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Ligand gamma-L-Glu-aminobutanoate

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (1 result)

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Show Substrate (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

6.3.2.3

ATP + gamma-L-Glu-aminobutanoate + Gly = ADP + phosphate + ophthalmic acid

714035, 714064

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Product in Enzyme-catalyzed Reactions (3 results)

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Show Product (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

6.3.2.2

ATP + L-Glu + L-2-aminobutyrate = ADP + phosphate + gamma-L-Glu-2-aminobutyrate

651896

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6.3.2.2

ATP + L-glutamate + 2-aminobutyrate = ADP + phosphate + gamma-L-glutamyl-(2-aminobutyrate)

0

-

6.3.2.2

ATP + alpha-methyl-L-glutamate + 2-aminobutyrate = ADP + phosphate + gamma-L-glutamyl-2-aminobutyrate

0

-

6.3.2.2

3 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (6 results)

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Show Turnover Number (6 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

6.3.2.3

13.6

-

mutant V45W, pH 8.2, 37°C

714064

6.3.2.3

16.4

-

mutant V44W, pH 8.2, 37°C

714064

6.3.2.3

17.4

-

mutant V45A, pH 8.2, 37°C

714064

6.3.2.3

18.9

-

mutant V44A, pH 8.2, 37°C

714064

6.3.2.3

19.5

-

wild-type, pH 8.2, 37°C

714064

6.3.2.3

21.7

-

mutant V44A/V45A, pH 8.2, 37°C

714064

6.3.2.3

6 entries

K_M Value (9 results)

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Show KM Value (9 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

6.3.2.3

0.1

-

mutant G371V, 37°C, pH not specified in the publication

714035

6.3.2.3

0.32

-

mutant V45W, pH 8.2, 37°C

714064

6.3.2.3

0.89

-

mutant G369V, 37°C, pH not specified in the publication

714035

6.3.2.3

0.95

-

mutant V44W, pH 8.2, 37°C

714064

6.3.2.3

1.26

-

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

714035

6.3.2.3

1.42

-

mutant V44A/V45A, pH 8.2, 37°C

714064

6.3.2.3

1.42

-

wild-type, pH 8.2, 37°C

714064

6.3.2.3

1.54

-

mutant V45A, pH 8.2, 37°C

714064

6.3.2.3

1.6

-

mutant V44A, pH 8.2, 37°C

714064

6.3.2.3

9 entries

References & Links

Literature References (3)

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Show Reference (3 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

651896

9756861

Trypanosoma brucei gamma-glutamylcysteine synthetase. Characterization of the kinetic mechanism and the role of Cys-319 in cystamine inactivation

1998

Brekken, D.L.; Phillips, M.A.

J. Biol. Chem.

273

26317-26322

714035

20800579

The role of the glycine triad in human glutathione synthetase

2010

Dinescu, A.; Brown, T.R.; Barelier, S.; Cundari, T.R.; Anderson, M.E.

Biochem. Biophys. Res. Commun.

400

511-516

714064

21683691

Valine 44 and valine 45 of human glutathione synthetase are key for subunit stability and negative cooperativity

2011

Slavens, K.D.; Brown, T.R.; Barakat, K.A.; Cundari, T.R.; Anderson, M.E.

Biochem. Biophys. Res. Commun.

410

597-601

Links to other databases for gamma-L-Glu-aminobutanoate

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Show Links (1 entry)

ChEBI

PubChem

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