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• • Molecular Structure
  • Sum Formula
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• Roles as Enzyme Ligand
• • In Vivo Substrate
  • In Vivo Product
  • Substrate
  • Product
  • Cofactor
  • Activator
  • Inhibitor
  • Metals and Ions
  • 3D Structure (PDB)
• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
  • IC₅₀ Value
• References & Links
• • References
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Ligand S-ethyl-L-cysteine

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (28 results)

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Show Substrate (28 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.11.45

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

730987

-

1.14.16.1

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

699746

-

1.14.16.1

(S)-ethyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2 = ?

699746

-

1.14.16.1

2 entries

2.3.1.80

acetyl-CoA + S-ethyl-L-cysteine = CoA + N-acetyl-S-ethyl-L-cysteine

487545

-

4.1.1.57

S-Ethyl-L-Cys = 2-Ethylthioethanamine + CO2

4723, 4721, 4725

-

4.1.99.1

S-ethyl-L-Cys + H2O = ethanethiol + pyruvate + NH4+

713955

-

4.1.99.1

S-ethyl-L-cysteine + H2O = ?

705579

-

4.1.99.1

S-ethyl-L-cysteine + H2O = ethanethiol + pyruvate + NH3

746632, 747167

-

4.1.99.1

S-ethyl-L-cysteine + H2O = ethanethiol + pyruvate + NH4+

715059

-

4.1.99.1

S-ethyl-L-cysteine + H2O = pyruvate + NH4+ + ethanethiol

664234

-

4.1.99.1

S-ethylcysteine + H2O = ?

37341

-

4.1.99.2

S-ethyl-L-Cys + H2O = ?

33462, 33471, 664018

-

4.1.99.2

S-ethyl-L-cysteine + H2O = ?

650404

-

4.1.99.2

S-ethyl-L-cysteine + H2O = ethanethiol + pyruvate + NH3

746580, 746892

-

4.1.99.2

S-ethyl-L-cysteine = ?

653702, 649731

-

4.1.99.2

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

678212

-

4.1.99.1

6 entries

4.1.99.2

5 entries

4.3.1.10

S-ethyl-L-cysteine = ?

6035

-

4.4.1.11

S-ethyl-L-cysteine + H2O = ?

728927

3jw9, 3D-view

4.4.1.11

S-ethyl-L-cysteine + H2O = ethanethiol + NH3 + 2-oxopropanoate

678355, 662034, 747172, 747207, 747211, 691377

3jw9, 3D-view

4.4.1.11

S-ethyl-L-cysteine + H2O = ethanethiol + NH3 + pyruvate

729181

3jw9, 3D-view

4.4.1.11

S-ethyl-L-cysteine = ?

650615

3jw9, 3D-view

4.4.1.13

S-ethyl-L-cysteine + H2O = ?

651551

-

4.4.1.13

S-ethyl-L-cysteine = ?

713846

-

4.4.1.11

4 entries

4.4.1.13

2 entries

4.4.1.28

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

730534

-

4.4.1.35

S-ethyl L-cysteine + H2O = ?

651551

-

4.4.1.4

S-ethyl-L-Cys = ?

34617, 34609

-

4.4.1.4

S-ethyl-L-cysteine + H2O = ethanethiol + NH3 + 2-oxopropanoate

747211

-

4.4.1.4

S-ethyl-L-cysteine = ?

728940

-

4.4.1.4

3 entries

Product in Enzyme-catalyzed Reactions (4 results)

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Show Product (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.47

O3-acetyl-L-serine + ethylmercaptan = S-ethyl-L-cysteine + acetate

-

-

3.5.1.14

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

-

-

4.4.1.9

O-acetyl-L-serine + ethylmercaptan = S-ethyl-L-cysteine + acetate

652590

-

4.5.1.5

3-chloro-L-alanine + ethylmercaptan = S-ethyl-L-cysteine + Cl-

648766

-

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

4.4.1.5

enhances significantly glyoxalase I activity, dose-dependently 0-2 g/l, pH 6.6, 37°C

694250

-

Inhibitor in Enzyme-catalyzed Reactions (3 results)

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Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.5.1.5

noncompetitive, 50% inhibition at 0.030 mM

667932

-

3.5.1.5

noncompetitive, 50% inhibition at 0.035 mM

667932

-

3.5.1.5

2 entries

4.4.1.4

competitive

34618

-

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

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

EC NUMBER

ENZYME 3D STRUCTURE

4.4.1.11

3jw9, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (34 results)

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Show Turnover Number (34 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

4.1.99.1

0.035

-

pH 7.8, 37°C, mutant enzyme Y72F

664234

4.1.99.1

0.074

-

recombinant mutant F464A, pH 7.8, 22°C

746632

4.1.99.1

0.4

-

pH 8.0, 25°C

713955

4.1.99.1

1.79

-

pH 7.6, 37°C

715059

4.1.99.1

1.87

-

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

705579

4.1.99.1

6

-

pH 8.0, 25°C

713955

4.1.99.1

6

-

recombinant wild-type enzyme, pH 7.8, 22°C

746632

4.1.99.2

0.000217

-

mutant enzyme Y71F

33471

4.1.99.2

0.0025

-

pH 8.0, 25°C, mutant enzyme K256A

664018

4.1.99.2

0.0088

-

pH 8.0, 25°C, mutant enzyme K256H

664018

4.1.99.2

0.02

-

pH 8.0, 25°C, mutant enzyme K256R

664018

4.1.99.2

0.083

-

recombinant mutant S51A, pH 8.0, 30°C

746892

4.1.99.2

0.12

-

pH 8.0, 25°C, recombinant mutant F449A

746580

4.1.99.2

0.23

-

pH 8.0, 25°C, recombinant mutant F448L

746580

4.1.99.2

0.27

-

pH 8.0, 25°C, recombinant mutant F448H

746580

4.1.99.2

0.37

-

pH 8.0, 25°C, mutant enzyme E69D/K256R

664018

4.1.99.2

0.51

-

pH 8.0, 25°C, recombinant mutant F448A

746580

4.1.99.2

1.4

-

mutant enzyme H343A

33462

4.1.99.2

1.7

-

wild-type enzyme

33470

4.1.99.2

3.88

-

wild-type enzyme

33462

4.1.99.2

3.9

-

pH 8.0, 25°C, recombinant wild-type enzyme

746580

4.1.99.2

5.4

-

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

0.57

-

mutant C115A, pH 8.0, 30°C

747207

4.4.1.11

2.38

-

mutant Y58F, pH 8.0, 30°C

747172

4.4.1.11

5

-

30°C, pH 8.0

678355

4.4.1.11

5.03

-

recombinant enzyme

662034

4.4.1.11

5.79

-

37°C, pH 8.0

650615

4.4.1.11

6.3

-

pH 8.0, 30°C, recombinant enzyme

728927

4.4.1.11

6.5

-

mutant C115H, pH 8.0, 30°C

747207

4.4.1.11

6.8

-

wild-type

662034

4.4.1.11

7.08

-

pH 8.0, 30°C, recombinant enzyme

728927

4.4.1.11

8.05

-

pH 8.0, 30°C, recombinant enzyme

728927

4.1.99.1

7 entries

4.1.99.2

15 entries

4.4.1.11

11 entries

4.4.1.28

9.5

-

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

730534

K_M Value (25 results)

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Show KM Value (25 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.3.1.80

7.1

-

-

487545

4.1.1.57

44

-

-

4721

4.1.1.57

1000

-

-

4725

4.1.99.1

0.26

-

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

705579

4.1.99.1

0.81

-

pH 7.8, 37°C, mutant enzyme Y72F

664234

4.1.99.1

1

-

strain B/1t7-A, 25°C

37341

4.1.99.1

3.3

-

pH 7.6, 37°C

715059

4.1.99.2

0.3

-

mutant enzyme Y71F

33471

4.1.99.2

1.2

-

mutant enzyme H343A

33462

4.1.99.2

1.57

-

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

746892

4.1.99.2

5.4

-

recombinant mutant S51A, pH 8.0, 30°C

746892

4.1.99.2

6.6

-

wild-type enzyme

33462, 33471

4.1.1.57

2 entries

4.1.99.1

4 entries

4.1.99.2

5 entries

4.3.1.10

38

-

enzyme A

6035

4.4.1.11

0.17

-

30°C, pH 8.0

678355

4.4.1.11

0.17

-

pH and temperature not specified in the publication

729181

4.4.1.11

0.17

-

recombinant enzyme

662034

4.4.1.11

0.26

-

mutant C115A, pH 8.0, 30°C

747207

4.4.1.11

0.358

-

pH 8.0, 30°C, recombinant enzyme

728927

4.4.1.11

0.48

-

37°C, pH 8.0

650615

4.4.1.11

0.49

-

wild-type

662034

4.4.1.11

0.72

-

pH 8.0, 30°C, recombinant enzyme

728927

4.4.1.11

0.93

-

mutant C115H, pH 8.0, 30°C

747207

4.4.1.11

2.17

-

pH 8.0, 30°C, recombinant enzyme

728927

4.4.1.11

8.19

-

mutant Y58F, pH 8.0, 30°C

747172

4.4.1.11

11 entries

4.4.1.28

0.28

-

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

730534

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

3.5.1.5

0.011

-

pH 5.0

667932

3.5.1.5

0.014

-

pH 8.2

667932

3.5.1.5

2 entries

References & Links

Literature References (44)

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Show Reference (44 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

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

4723

2271525

Streptomyces L-methionine decarboxylase: purification and properties of the enzyme and stereochemical course of substrate decarboxylation

1990

Stevenson, D.E.; Akhtar, M.; Gani, D.

Biochemistry

29

7660-7666

4725

2271523

L-Methionine decarboxylase from Dryopteris filix-mas: purification, characterization, substrate specificity, abortive transamination of the coenzyme, and stereochemical courses of substrate decarboxylation and coenzyme transamination

1990

Stevenson, D.E.; Akhtar, M.; Gani, D.

Biochemistry

29

7631-7647

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

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

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

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

34617

-

Enzymatic cleavage of cysteine sulfoxide in Lentinus edodes

1975

Iwami, K.; Yasumoto, K.; Mitsuda, H.

Agric. Biol. Chem.

39

1947-1955

34618

17262456

Alliin lyase from garlic, Allium sativum: investigations on enzyme/substrate, enzyme/inhibitor interactions and on a new coenzyme

1989

Jansen, H.; Muller, B.; Knobloch, K.

Planta Med.

55

440-445

37341

236639

Tryptophanase: structure, catalytic activities, and mechanism of action

1975

Snell, E.E.

Adv. Enzymol. Relat. Areas Mol. Biol.

42

287-333

487545

3003508

Cysteine S-conjugate N-acetyltransferase

1985

Duffel, M.W.; Jakoby, W.B.

Methods Enzymol.

113

516-521

648766

-

S-Carboxymethylcysteine synthase from Escherichia coli

1989

Kumagai, H.; Suzuki, H.; Shigematsu, H.; Tochikura, T.

Agric. Biol. Chem.

53

2481-2487

649731

11964175

Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with L-tyrosine

2002

Demidkina, T.V.; Barbolina, M.V.; Faleev, N.G.; Sundararaju, B.; Gollnick, P.D.; Phillips, R.S.

Biochem. J.

363

745-752

650404

12686128

Structure and mechanism of tryptophan indole-lyase and tyrosine phenol-lyase

2003

Phillips, R.S.; Demidkina, T.V.; Faleev, N.G.

Biochim. Biophys. Acta

1647

167-172

650615

11193400

Role of tyrosine 114 of L-methionine gamma-lyase from Pseudomonas putida

2000

Inoue, H.; Inagaki, K.; Adachi, N.; Tamura, T.; Esaki, N.; Soda, K.; Tanaka, H.

Biosci. Biotechnol. Biochem.

64

2336-2343

651551

10794613

Biochemical characterization of cystine lyase from broccoli (Brassica oleracea var. italica)

1999

Ramirez, E.C.; Whitaker, J.R.

J. Agric. Food Chem.

47

2218-2225

652590

16233442

Purification, characterization and gene cloning of thermostable O-acetyl-L-serine sulfhydrylase forming b-cyano-L-alanine

2003

Omura, H.; Kuroda, M.; Kobayashi, M.; Shimizu, S.; Yoshida, T.; Nagasawa, T.

J. Biosci. Bioeng.

95

470-475

653702

10775663

Citrobacter freundii tyrosine phenol-lyase: the role of asparagine 185 in modulating enzyme function through stabilization of a quinonoid intermediate

2000

Barbolina, M.V.; Phillips, R.S.; Gollnick, P.D.; Faleev, N.G.; Demidkina, T.V.

Protein Eng.

13

207-215

662034

15901718

A gene encoding L-methionine gamma-lyase is present in Enterobacteriaceae family genomes: identification and characterization of Citrobacter freundii L-methionine gamma-lyase

2005

Manukhov, I.V.; Mamaeva, D.V.; Rastorguev, S.M.; Faleev, N.G.; Morozova, E.A.; Demidkina, T.V.; Zavilgelsky, G.B.

J. Bacteriol.

187

3889-3893

664018

15533046

Role of lysine-256 in Citrobacter freundii tyrosine phenol-lyase in monovalent cation activation

2004

Phillips, R.S.; Chen, H.Y.; Shim, D.; Lima, S.; Tavakoli, K.; Sundararaju, B.

Biochemistry

43

14412-14419

664234

16455316

Tryptophanase from Proteus vulgaris: The conformational rearrangement in the active site, induced by the mutation of tyrosine 72 to phenylalanine, and its mechanistic consequences

2006

Kulikova, V.V.; Zakomirdina, L.N.; Dementieva, I.S.; Phillips, R.S.; Gollnick, P.D.; Demidkina, T.V.; Faleev, N.G.

Biochim. Biophys. Acta

1764

750-757

667932

16859909

Cysteine based novel noncompetitive inhibitors of urease(s)- distinctive inhibition susceptibility of microbial and plant ureases

2006

Amtul, Z.; Kausar, N.; Follmer, C.; Rozmahel, R.F.; Atta-Ur-Rahman, R.F.; Kazmi, S.A.; Shekhani, M.S.; Eriksen, J.L.; Khan, K.M.; Choudhary, M.I.

Bioorg. Med. Chem.

14

6737-6744

678212

16878992

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

2006

Phillips, R.S.; Chen, H.Y.; Faleev, N.G.

Biochemistry

45

9575-9583

678355

16615855

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

2006

Manukhov, I.V.; Mamaeva, D.V.; Morozova, E.A.; Rastorguev, S.M.; Faleev, N.G.; Demidkina, T.V.; Zavilgelsky, G.B.

Biochemistry (Moscow)

71

361-369

691377

18603802

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

2008

Kudou, D.; Misaki, S.; Yamashita, M.; Tamura, T.; Esaki, N.; Inagaki, K.

Biosci. Biotechnol. Biochem.

72

1722-1730

694250

18720345

Antiglycative and anti-VEGF effects of s-ethyl cysteine and s-propyl cysteine in kidney of diabetic mice

2008

Lin, C.C.; Yin, M.C.

Mol. Nutr. Food Res.

52

1358-1364

699746

19126298

Human phenylalanine monooxygenase and thioether metabolism

2009

Boonyapiwat, B.; Panaretou, B.; Forbes, B.; Mitchell, S.C.; Steventon, G.B.

J. Pharm. Pharmacol.

61

63-67

705579

19246767

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

2009

Yoshida, Y.; Sasaki, T.; Ito, S.; Tamura, H.; Kunimatsu, K.; Kato, H.

Microbiology

155

968-978

713846

21478306

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

2011

Holt, S.; Cordente, A.G.; Williams, S.J.; Capone, D.L.; Jitjaroen, W.; Menz, I.R., Curtin, C.; Anderson, P.A.

Appl. Environ. Microbiol.

77

3626-3632

713955

21081107

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

2011

Phillips, R.S.; Ghaffari, R.; Dinh, P.; Lima, S.; Bartlett, D.

Arch. Biochem. Biophys.

506

35-41

715059

21658104

Molecular basis of indole production catalyzed by tryptophanase in the genus Prevotella

2011

Sasaki-Imamura, T.; Yoshida, Y.; Suwabe, K.; Yoshimura, F.; Kato, H.

FEMS Microbiol. Lett.

322

51-59

728927

24303205

Kinetic parameters and cytotoxic activity of recombinant methionine gamma-lyase from Clostridium tetani, Clostridium sporogenes, Porphyromonas gingivalis and Citrobacter freundii

2013

Morozova, E.A.; Kulikova, V.V.; Yashin, D.V.; Anufrieva, N.V.; Anisimova, N.Y.; Revtovich, S.V.; Kotlov, M.I.; Belyi, Y.F.; Pokrovsky, V.S.; Demidkina, T.V.

Acta Naturae

5

92-98

728940

21906328

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

2011

Yutani, M.; Taniguchi, H.; Borjihan, H.; Ogita, A.; Fujita, K.; Tanaka, T.

AMB Express

1

2-2

729181

21639836

Three-dimensional structures of noncovalent complexes of Citrobacter freundii methionine gamma-lyase with substrates

2011

Revtovich, S.V.; Morozova, E.A.; Khurs, E.N.; Zakomirdina, L.N.; Nikulin, A.D.; Demidkina, T.V.; Khomutov, R.M.

Biochemistry (Moscow)

76

564-570

730534

10495709

Sulfhemoglobin formation in human erythrocytes by cystalysin, an L-cysteine desulfhydrase from Treponema denticola

1999

Kurzban, G.P.; Chu, L.; Ebersole, J.L.; Holt, S.C.

Oral Microbiol. Immunol.

14

153-164

730987

-

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

2013

Hibi, M.; Kawashima, T.; Yajima, H.; Smirnov, S.; Kodera, T.; Sugiyama, M.; Shimizu, S.; Yokozeki, K.; Ogawa, J.

Tetrahedron Asymmetry

24

990-994

746580

-

Ground-state destabilization by Phe-448 and Phe-449 contributes to tyrosine phenol-lyase catalysis

2016

Phillips, R.; Vita, A.; Spivey, J.; Rudloff, A.; Driscoll, M.; Hay, S.

ACS Catal.

6

6770-6779

746632

30082510

The crystal structure of Proteus vulgaris tryptophan indole-lyase complexed with oxindolyl-L-alanine implications for the reaction mechanism

2018

Phillips, R.S.; Buisman, A.A.; Choi, S.; Hussaini, A.; Wood, Z.A.

Acta Crystallogr. Sect. D

74

748-759

746892

25758959

Construction of a novel phenol synthetic pathway in Escherichia coli through 4-hydroxybenzoate decarboxylation

2015

Miao, L.; Li, Q.; Diao, A.; Zhang, X.; Ma, Y.

Appl. Microbiol. Biotechnol.

99

5163-5173

747167

25084024

A straightforward kinetic evidence for coexistence of induced fit and selected fit in the reaction mechanism of a mutant tryptophan indole lyase Y72F from Proteus vulgaris

2014

Faleev, N.G.; Zakomirdina, L.N.; Vorobev, M.M.; Tsvetikova, M.A.; Gogoleva, O.I.; Demidkina, T.V.; Phillips, R.S.

Biochim. Biophys. Acta

1844

1860-1867

747172

25584856

The role of active site tyrosine 58 in Citrobacter freundii methionine gamma-lyase

2015

Anufrieva, N.V.; Faleev, N.G.; Morozova, E.A.; Bazhulina, N.P.; Revtovich, S.V.; Timofeev, V.P.; Tkachev, Y.V.; Nikulin, A.D.; Demidkina, T.V.

Biochim. Biophys. Acta

1854

1220-1228

747207

27430732

Engineered Citrobacter freundii methionine gamma-lyase effectively produces antimicrobial thiosulfinates

2016

Morozova, E.; Kulikova, V.; Rodionov, A.; Revtovich, S.; Anufrieva, N.; Demidkina, T.

Biochimie

128-129

92-98

747211

29803632

Non-stereoselective decomposition of (+-)-S-alk(en)yl-l-cysteine sulfoxides to antibacterial thiosulfinates catalyzed by C115H mutant methionine gamma-lyase from Citrobacter freundii

2018

Kulikova, V.; Morozova, E.; Rodionov, A.; Koval, V.; Anufrieva, N.; Revtovich, S.; Demidkina, T.

Biochimie

151

42-44

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

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ChEBI

PubChem

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