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Ligand L-erythrulose

Basic Ligand Information

Molecular Structure

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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

1.1.1.406

L-erythrulose + NADH = ? + NAD+

389404

-

2.7.1.209

ATP + L-erythrulose = ADP + L-erythrulose 4-phosphate

736313

-

In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.1.1.120

3-oxoisoapionate = L-erythrulose + CO2

0

-

Substrate in Enzyme-catalyzed Reactions (13 results)

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Show Substrate (13 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.10

L-erythrulose + NADPH + H+ = ? + NADP+

722271

-

1.1.1.10

L-erythrulose + NADPH = ?

656049

-

1.1.1.10

2 entries

1.1.1.14

L-erythrulose + NADH = ?

285892

-

1.1.1.406

L-erythrulose + NADH = ? + NAD+

389404

-

1.1.1.9

L-erythrulose + NADH = erythritol + NAD+

246415, 246414

-

2.2.1.1

D-ribose-5-phosphate + L-erythrulose = D-sedoheptulose 7-phosphate + glycolaldehyde

757041

-

2.2.1.1

L-erythrulose + D-ribose-5-phosphate = D-sedoheptulose 7-phosphate + glycolaldehyde

735415

-

2.2.1.1

L-erythrulose + ribose 5-phosphate = ?

485991, 485994

-

2.2.1.1

3 entries

2.6.1.18

L-erythrulose + pyruvate = 2-amino-1,3,4-butanetriol + ?

672713

-

2.6.1.2

L-erythrulose + ? = 2-amino-1,3,4-butanetriol + ?

672713

-

2.7.1.17

ATP + L-erythrulose = ADP + ?

645055

-

2.7.1.209

ATP + L-erythrulose = ADP + L-erythrulose 4-phosphate

736313

-

2.7.1.210

ATP + L-erythrulose = ADP + L-erythrulose 4-phosphate

736313

-

Product in Enzyme-catalyzed Reactions (10 results)

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Show Product (10 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.9

erythritol + NAD+ = L-erythrulose + NADH

246415

-

1.1.99.21

meso-erythritol + acceptor = L-erythrulose + reduced acceptor

0

-

1.1.99.22

meso-erythritol + acceptor = L-erythrulose + reduced acceptor

0

-

2.2.1.1

beta-hydroxypyruvate + glycolaldehyde = L-erythrulose + CO2

0

-

2.2.1.1

glycolaldehyde + hydroxypyruvate = L-erythrulose + CO2

0

-

2.2.1.1

hydroxypyruvate + glycolaldehyde = L-erythrulose + ?

0

-

2.2.1.1

lithium beta-hydroxypyruvate + glycolaldehyde = L-erythrulose + ?

0

-

2.2.1.1

4 entries

4.1.1.120

3-oxoisoapionate = L-erythrulose + CO2

0

-

5.3.1.14

L-erythrose = L-erythrulose + L-threose

0

-

5.3.1.14

L-threose = L-erythrulose + L-erythrose

0

-

5.3.1.14

2 entries

Inhibitor in Enzyme-catalyzed Reactions (3 results)

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Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.2.1.1

competitive inhibition

486024

-

2.7.1.16

competitive inhibition

723743

-

2.7.1.16

competitive inhibition to L-ribulose

641013

-

2.7.1.16

2 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

1.1.1.10

0.6

-

pH 7.0, 25°C

656049

1.1.1.10

3.32

-

pH 7.0, temperature not specified in the publication

722271

1.1.1.10

23

-

pH 7.0, 25°C

656049

1.1.1.10

24

-

pH 7.0, 25°C

656049

1.1.1.10

25

-

pH 7.0, 25°C

656049

1.1.1.10

5 entries

2.7.1.209

1.79

-

pH and temperature not specified in the publication

736313

K_M Value (12 results)

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Show KM Value (12 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.10

0.17

-

pH 7.0, temperature not specified in the publication

722271

1.1.1.10

2

-

pH 7.0, 25°C

656049

1.1.1.10

2.5

-

pH 7.0, 25°C

656049

1.1.1.10

2.9

-

pH 7.0, 25°C

656049

1.1.1.10

4.8

-

pH 7.0, 25°C

656049

1.1.1.10

5.5

-

pH 7.0, 25°C

656049

1.1.1.10

6 entries

1.1.1.14

25

-

-

285892

1.1.1.406

144

-

-

389404

2.2.1.1

4.9

-

cosubstrate glyceraldehyde 3-phosphate

485991

2.2.1.1

5.2

-

at pH 7.5 and 25°C

735415

2.2.1.1

8

-

at pH 7.5 and 50°C

735415

2.2.1.1

3 entries

2.7.1.209

0.003

-

pH and temperature not specified in the publication

736313

References & Links

Literature References (16)

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Show Reference (16 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

246414

13654257

A sensitive and stereospecific enzymatic assay for xylulose

1959

Hickman, J.; Ashwell, G.

J. Biol. Chem.

234

758-761

246415

13789254

Erythritol dehydrogenase from Aerobacter aerogenes

1961

Jakoby, W.B.; Fredericks, J.

Biochim. Biophys. Acta

48

26-32

285892

9059643

Human sorbitol dehydrogenase - a secondary alcohol dehydrogenase with distinct pathophysiological roles, pH dependent kinetic studies

1996

Maret, W.

Adv. Exp. Med. Biol.

-

383-393

389404

7551050

Enzyme evolution in Rhodobacter sphaeroides: Selection of a mutant expressing a new galactitol dehydrogenase and biochemical characterization of the enzyme

1995

Schneider, K.H.; Jäkel, G.; Hoffmann, R.; Giffhorn, F.

Microbiology

141

1865-1873

485991

-

Transketolase

1961

Racker, E.

The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbäck, K. , eds. )

5

397-406

485994

14367398

Crystalline transketolase from bakers yeast: isolation and properties

1955

De La Haba, G.; Leder, I.G.; Racker, E.

J. Biol. Chem.

214

409-426

486024

-

Kinetics of overexpressed transketolase from Escherichia coli JM 107/pQR 700

1997

Gyamerah, M.; Willetts, A.J.

Enzyme Microb. Technol.

20

127-134

641013

11747300

Substrate specificity and kinetic mechanism of Escherichia coli ribulokinase

2001

Lee, L.V.; Gerratana, B.; Cleland, W.W.

Arch. Biochem. Biophys.

396

219-224

645055

-

Purification and characterization of D-xylulokinase from the pentose-fermenting yeast Pichia stipitis NCYC 1541

1992

Waites, M.J.; Flanagan, T.

Enzyme Microb. Technol.

14

975-979

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

672713

16902948

One-pot synthesis of amino-alcohols using a de-novo transketolase and beta-alanine:pyruvate transaminase pathway in Escherichia coli

2006

Ingram, C.U.; Bommer, M.; Smith, M.E.; Dalby, P.A.; Ward, J.M.; Hailes, H.C.; Lye, G.J.

Biotechnol. Bioeng.

96

559-569

722271

21477590

DHS-21, a dicarbonyl/L-xylulose reductase (DCXR) ortholog, regulates longevity and reproduction in Caenorhabditis elegans

2011

Son, l.e..T.; Ko, K.M.; Cho, J.H.; Singaravelu, G.; Chatterjee, I.; Choi, T.W.; Song, H.O.; Yu, J.R.; Park, B.J.; Lee, S.K.; Ahnn, J.

FEBS Lett.

585

1310-1316

723743

22072612

Structural insight into mechanism and diverse substrate selection strategy of L-ribulokinase

2012

Agarwal, R.; Burley, S.K.; Swaminathan, S.

Proteins

80

261-268

735415

-

Thermostable transketolase from Geobacillus stearothermophilus: Characterization and catalytic properties

2013

Abdoul-Zabar, J.; Sorel, I.; Helaine, V.; Charmantray, F.; Devamani, T.; Yi, D.; De Berardinis, V.; Louis, D.; Marliere, P.; Fessner, W.; Hecquet, L.

Adv. Synth. Catal.

355

116-128

736313

26560079

A general strategy for the discovery of metabolic pathways: D-threitol, L-threitol, and erythritol utilization in Mycobacterium smegmatis

2015

Huang, H.; Carter, M.S.; Vetting, M.W.; Al-Obaidi, N.; Patskovsky, Y.; Almo, S.C.; Gerlt, J.A.

J. Am. Chem. Soc.

137

14570-14573

757041

28880548

Transketolase A from E. coli significantly suppresses protein glycation by glycolaldehyde and glyoxal in vitro

2017

Klaus, A.; Pfirrmann, T.; Glomb, M.A.

J. Agric. Food Chem.

65

8196-8202

Links to other databases for L-erythrulose

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ChEBI

PubChem