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Ligand L-threonic acid

Basic Ligand Information

Molecular Structure

Related pathways

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Roles as Enzyme Ligand

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

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Show Natural Substrate (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.129

L-threonate + NAD+ = 3-dehydro-L-threonate + NADH

285825

-

1.1.1.411

L-threonate + NAD+ = 3-dehydro-L-erythronate + NADH + H+

762717

-

Substrate in Enzyme-catalyzed Reactions (7 results)

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Show Substrate (7 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.129

L-threonate + NAD+ = 3-dehydro-L-threonate + NADH

285825

-

1.1.1.411

L-threonate + NAD+ = 2-dehydro-L-erythronate + NADH + H+

741345, 762717

-

1.1.1.411

L-threonate + NAD+ = 3-dehydro-L-erythronate + NADH + H+

762717

-

1.1.1.411

L-threonate + NADP+ = 2-dehydro-L-erythronate + NADPH + H+

741345

-

1.1.1.45

L-threonate + ? = ?

669147

-

1.1.1.45

L-threonic acid + NAD+ = ?

286905

-

1.1.1.411

3 entries

1.1.1.45

2 entries

4.2.1.9

L-threonate = ?

33981, 730702

-

Inhibitor in Enzyme-catalyzed Reactions (4 results)

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Show Inhibitors (4 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.10

50% inhibition at 0.75 mM

656049

-

1.1.1.10

50% inhibition at 1.5 mM

656049

-

1.1.1.10

50% inhibition at 1.9 mM

656049

-

1.1.1.10

3 entries

4.2.1.32

K-salt of

5653

-

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

1.1.1.411

2.2

-

cosubstrate NADP+, pH 8.0, 25°C

741345

1.1.1.411

4.2

-

pH 8.0, 25°C

762717

1.1.1.411

4.7

-

cosubstrate NADP+, pH 8.0, 25°C

741345

1.1.1.411

20

-

pH 8.0, 25°C

762717

1.1.1.411

29

-

cosubstrate NAD+, pH 8.0, 25°C

741345

1.1.1.411

54

-

cosubstrate NAD+, pH 8.0, 25°C

741345

1.1.1.411

6 entries

K_M Value (10 results)

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Show KM Value (10 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.411

0.13

-

cosubstrate NAD+, pH 8.0, 25°C

741345

1.1.1.411

0.3

-

cosubstrate NADP+, pH 8.0, 25°C

741345

1.1.1.411

0.35

-

cosubstrate NAD+, pH 8.0, 25°C

741345

1.1.1.411

0.97

-

cosubstrate NADP+, pH 8.0, 25°C

741345

1.1.1.411

1

-

pH 8.0, 25°C

762717

1.1.1.411

1.19

-

pH 8.0, 25°C

762717

1.1.1.45

1.2

-

at pH 8.5, recombinant rabbit GDH

669147

1.1.1.45

2.9

-

at pH 8.5, rabbit liver GDH

669147

4.2.1.9

0.65

-

-

33981

4.2.1.9

10.1

-

pH 8, 22°C

730702

1.1.1.411

6 entries

1.1.1.45

2 entries

4.2.1.9

2 entries

References & Links

Literature References (10)

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Show Reference (10 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

5653

14342293

Tartaric acid metabolism

1965

Hurlbert, R.E.; Jakoby, W.B.

J. Biol. Chem.

240

2772-2777

33981

7648198

Conversion of aldonic acids to their corresponding 2-keto-3-deoxy-analogs by the non-carbohydrate enzyme dihydroxy acid dehydratase (DHAD)

1995

Limberg, G.; Klaffke, W.; Thiem, J.

Bioorg. Med. Chem.

3

487-494

285825

14154441

L-threonic acid dehydrogenase: Purification and properties

1964

Aspen, A.J.; Jakoby, W.B.

J. Biol. Chem.

239

710-713

286905

-

Purification and properties of beta-L-hydroxy acid dehydrogenase

1961

Smiley, J.D.; Ashwell, G.

J. Biol. Chem.

236

357-364

656049

11882650

Molecular characterization of mammalian dicarbonyl/L-xylulose reductase and its localization in kidney

2002

Nakagawa, J.; Ishikura, S.; Asami, J.; Isaji, T.; Usami, N.; Hara, A.; Sakurai, T.; Tsuritani, K.; Oda, K.; Takahashi, M.; Yoshimoto, M.; Otsuka, N.; Kitamura, K.

J. Biol. Chem.

277

17888-17891

669147

15809331

Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase

2005

Ishikura, S.; Usami, N.; Araki, M.; Hara, A.

J. Biochem.

137

303-314

730702

23028460

The Aspergillus fumigatus dihydroxyacid dehydratase Ilv3A/IlvC is required for full virulence

2012

Oliver, J.D.; Kaye, S.J.; Tuckwell, D.; Johns, A.E.; Macdonald, D.A.; Livermore, J.; Warn, P.A.; Birch, M.; Bromley, M.J.

PLoS ONE

7

e43559

741345

27402745

Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars

2016

Zhang, X.; Carter, M.; Vetting, M.; Francisco, B.; Zhao, S.; Al-Obaidi, N.; Solbiati, J.; Thiaville, J.; Crecy-Lagard, V.; Jacobson, M.; Almo, S.; Gerlt, J.

Proc. Natl. Acad. Sci. USA

113

E4161-E4169

762717

32569553

Substrate diversity of L-threonic acid dehydrogenase homologs

2020

Zhang, C.F.; Liu, Y.P.; Wu, X.X.; Zhang, X.S.; Huang, H.

Biochemistry (Moscow)

85

463-471

762717

32569553

Substrate diversity of L-threonic acid dehydrogenase homologs

2020

Zhang, C.F.; Liu, Y.P.; Wu, X.X.; Zhang, X.S.; Huang, H.

Biochemistry (Moscow)

85

463-471

762717

2 entries

Links to other databases for L-threonic acid

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Show Links (1 entry)