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Ligand D-erythronate

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (5 results)

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Show Substrate (5 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.410

D-erythronate + NAD+ = 2-dehydro-D-erythronate + NADH + H+

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1.1.1.410

D-erythronate + NADP+ = 2-dehydro-D-erythronate + NADPH + H+

741345

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1.1.1.410

2 entries

1.1.99.22

D-erythronate + 2,6-dichlorophenolindophenol = 3-dehydro-D-erythronate + reduced 2,6-dichlorophenolindophenol

740188, 760731

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2.7.1.220

ATP + D-erythronate = ADP + 4-phospho-D-erythronate

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4.2.1.9

D-erythronate = ?

33981

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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

1.1.1.410

3

-

cosubstrate NADP+, pH 8.0, 25°C

741345

1.1.1.410

19

-

cosubstrate NAD+, pH 8.0, 25°C

741345

1.1.1.410

2 entries

2.7.1.220

16

-

pH 8.0, 25°C

743690

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

1.1.1.410

0.59

-

cosubstrate NAD+, pH 8.0, 25°C

741345

1.1.1.410

2.4

-

cosubstrate NADP+, pH 8.0, 25°C

741345

1.1.1.410

2 entries

2.7.1.220

0.081

-

pH 8.0, 25°C

743690

4.2.1.9

1.75

-

-

33981

References & Links

Literature References (5)

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Show Reference (5 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

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

740188

27849146

Membrane-bound glycerol dehydrogenase catalyzes oxidation of D-pentonates to 4-dehydro-D-pentonates, D-fructose to 5-dehydro-D-fructose, and D-psicose to 5-dehydro-D-psicose

2017

Ano, Y.; Hours, R.A.; Akakabe, Y.; Kataoka, N.; Yakushi, T.; Matsushita, K.; Adachi, O.

Biosci. Biotechnol. Biochem.

81

411-418

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

743690

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

760731

27849146

Membrane-bound glycerol dehydrogenase catalyzes oxidation of D-pentonates to 4-keto-D-pentonates, D-fructose to 5-keto-D-fructose, and D-psicose to 5-keto-D-psicose

2017

Ano, Y.; Hours, R.; Akakabe, Y.; Kataoka, N.; Yakushi, T.; Matsushita, K.; Adachi, O.

Biosci. Biotechnol. Biochem.

81

411-418

Links to other databases for D-erythronate

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Show Links (1 entry)

ChEBI

PubChem

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