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Ligand O-succinyl-L-homoserine

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for O-succinyl-L-homoserine

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Natural Substrate (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.48

O-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate

34706, 660307, 637426, 637454, 637455, 637452, 637453, 637456, 637424, 637428, 637458, 660344, 657952

-

2.5.1.48

O-succinyl-L-homoserine + L-selenocysteine = selenocystathionine + succinate

660307

-

2.5.1.48

O4-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate

758595

-

2.5.1.48

3 entries

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.31

succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine

-

-

2.3.1.46

succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine

487045, , 487043, 487046

-

Substrate in Enzyme-catalyzed Reactions (19 results)

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Show Substrate (19 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.47

O-succinyl-L-homoserine + sulfide = ?

637383

-

2.5.1.48

O-succinyl-L-homoserine + 2-mercaptoethanol = S-ethyl-L-homocysteine + succinate

637454

-

2.5.1.48

O-succinyl-L-homoserine + beta-mercaptopropionate = S-carboxyethyl-L-homocysteine + succinate

637430

-

2.5.1.48

O-succinyl-L-homoserine + CH3SH = L-methionine + succinate

637424, 637429, 676404

-

2.5.1.48

O-succinyl-L-homoserine + D-cysteine = ?

637454

-

2.5.1.48

O-succinyl-L-homoserine + H2O = succinate + 2-oxobutyrate + NH3

637425, 637427, 637429, 637430, 637431, 637432, 637433, 637443, 637444, 637435, 687456, 637424, 637428, 702106, 704053

-

2.5.1.48

O-succinyl-L-homoserine + H2S = L-homocysteine + succinate

637424, 637429

-

2.5.1.48

O-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate

34706, 637424, 637425, 637427, 637428, 637429, 637430, 637431, 637432, 637433, 637437, 637443, 637444, 637423, 672232, 673497, 723726, 637446, 637426, 637449, 637452, 637457, 660307, 666989, 676404, 676507, 637439, 637440, 637453, 676544, 637434, 660344, 637454, 637455, 637456, 637458, 657952

-

2.5.1.48

O-succinyl-L-homoserine + L-selenocysteine = selenocystathionine + succinate

660307

-

2.5.1.48

O-succinyl-L-homoserine + sodium sulfide = L-homocysteine + sodium succinate

637454

-

2.5.1.48

O-succinyl-L-homoserine = succinate + pyruvate + NH3

657952

-

2.5.1.48

O4-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate

758595

-

2.5.1.49

O-succinyl-L-homoserine + H2S = homocysteine + ?

637834, 637839

-

2.5.1.49

O-succinyl-L-homoserine + H2S = L-homocysteine + succinate

661358

-

2.5.1.49

o-succinyl-L-homoserine + KCN = ?

662480

-

4.4.1.1

O-succinyl-L-homoserine + H2O = NH3 + ?

651810

-

4.4.1.1

O-succinyl-L-homoserine = ?

34487

-

2.5.1.48

11 entries

2.5.1.49

3 entries

4.4.1.1

2 entries

4.4.1.11

O-succinyl-L-homoserine + H2O = ?

691377

-

4.4.1.13

O-succinyl-L-homoserine + H2O = 2-oxobutyrate + succinate + NH3

690554

-

Product in Enzyme-catalyzed Reactions (2 results)

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Show Product (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.31

succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine

-

-

2.3.1.46

succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine

487045, 487043, 487044, , 487046

-

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.31

weak

486784

-

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

2.3.1.46

5.23

-

recombinant protein

487046

2.5.1.48

0.15

-

mutant R48K, pH 7.8, 25°C

723726

2.5.1.48

0.297

-

25°C, pH 9.0

687456

2.5.1.48

0.31

-

mutant S326A, pH 7.8, 25°C

723726

2.5.1.48

0.5

-

mutant R361K, pH 7.8, 25°C

723726

2.5.1.48

1.23

-

mutant D45F/E325Y, gamma-elimination, 25°C, pH 7.8

702106

2.5.1.48

1.39

-

mutant E325Y, gamma-elimination, 25°C, pH 7.8

702106

2.5.1.48

1.4

-

mutant D45F, gamma-elimination, 25°C, pH 7.8

702106

2.5.1.48

1.4

-

mutant R106A, pH 7.8, 25°C

723726

2.5.1.48

1.8

-

pH 7.8, 25°C, elimination reaction, modified ping-pong mechanism

657952

2.5.1.48

1.8

-

wild-type, gamma-elimination, 25°C, pH 7.8

702106

2.5.1.48

4

-

gamma-elimination reaction, pH 7.3, 30°C

637427

2.5.1.48

5.3

-

mutant R106K, pH 7.8, 25°C

723726

2.5.1.48

5.6

-

mutant R49A, pH 7.8, 25°C

723726

2.5.1.48

6

-

mutant Y46F, pH 7.8, 25°C

723726

2.5.1.48

9.6

-

mutant Y101F, pH 7.8, 25°C

723726

2.5.1.48

12.7

-

gamma-elimination reaction , pH 8.2, 37°C

637427

2.5.1.48

33

-

mutant N227A, pH 7.8, 25°C

723726

2.5.1.48

57

-

mutant E325Q, pH 7.8, 25°C

723726

2.5.1.48

59

-

mutant E325A, pH 7.8, 25°C

723726

2.5.1.48

63.3

-

gamma-replacement reaction, pH 8.2, 37°C

637427

2.5.1.48

79

-

mutant D45A, pH 7.8, 25°C

723726

2.5.1.48

100

-

mutant D45N, pH 7.8, 25°C

723726

2.5.1.48

112

-

wild-type, pH 7.8, 25°C

723726

2.5.1.48

117

-

pH 7.8, 25°C, replacement reaction, ordered mechanism

657952

2.5.1.48

121

-

pH 7.8, 25°C, replacement reaction, modified ping-pong mechanism

657952

2.5.1.48

130

-

mutant R49K, pH 7.8, 25°C

723726

2.5.1.48

26 entries

K_M Value (35 results)

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Show KM Value (35 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.3.1.46

3.5

-

recombinant protein

487046

2.5.1.48

0.05

-

pH 7.3, 30°C, reaction with H2S

637424

2.5.1.48

0.07

-

pH 7.3, 30°C, gamma-replacement reaction

637424

2.5.1.48

0.3

-

pH 7.3, 30°C, gamma-elimination reaction

637424

2.5.1.48

0.32

-

pH 7.5, 30°C

704053

2.5.1.48

0.33

-

pH 8.2, 25°C, gamma-elimination reaction

637444

2.5.1.48

0.7

-

mutant E325A, pH 7.8, 25°C

723726

2.5.1.48

1.1

-

mutant E325Q, pH 7.8, 25°C

723726

2.5.1.48

1.2

-

pH 7.8, 25°C, replacement reaction, ordered mechanism

657952

2.5.1.48

1.3

-

pH 7.8, 25°C, elimination reaction, modified ping-pong mechanism

657952

2.5.1.48

1.3

-

wild-type, gamma-elimination, 25°C, pH 7.8

702106

2.5.1.48

1.5

-

mutant D45F/E325Y, gamma-elimination, 25°C, pH 7.8

702106

2.5.1.48

1.7

-

mutant E325Y, gamma-elimination, 25°C, pH 7.8

702106

2.5.1.48

1.8

-

mutant R48K, pH 7.8, 25°C

723726

2.5.1.48

1.9

-

mutant Y101F, pH 7.8, 25°C

723726

2.5.1.48

2

-

mutant D45F, gamma-elimination, 25°C, pH 7.8

702106

2.5.1.48

2.1

-

mutant E325Y, gamma-replacement, 25°C, pH 7.8

702106

2.5.1.48

2.5

-

pH 7.8, 25°C, replacement reaction, modified ping-pong mechanism

657952

2.5.1.48

2.5

-

wild-type, gamma-replacement, 25°C, pH 7.8

702106

2.5.1.48

3.02

-

25°C, pH 9.0

687456

2.5.1.48

4

-

pH 7.3, 30°C, gamma-replacement reaction

637424

2.5.1.48

4.4

-

wild-type, pH 7.8, 25°C

723726

2.5.1.48

5.4

-

mutant D45F, gamma-replacement, 25°C, pH 7.8

702106

2.5.1.48

8

-

mutant N227A, pH 7.8, 25°C

723726

2.5.1.48

8

-

mutant R49K, pH 7.8, 25°C

723726

2.5.1.48

9

-

pH 7.3, 30°C, reaction wirh CH3SH

637424

2.5.1.48

11

-

mutant R106A, pH 7.8, 25°C

723726

2.5.1.48

13.34

-

pH 7.5, 30°C

637449

2.5.1.48

19

-

mutant D45A, pH 7.8, 25°C

723726

2.5.1.48

21

-

mutant S326A, pH 7.8, 25°C

723726

2.5.1.48

39

-

mutant D45N, pH 7.8, 25°C

723726

2.5.1.48

39

-

mutant R106K, pH 7.8, 25°C

723726

2.5.1.48

45.5

-

-

637440

2.5.1.48

90

-

mutant Y46F, pH 7.8, 25°C

723726

2.5.1.48

33 entries

2.5.1.49

11.1

-

-

637834

References & Links

Literature References (56)

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Show Reference (56 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

34487

-

gamma-Cystathionase (Neurospora)

1971

Flavin, M.; Slaughter, C.

Methods Enzymol.

17B

433-439

34706

3307782

Pyridoxal 5 phosphate binding site of Escherichia coli beta cystathionase and cystathionine gamma synthase comparison of their sequences

1987

Martel, A.; Bouthier de la Tour, C.; le Goffic, F.

Biochem. Biophys. Res. Commun.

147

565-571

486784

3301801

Partial purification and some properties of homoserine O-acetyltransferase of a methionine auxotroph of Saccharomyces cerevisiae

1987

Yamagata, S.

J. Bacteriol.

169

3458-3463

487043

14217349

O-Succinyl-homoserine as an intermediate in the synthesis of cystathionine by Escherichia coli

1964

Rowbury, R.J.; Woods, D.D.

J. Gen. Microbiol.

36

341-358

487044

3304182

Biological properties and mode of action of clavams

1987

Röhl, F.; Rabenhorst, J.; Zähner, H.

Arch. Microbiol.

147

315-320

487045

1729233

Regulation of the Salmonella typhimurium metA gene by the metR protein and homocysteine

1992

Mares, R.; Urbanowski, M.L.; Stauffer, G.V.

J. Bacteriol.

174

390-397

487046

10572016

Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Escherichia coli metA-encoded homoserine transsuccinylase

1999

Born, T.L.; Blanchard, J.S.

Biochemistry

38

14416-14423

637383

12005048

Cysteine synthase of an extremely thermophilic bacterium, Thermus thermophilus HB8

2002

Mizuno, Y.; Miyashita, Y.; Yamagata, S.; Iwama, T.; Akamatsu, T.

Biosci. Biotechnol. Biochem.

66

549-557

637423

12325384

Acyl derivatives of homoserine as substrates for homocysteine synthesis in Neurospora crassa, yeast and Escherichia coli

1967

Wiebers, J.L.; Garner, H.R.

J. Biol. Chem.

242

5644-5649

637424

5340123

Enzymatic synthesis of homocysteine or methionine directly from O-succinyl-homoserine

1967

Flavin, M.; Slaughter, C.

Biochim. Biophys. Acta

132

400-405

637425

5646044

Proton retention in the gamma-elimination reaction catalysed by cystathionine gamma-synthase

1968

Guggenheim, S.; Flavin, M.

Biochim. Biophys. Acta

151

664-669

637426

5781194

Inhibition of cystathionine gamma-synthase by S-adenosylmethionine: A control mechanism for methionine synthesis in Neurospora

1969

Kerr, D.; Flavin, M.

Biochim. Biophys. Acta

177

177-179

637427

4893684

Cystathionine gamma-synthase from Salmonella. Beta elimination and replacement reactions and inhibition by O-succinylserine

1969

Guggenheim, S.; Flavin, M.

J. Biol. Chem.

244

3722-3727

637428

5350958

Cystathionine gamma-synthase. A pyridoxal phosphate enzyme catalyzing rapid exchanges of beta and alpha hydrogen atoms in amino acids

1969

Guggenheim, S.; Flavin, M.

J. Biol. Chem.

244

6217-6227

637429

-

Cystathionine gamma-synthase (Salmonella)

1971

Kaplan, M.; Guggenheim, S.

Methods Enzymol.

17B

425-433

637430

5047707

Cystathionine-synthase: studies on the replacement reaction

1972

Posner B.I.

Biochim. Biophys. Acta

276

277-283

637431

5076763

Cystathionine -synthase. Studies of hydrogen exchange reactions

1972

Posner, B.I.; Flavin, M.

J. Biol. Chem.

247

6402-6411

637432

5076764

Cystathionine -synthase. The nature of intramolecular proton shifts in the elimination reaction

1972

Posner, B.I.; Flavin, M.

J. Biol. Chem.

247

6412-6419

637433

1091265

Active site-directed inactivation of cystathionine gamma-synthetase and glutamic pyruvic transaminase by propargylglycine

1975

Marcotte,P.; Walsh, C.

Biochem. Biophys. Res. Commun.

62

677-682

637434

16662678

Methionine synthesis in Lemna. Inhibition of cystathionine gamma-synthase by propargylglycine

1982

Thompson, G.A.; Datko, A.H.; Mudd, S.H.

Plant Physiol.

70

1347-1352

637435

6361021

Appendix. Purification, molecular weight, and NH2-terminal sequence of cystathionine gamma-synthase of Escherichia coli

1983

Tran, S.V.; Schaeffer, E.; Bertrand, O.; Mariuzza, R.; Ferrara, P.

J. Biol. Chem.

258

14872-14873

637437

-

Distribution to two kinds of cystathionine gamma-synthase in various bacteria

1987

Kanzaki, H.; Kobayashi, M.; Nagasawa, T.; Yamada, H.

FEMS Microbiol. Lett.

33

65-68

637439

3816790

Purification and characterization of cystathionine gamma-synthase type II from Bacillus sphaericus

1987

Kanzaki, H.; Kobayashi, M.; Nagasawa, T.; Yamada, H.

Eur. J. Biochem.

163

105-112

637440

-

Production of L-cystathionine using bacterial cystathionine gamma-synthase

1987

Kanzaki, H.; Kobayashi, M.; Nagasawa, T.; Yamada, H.

Appl. Microbiol. Biotechnol.

25

322-326

637443

2405904

Reaction mechanism of Escherichia coli cystathionine gamma-synthase: direct evidence for a pyridoxamine derivative of vinylglyoxylate as a key intermediate in pyridoxal phosphate dependent gamma-elimination and gamma-replacement reactions

1990

Brzovic, P.; Litzenberger Holbrook, E; Greene, R.C.; Dunn, M.F.

Biochemistry

29

442-451

637444

2405903

Purification and properties of cystathionine gamma-synthase from overproducing strains of Escherichia coli

1990

Litzenberger Holbrook, E.; Greene, R.C.; Heilig Krueger, J.

Biochemistry

29

435-442

637446

8511969

Cystathionine gamma-lyase of Saccharomyces cerevisiae: structural gene and cystathionine gamma-synthase activity

1993

Ono, B.I.; Ishi, N.; Naito, K.; Miyoshi, S.I.; Shinoda, S.; Yamamoto, S.; Ohmori, S.

Yeast

9

389-397

637449

7840669

Methionine biosynthesis in higher plants. I. Purification and characterization of cystathionine gamma-synthase from spinach chloroplasts

1995

Ravanel, S.; Droux, M.; Douce, R.

Arch. Biochem. Biophys.

316

572-584

637452

12121993

Identification of a short highly conserved amino acid sequence as the functional region required for posttranscriptional autoregulation of the cystathionine gamma-synthase gene in Arabidopsis

2002

Ominato, K.; Akita, H.; Suzuki, A.; Kijima, F.; Yoshino, T.; Yoshino, M.; Chiba, Y.; Onouchi, H.; Naito, S.

J. Biol. Chem.

277

36380-36386

637453

10420990

Analysis of Corynebacterium glutamicum methionine biosynthetic pathway: isolation and analysis of metB encoding cystathionine gamma-synthase: Isolation and analysis of metB encoding cystathionine gamma synthase

1999

Hwang, B.J.; Kim, Y.; Kim, H.B.; Hwang, H.J.; Kim, J.H.; Lee, H.S.

Mol. Cells

9

300-308

637454

10595588

Cloning, purification, and characterization of cystathionine g-synthase from Nicotiana tabacum

1999

Clausen, T.; Wahl, M.C.; Messerschmidt, A.; Huber, R.; Fuhrmann, J.C.; Laber, B.; Streber, W.; Steegborn, C.

Biol. Chem.

380

1237-1242

637455

11788756

Constitutive overexpression of cystathionine gamma-synthase in Arabidopsis leads to accumulation of soluble methionine and S-methylmethionine

2002

Kim, J.; Lee, M.; Chalam, R.; Martin, M.N.; Leustek, T.; Boerjan, W.

Plant Physiol.

128

95-107

637456

11842149

The N-terminal region of Arabidopsis cystathionine gamma-synthase plays an important regulatory role in methionine metabolism

2002

Hacham, Y.; Avraham, T.; Amir, R.

Plant Physiol.

128

454-462

637457

10438597

The crystal structure of cystathionine gamma-synthase from Nicotiana tabacum reveals its substrate and reaction specificity

1999

Steegborn, C.; Messerschmidt, A.; Laber, B.; Streber, W.; Huber, R.; Clausen, T.

J. Mol. Biol.

290

983-996

637458

12692344

Functional analysis of cystathionine gamma-synthase in genetically engineered potato plants

2003

Kreft, O.; Hoefgen, R.; Hesse, H.

Plant Physiol.

131

1843-1854

637834

6526818

O-Acetylhomoserine sulfhydrylase of the fission yeast Schizosaccharomyces pombe: Partial purification, characterization, and its probable role in homocysteine biosynthesis

1984

Yamagata, S.

J. Biochem.

96

1511-1523

637839

11566369

Cloning and overexpression of the oah1 gene encoding O-acetyl-L-homoserine sulfhydrylase of Thermus thermophilus HB8 and characterization of the gene product

2001

Shimizu, H.; Yamagata, S.; Masui, R.; Inoue,Y.; Shibata, T.; Yokoyama, S.; Kuramitsu, S.; Iwama, T.

Biochim. Biophys. Acta

1549

61-72

651810

14607989

Conversion of the aminocrotonate intermediate limits the rate of gamma-elimination reaction catalyzed by L-cystathionine gamma-lyase of the yeast Saccharomyces cerevisiae

2003

Yamagata, S.; Yasugahira, T.; Okuda, Y.; Iwama, T.

J. Biochem.

134

607-613

657952

14503880

Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for the elimination and substitution reactions

2003

Aitken, S.M.; Kim, D.H.; Kirsch, J.F.

Biochemistry

42

11297-11306

660307

14618405

Overexpression of cystathionine-gamma-synthase enhances selenium volatilization in Brassica juncea

2003

Van Huysen, T.; Abdel-Ghany, S.; Hale, K.L.; LeDuc, D.; Terry, N.; Pilon-Smits, E.A.

Planta

218

71-78

660344

12934018

S-adenosyl-L-methionine is an effector in the posttranscriptional autoregulation of the cystathionine gamma-synthase gene in Arabidopsis

2003

Chiba, Y.; Sakurai, R.; Yoshino, M.; Ominato, K.; Ishikawa, M.; Onouchi, H.; Naito, S.

Proc. Natl. Acad. Sci. USA

100

10225-10230

661358

15215603

Comparative characterization of the oah2 gene homologous to the oah1 of Thermus thermophilus HB8

2004

Iwama, T.; Hosokawa, H.; Lin, W.; Shimizu, H.; Kawai, K.; Yamagata, S.

Biosci. Biotechnol. Biochem.

68

1357-1361

662480

16233482

Purification, characterization and gene cloning of thermostable o-acetyl-L-homoserine sulfhydrylase forming gamma-cyano-alpha-aminobutyric acid

2003

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

J. BIOSCI. BIOENG.

96

53-58

666989

16145838

The expression level of threonine synthase and cystathionine-gamma-synthase is influenced by the level of both threonine and methionine in Arabidopsis plants

2005

Avraham, T.; Amir, R.

Transgenic Res.

14

299-311

672232

17302437

Identification of catalytic cysteine, histidine, and lysine residues in Escherichia coli homoserine transsuccinylase

2007

Ziegler, K.; Noble, S.M.; Mutumanje, E.; Bishop, B.; Huddler, D.P.; Born, T.L.

Biochemistry

46

2674-2683

673497

16708165

Purification and characterization of Thermotoga maritima homoserine transsuccinylase indicates it is a transacetylase

2006

Goudarzi, M.; Born, T.L.

Extremophiles

10

469-478

676404

17168900

Enhanced levels of methionine and cysteine in transgenic alfalfa (Medicago sativa L.) plants over-expressing the Arabidopsis cystathionine gamma-synthase gene

2005

Avraham, T.; Badani, H.; Galili, S.; Amir, R.

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676507

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Enzymatic characterization and inhibitor discovery of a new cystathionine gamma-synthase from Helicobacter pylori

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Cloning and characterization of two Lactobacillus casei genes encoding a cystathionine lyase

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Appl. Environ. Microbiol.

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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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Interconversion of a pair of active-site residues in Escherichia coli cystathionine gamma-synthase, E. coli cystathionine beta-lyase, and Saccharomyces cerevisiae cystathionine gamma-lyase and development of tools for the investigation of their mechanisms

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Farsi, A.; Lodha, P.H.; Skanes, J.E.; Los, H.; Kalidindi, N.; Aitken, S.M.

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The hyperthermophilic cystathionine gamma-synthase from the aerobic crenarchaeon Sulfolobus tokodaii expression, purification, crystallization and structural insights

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Sato, D.; Shiba, T.; Mizuno, S.; Kawamura, A.; Hanada, S.; Yamada, T.; Shinozaki, M.; Yanagitani, M.; Tamura, T.; Inagaki, K.; Harada, S.

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Links to other databases for O-succinyl-L-homoserine

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