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Ligand (2R)-propyl-(3S)-methylmalate

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (2 results)

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Show Substrate (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.1.3.1

(2R)-propyl-(3S)-methyl malate = 4-methyl-2-oxopentanoate + propanoate

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4.1.3.32

(2R)-propyl-(3S)-methylmalate = ?

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Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (3 results)

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Show Turnover Number (3 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

4.1.3.32

0.79

-

-

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4.1.3.32

0.79

-

wild type enzyme, at pH 7.5 and 25°C

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4.1.3.32

0.79

-

wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)

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4.1.3.32

3 entries

K_M Value (4 results)

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Show KM Value (4 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

4.1.3.1

0.098

-

pH 7.5, 25°C

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4.1.3.32

2.7

-

-

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4.1.3.32

2.7

-

wild type enzyme, at pH 7.5 and 25°C

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4.1.3.32

2.7

-

wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)

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4.1.3.32

3 entries

References & Links

Literature References (2)

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Show Reference (2 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

664083

16342929

Diversity of function in the isocitrate lyase enzyme superfamily: the Dianthus caryophyllus petal death protein cleaves alpha-keto and alpha-hydroxycarboxylic acids

2005

Lu, Z.; Feng, X.; Song, L.; Han, Y.; Kim, A.; Herzberg, O.; Woodson, W.R.; Martin, B.M.; Mariano, P.S.; Dunaway-Mariano, D.

Biochemistry

44

16365-16376

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19133276

Structure and function of 2,3-dimethylmalate lyase, a PEP mutase/isocitrate lyase superfamily member

2009

Narayanan, B.; Niu, W.; Joosten, H.J.; Li, Z.; Kuipers, R.K.; Schaap, P.J.; Dunaway-Mariano, D.; Herzberg, O.

J. Mol. Biol.

386

486-503

Links to other databases for (2R)-propyl-(3S)-methylmalate

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Show Links (1 entry)

ChEBI

PubChem

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