v69, 3D-view

4.1.1.39

2v6a, 3D-view

4.1.1.39

2vdh, 3D-view

4.1.1.39

2vdi, 3D-view

4.1.1.39

7jfo, 3D-view

4.1.1.39

7jn4, 3D-view

4.1.1.39

7jsx, 3D-view

4.1.1.39

1gk8, 3D-view

4.1.1.39

1ir2, 3D-view

4.1.1.39

1uw9, 3D-view

4.1.1.39

1uwa, 3D-view

4.1.1.39

1uzd, 3D-view

4.1.1.39

1uzh, 3D-view

4.1.1.39

2v63, 3D-view

4.1.1.39

2v67, 3D-view

4.1.1.39

2v68, 3D-view

4.1.1.39

2v69, 3D-view

4.1.1.39

2v6a, 3D-view

4.1.1.39

2vdh, 3D-view

4.1.1.39

2vdi, 3D-view

4.1.1.39

7jfo, 3D-view

4.1.1.39

7jn4, 3D-view

4.1.1.39

7jsx, 3D-view

4.1.1.39

1gk8, 3D-view

4.1.1.39

1ir2, 3D-view

4.1.1.39

1uw9, 3D-view

4.1.1.39

1uwa, 3D-view

4.1.1.39

1uzd, 3D-view

4.1.1.39

1uzh, 3D-view

4.1.1.39

2v63, 3D-view

4.1.1.39

2v67, 3D-view

4.1.1.39

2v68, 3D-view

4.1.1.39

2v69, 3D-view

4.1.1.39

2v6a, 3D-view

4.1.1.39

2vdh, 3D-view

4.1.1.39

2vdi, 3D-view

4.1.1.39

7jfo, 3D-view

4.1.1.39

7jn4, 3D-view

4.1.1.39

7jsx, 3D-view

4.1.1.39

1gk8, 3D-view

4.1.1.39

1ir2, 3D-view

4.1.1.39

1uw9, 3D-view

4.1.1.39

1uwa, 3D-view

4.1.1.39

1uzd, 3D-view

4.1.1.39

1uzh, 3D-view

4.1.1.39

2v63, 3D-view

4.1.1.39

2v67, 3D-view

4.1.1.39

2v68, 3D-view

4.1.1.39

2v69, 3D-view

4.1.1.39

2v6a, 3D-view

4.1.1.39

2vdh, 3D-view

4.1.1.39

2vdi, 3D-view

4.1.1.39

7jfo, 3D-view

4.1.1.39

7jn4, 3D-view

4.1.1.39

7jsx, 3D-view

4.1.1.39

1gk8, 3D-view

4.1.1.39

1ir2, 3D-view

4.1.1.39

1uw9, 3D-view

4.1.1.39

1uwa, 3D-view

4.1.1.39

1uzd, 3D-view

4.1.1.39

1uzh, 3D-view

4.1.1.39

2v63, 3D-view

4.1.1.39

2v67, 3D-view

4.1.1.39

2v68, 3D-view

4.1.1.39

2v69, 3D-view

4.1.1.39

2v6a, 3D-view

4.1.1.39

2vdh, 3D-view

4.1.1.39

2vdi, 3D-view

4.1.1.39

7jfo, 3D-view

4.1.1.39

7jn4, 3D-view

4.1.1.39

7jsx, 3D-view

4.1.1.39

1gk8, 3D-view

4.1.1.39

1ir2, 3D-view

4.1.1.39

1uw9, 3D-view

4.1.1.39

1uwa, 3D-view

4.1.1.39

1uzd, 3D-view

4.1.1.39

1uzh, 3D-view

4.1.1.39

2v63, 3D-view

4.1.1.39

2v67, 3D-view

4.1.1.39

2v68, 3D-view

4.1.1.39

2v69, 3D-view

4.1.1.39

2v6a, 3D-view

4.1.1.39

2vdh, 3D-view

4.1.1.39

2vdi, 3D-view

4.1.1.39

7jfo, 3D-view

4.1.1.39

7jn4, 3D-view

4.1.1.39

7jsx, 3D-view

4.1.1.39

1gk8, 3D-view

4.1.1.39

1ir2, 3D-view

4.1.1.39

1uw9, 3D-view

4.1.1.39

1uwa, 3D-view

4.1.1.39

1uzd, 3D-view

4.1.1.39

1uzh, 3D-view

4.1.1.39

2v63, 3D-view

4.1.1.39

2v67, 3D-view

4.1.1.39

2v68, 3D-view

4.1.1.39

2v69, 3D-view

4.1.1.39

2v6a, 3D-view

4.1.1.39

2vdh, 3D-view

4.1.1.39

2vdi, 3D-view

4.1.1.39

7jfo, 3D-view

4.1.1.39

7jn4, 3D-view

4.1.1.39

7jsx, 3D-view

4.1.1.39

1gk8, 3D-view

4.1.1.39

1ir2, 3D-view

4.1.1.39

1uw9, 3D-view

4.1.1.39

1uwa, 3D-view

4.1.1.39

1uzd, 3D-view

4.1.1.39

1uzh, 3D-view

4.1.1.39

2v63, 3D-view

4.1.1.39

2v67, 3D-view

4.1.1.39

2v68, 3D-view

4.1.1.39

2v69, 3D-view

4.1.1.39

2v6a, 3D-view

4.1.1.39

2vdh, 3D-view

4.1.1.39

2vdi, 3D-view

4.1.1.39

7jfo, 3D-view

4.1.1.39

7jn4, 3D-view

4.1.1.39

7jsx, 3D-view

4.1.1.39

128 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (26 results)

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Show Turnover Number (26 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

4.1.99.1

0.0051

-

pH 7.8, 37°C, mutant enzyme Y72F

664234

4.1.99.1

0.2

-

pH 8.0, 25°C

713955

4.1.99.1

0.2

-

pH 7.6, 37°C

715059

4.1.99.1

0.49

-

recombinant His-tagged wild-type enzyme, pH 7.8, 37°C

746778

4.1.99.1

0.5

-

purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37°C

705579

4.1.99.1

5

-

pH 8.0, 25°C

713955

4.1.99.2

0.000383

-

mutant enzyme Y71F

33471

4.1.99.2

0.0016

-

mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C

678401

4.1.99.2

0.0052

-

mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C

678401

4.1.99.2

0.044

-

recombinant mutant S51A, pH 8.0, 30°C

746892

4.1.99.2

0.15

-

mutant enzyme H343A

33462

4.1.99.2

0.9

-

wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C

678401

4.1.99.2

0.9

-

wild-type enzyme

33471, 33470

4.1.99.2

1.13

-

recombinant wild-type enzyme, pH 8.0, 30°C

746892

4.4.1.11

-999

-

37°C, pH 8.0

650615

4.4.1.11

0.12

-

pH 8.0, 37°C, recombinant mutant Y114F/C116H

729426

4.4.1.11

1.38

-

mutant C115A, pH 8.0, 30°C

747207

4.4.1.11

1.58

-

pH 8.0, 37°C, recombinant wild-type enzyme

729426

4.4.1.11

4.6

-

30°C, pH 8.0

678355

4.4.1.11

4.6

-

recombinant enzyme

662034

4.4.1.11

5.53

-

37°C, pH 8.0

650615

4.4.1.11

5.9

-

-

701880

4.4.1.11

5.97

-

wild-type

662034

4.4.1.11

23.08

-

mutant C115H, pH 8.0, 30°C

747207

4.4.1.11

46.3

-

pH 8.0, 37°C, recombinant mutant C166H

729426

4.1.99.1

6 entries

4.1.99.2

8 entries

4.4.1.11

11 entries

4.4.1.28

5.95

-

pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer

730534

K_M Value (54 results)

top print hide

Show KM Value (54 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.16.1

18.32

-

at 37°C, 50 mM potassium phosphate buffer, pH 6.8

699235

1.14.16.1

20.3

-

wild type enzyme, in 50 mM potassium phosphate buffer, pH 6.8, at 37°C

699746

1.14.16.1

43.25

-

at 37°C, 50 mM potassium phosphate buffer, pH 6.8

699235

1.14.16.1

43.25

-

pH 6.8, 37°C

658533

1.14.16.1

43.25

-

wild type enzyme from hepatic cytosol

697830

1.14.16.1

44.63

-

wild type enzyme from hepatic cytosol

697830

1.14.16.1

51.6

-

wild type enzyme from Hep-G2 cell cytosol

697830

1.14.16.1

7 entries

2.6.1.64

2.85

-

pH 7.0, 30°C

640172

4.1.99.1

0.18

-

pH 7.8, 37°C, mutant enzyme Y72F

664234

4.1.99.1

0.49

-

recombinant His-tagged wild-type enzyme, pH 7.8, 37°C

746778

4.1.99.1

0.87

-

pH 7.6, 37°C

715059

4.1.99.1

1.52

-

-

37356

4.1.99.1

2.04

-

purified recombinant tryptophanase in 200 mM potassium phosphate buffer (pH 7.5), at 37°C

705579

4.1.99.1

3.1

-

beta-replacement reaction

37352

4.1.99.1

5

-

alpha,beta-elimination

37349, 37352

4.1.99.1

10

-

strain B/1t7-A, 37°C

37341

4.1.99.1

12

-

-

37335

4.1.99.1

15.2

-

-

37356

4.1.99.1

16

-

pH 8.0, 25°C

653815

4.1.99.2

0.52

-

mutant enzyme Y71F

33471

4.1.99.2

1.67

-

-

33465

4.1.99.2

2.32

-

recombinant wild-type enzyme, pH 8.0, 30°C

746892

4.1.99.2

3.2

-

pH 8.0, 25°C

653815

4.1.99.2

3.4

-

wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C

678401

4.1.99.2

3.4

-

wild-type enzyme

33471, 33462

4.1.99.2

4.17

-

-

33456

4.1.99.2

5.5

-

pH 7.2, 60°C

651817

4.1.99.2

10.5

-

recombinant mutant S51A, pH 8.0, 30°C

746892

4.1.99.2

12.99

-

mutant enzyme H343A

33462

4.1.99.2

13.4

-

mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C

678401

4.1.99.2

50

-

mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C

678401

4.1.99.2

56.4

-

wild-type enzyme

33462

4.3.1.10

17.8

-

enzyme A

6035

4.3.1.10

56

-

enzyme B

6035

4.1.99.1

11 entries

4.1.99.2

13 entries

4.3.1.10

2 entries

4.4.1.1

13.13

-

pH 8.0, 37°C

653162

4.4.1.11

0.4

-

37°C, pH 8.0

650615

4.4.1.11

0.4

-

pH 8.0, 37°C, recombinant mutant Y114F/C116H

729426

4.4.1.11

0.61

-

-

701880

4.4.1.11

0.61

-

wild-type

662034

4.4.1.11

0.69

-

-

34519

4.4.1.11

0.7

-

pH 8.0, 37°C, recombinant wild-type enzyme

729426

4.4.1.11

0.71

-

30°C, pH 8.0

678355

4.4.1.11

0.71

-

recombinant enzyme

662034

4.4.1.11

0.77

-

-

34518

4.4.1.11

0.77

-

-

701880

4.4.1.11

0.8

-

mutant C115A, pH 8.0, 30°C

747207

4.4.1.11

1.4

-

-

34516

4.4.1.11

2.1

-

pH 8.0, 37°C, recombinant mutant C166H

729426

4.4.1.11

2.62

-

mutant C115H, pH 8.0, 30°C

747207

4.4.1.13

0.67

-

-

34712

4.4.1.13

2.3

-

-

34677, 34681

4.4.1.13

5.1

-

-

34685

4.4.1.13

5.3

-

-

34678, 34679

4.4.1.11

14 entries

4.4.1.13

4 entries

4.4.1.28

1.26

-

pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer

730534

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

1.13.11.20

0.75

-

-

439548

1.14.16.1

17.32

-

at 37°C, 50 mM potassium phosphate buffer, pH 6.8

699235

1.14.16.1

41.53

-

at 37°C, 50 mM potassium phosphate buffer, pH 6.8

699235

2.1.1.228

33

-

pH not specified in the publication, 37°C

721029

2.1.1.228

44

-

pH not specified in the publication, 55°C

721029

1.14.16.1

2 entries

2.1.1.228

2 entries

References & Links

Literature References (107)

top print hide

Show Reference (107 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

192

-

Specificity and kinetic properties of the cysteinyl-tRNA synthetase from rat liver

1976

Pan, F.; Yu, T.C.; Duh, G.M.; Lee, H.H.

J. Chin. Biochem. Soc.

5

45-56

1118

2895925

On the active site thiol of gamma-glutamylcysteine synthetase: relationship to catalysis, inhibition, and regulation

1988

Huang, C.S.; Moore, W.R.; Meister, A.

Proc. Natl. Acad. Sci. USA

85

2464-2468

1713

5076775

Glutamine-dependent asparagine synthetase from leukemia cells. Chloride dependence mechanism of action and inhibition

1972

Horowitz, B.; Meister, A.

J. Biol. Chem.

247

6708-6719

2045

-

Purification and characterization of amino acid racemase with very broad substrate specificity from Aeromonas caviae

1987

Inagaki, K.; Tanizawa, K.; Tanaka, H.; Soda, K.

Agric. Biol. Chem.

51

173-180

2047

8320235

A new amino acid racemase with threonine alpha-epimerase activity from Pseudomonas putida: purification and characterization

1993

Lim, Y.H.; Yokoigawa, K.; Esaki, N.; Soda, K.

J. Bacteriol.

175

4213-4217

4721

-

Purification and properties of L-methionine decarboxylase of Streptomyces sp.

1980

Misono, H.; Kawabata, Y.; Toyosato, M.; Yamamoto, T.; Soda, K.

Bull. Inst. Chem. Res. Kyoto Univ.

58

323-333

4748

-

L-Alanine-alpha-ketobutyrate aminotransferase of Pseudomonas sp.

1981

Koide, Y.; Honma, M.; Shimomura, T.

Agric. Biol. Chem.

45

775-776

5594

5121611

Specificity and some other properties of liver serine sulphhydrolase: evidence for its identity with cystathionine beta-synthase

1971

Braunstein, A.E.; Goryachenkova, E.V.; Tolosa, E.A.; Willhardt, I.H.; Yefremova, L.L.

Biochim. Biophys. Acta

242

247-260

6035

1260040

Substrate specificity of the L-serine O-sulphate degrading activities of Pseudomonas FR

1976

Tudball, N.; O'Neill, J.G.

Biochim. Biophys. Acta

429

616-623

33454

-

Elimination, replacement and isomerization reactions by intact cells containing tyrosine phenol lyase

1972

Enei, H.; Matsui, H.; Okumura, S.; Yamada, H.

Agric. Biol. Chem.

36

1869-1876

33456

-

Purification, crystallization and properties of tyrosine phenol lyase from Erwinia herbicola

1972

Kumagai, H.; Kashima, N.; Torii, H.; Yamada, H.; Enei, H.; Okumura, S.

Agric. Biol. Chem.

36

472-482

33458

4908868

Tyrosine phenol lyase. I. Purification, crystallization, and properties

1970

Kumagai, H.; Yamada, H.; Matsui, H.; Ohkishi, H.; Ogata, K.

J. Biol. Chem.

245

1767-1772

33462

7744078

Site-directed mutagenesis of His343-->Ala in Citrobacter freundii tyrosine phenol-lyase. Effects on the kinetic mechanism and rate-determining step

1995

Chen, H.; Gollnick, P.; Phillips, R.S.

Eur. J. Biochem.

229

540-549

33465

-

Purification and properties of thermostable beta-tyrosinase from an obligate symbiotic thermophile, Symbiobacterium thermophilum

1992

Suzuki, S.; Hirahara, T.; Shim, J.K.; Horinouchi, S.; Beppu, T.

Biosci. Biotechnol. Biochem.

56

84-89

33470

9174368

The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4 -hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity

1997

Sundaraju, B.; Antson, A.A.; Phillips, R.S.; Demidkina, T.V.; Barbolina, M.V.; Gollnick, P.; Dodson, G.G.; Wilson, K.S.

Biochemistry

36

6502-6510

33471

7547970

Site-directed mutagenesis of tyrosine-71 to phenylalanine in Citrobacter freundii tyrosine phenol-lyase: evidence for dual roles of tyrosine-71 as a general acid catalyst in the reaction mechanism and in cofactor binding

1995

Chen, H.Y.; Demidkina, T.V.; Phillips, R.S.

Biochemistry

34

12276-12283

34487

-

gamma-Cystathionase (Neurospora)

1971

Flavin, M.; Slaughter, C.

Methods Enzymol.

17B

433-439

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

34518

955094

Purification and properties of methioninase from Pseudomonas ovalis

1976

Tanaka, H.; Esaki, N.; Yamamoto, T.; Soda, K.

FEBS Lett.

66

307-311

34519

8440

Purification and characterization of methioninase from Pseudomonas putida

1976

Ito, S.; Nakamura, T.; Eguchi, Y.

J. Biochem.

79

1263-1272

34520

831771

Properties of L-methionine gamma-lyase from Pseudomonas ovalis

1977

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

Biochemistry

16

100-106

34534

9726878

Purification and characterization of L-methionine gamma-lyase from Brevibacterium linens BL2

1998

Dias, B.; Weimer, B.

Appl. Environ. Microbiol.

64

3327-3331

34609

-

Aliinase-like enzymes in fruiting bodies of Lentinus edodes: their purification and substrate specificity

1980

Iwami, K.; Yasumoto, K.

Agric. Biol. Chem.

44

3003-3004

34677

-

S-Alkyl-L-cysteine Lyase (Pseudomonas)

1971

Nishizuka, Y.

Methods Enzymol.

17B

470-474

34678

241329

Purification and properties of S-alkyl-L-cysteine lyase from seedlings of Acacia farnesiana Willd.

1975

Mazelis, M.; Creveling, R.K.

Biochem. J.

147

485-491

34679

1132508

The cleavage of the ether linkage of O-methyl serine by the alkyl cysteine lyase of Acacia farnesiana

1975

Mazelis, M.

FEBS Lett.

54

193-195

34681

-

S-Alkylcysteinease: Enzymatic cleavage of S-methyl-L-cysteine and its sulfoxide

1963

Nomura, J.; Nishizuta, Y.; Hayaishi, O.

J. Biol. Chem.

238

1441-1446

34685

1368609

Thermostable S-alkylcysteine alpha, beta-lyase from a thermophile: purification and properties

1990

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

Agric. Biol. Chem.

54

2069-2076

34712

8463265

Toxicity of Bordetella avium beta-cystathionase toward MC3T3-E1 osteogenic cells

1993

Gentry-Weeks, C.R.; Keith, J.M.; Thompson, J.

J. Biol. Chem.

268

7298-7314

34716

-

Purification and properties of beta-cyano-L-alanine synthase from Vicia angustifolia

1989

Ikegami, F.; Takayama, K.; Kurihara, T.; Horiuchi, S.; Tajima, C.; Shirai, R.; Murakoshi, I.

Phytochemistry

28

2285-2291

34718

-

Purification and properties of beta-cyano-L-alanine synthase from Spinacia oleracea

1988

Ikegami, F.; Takayama, K.; Tajima, Ch.; Murakoshi, I.

Phytochemistry

27

2011-2016

37334

3061452

Mechanistic deductions from multiple kinetic and solvent deuterium isotope effects and pH studies of pyridoxal phosphate dependent carbon-carbon lyases: Escherichia coli tryptophan indole-lyase

1988

Kiick, D.M.; Phillips, R.S.

Biochemistry

27

7339-7344

37335

3298983

Tryptophanase from Escherichia coli B/1t7-A

1987

Behbahani-Nejad, I.; Dye, J.L.; Suelter, C.H.

Methods Enzymol.

142

414-422

37337

6389021

Kinetics of tryptophanase inactivation/activation by sudden removal/addition of potassium ions with the aid of a crown ether or cryptand

1984

Behbahani-Nejad, I.; Suelter, C.H.; Dye, J.L.

Curr. Top. Cell. Regul.

24

219-228

37341

236639

Tryptophanase: structure, catalytic activities, and mechanism of action

1975

Snell, E.E.

Adv. Enzymol. Relat. Areas Mol. Biol.

42

287-333

37349

-

Purification, crystallization and properties of tryptophanase from Proteus rettgeri

1974

Yoshida, H.; Utagawa, T.; Kumagai, H.; Yamada, H.

Agric. Biol. Chem.

38

2065-2072

37352

-

Catalytic properties of tryptophanase from Proteus rettgeri

1974

Yoshida, H.; Kumagai, H.; Yamada, H.

Agric. Biol. Chem.

38

463-464

37356

4698211

Catalytic studies on tryptophanase from Bacillus alvei

1973

O'Neill Hoch, S.; DeMoss, R.D.

J. Bacteriol.

114

341-350

37363

1368766

Purification and properties of thermostable tryptophanase from an obligately symbiotic thermophile, Symbiobacterium thermophilum

1991

Suzuki, S.; Hirahara, T.; Horinouchi, S.; Beppu, T.

Agric. Biol. Chem.

55

3059-3066

349682

8597545

Gene cloning, purification, and characterization of thermostable and halophilic leucine dehydrogenase from a halophilic thermophile, Bacillus licheniformis TSN9

1995

Nagata, S.; Bakthavatsalam, S.; Galkin, A.G.; Asada, H.; Sakai, S.; Esaki, N.; Soda, K.; Ohshima, T.; Nagasaki, S.; Misono, H.

Appl. Microbiol. Biotechnol.

44

432-438

438714

3600372

Phenylalanine 4-monooxygenase from rat liver

1987

Kaufman, S.

Methods Enzymol.

142

3-17

439542

2821347

Cysteine dioxygenase

1987

Yamaguchi, K.; Hosokawa, Y.

Methods Enzymol.

143

395-403

439548

632231

Rat liver cysteine dioxygenase (cysteine oxidase). Further purification, characterization, and analysis of the activation and inactivation

1978

Yamaguchi, K.; Hosokawa, Y.; Kohashi, N.; Kori, Y.; Sakakibara, S.; Ueda, I.

J. Biochem.

83

479-491

486761

8117730

Kinetic mechanism of serine transacetylase from Salmonella typhimurium

1994

Leu, L.S.; Cook, P.F.

Biochemistry

33

2667-2671

487954

6030345

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Aminoacrylate intermediates in the reaction of Citrobacter freundii tyrosine phenol-lyase

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L-methionine gamma-lyase from Citrobacter freundii: cloning of the gene and kinetic parameters of the enzyme

2006

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Aspartic acid 214 in Citrobacter freundii tyrosine phenol-lyase ensures sufficient C--H-acidity of the external aldimine intermediate and proper orientation of the cofactor at the active site

2006

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The role of cysteine 116 in the active site of the antitumor enzyme L-methionine gamma-lyase from Pseudomonas putida

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Identification and molecular characterization of tryptophanase encoded by tnaA in Porphyromonas gingivalis

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Engineering Saccharomyces cerevisiae to release 3-mercaptohexan-1-ol during fermentation through overexpression of an S. cerevisiae gene, STR3, for improvement of wine aroma

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Properties of tryptophan indole-lyase from a piezophilic bacterium, Photobacterium profundum SS9

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Alliinase from Ensifer adhaerens and its use for generation of fungicidal activity

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Enzymatic synthesis of chiral amino acid sulfoxides by Fe(II)/alpha-ketoglutarate-dependent dioxygenase

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Gene cloning, recombinant expression, purification and characterization of L-methionine decarboxylase from Streptomyces sp. 590

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Links to other databases for S-methyl-L-cysteine

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