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Tartrate dehydrogenase-oxalate complexes: formation of a stable analog of a reaction intermediate complex

Data extracted from this reference:

Inhibitors

Commentary

Organism

Structure

oxalate

time-dependent inhibition

Escherichia coli

KM Value [mM]

KM Value Maximum [mM]

Substrate

Commentary

Organism

Structure

0.032

-

D-malate

thio-NAD+ as coenzyme

Escherichia coli

0.049

-

D-malate

NAD+ as coenzyme

Escherichia coli

0.092

-

(+)-tartrate

thio-NAD+ as coenzyme

Escherichia coli

0.111

-

(+)-tartrate

NAD+ as coenzyme

Escherichia coli

0.83

-

(+)-tartrate

-

Escherichia coli

0.99

-

D-malate

-

Escherichia coli

1.63

-

D-malate

3-acetylpyridine-NAD+ as coenzyme

Escherichia coli

2.62

-

(+)-tartrate

3-acetylpyridine-NAD+ as coenzyme

Escherichia coli

Turnover Number Minimum [1/s]

Turnover Number Maximum [1/s]

Substrate

Commentary

Organism

Structure

0.417

-

(+)-tartrate

-

Escherichia coli

13.3

-

D-malate

-

Escherichia coli

Cofactor

Commentary

Organism

Structure

3-acetylpyridine adenine dinucleotide

APAD

Escherichia coli

3-pyridinealdehyde adenine dinucleotide

PAAD

Escherichia coli

NAD+

-

Escherichia coli

thio-NAD+

-

Escherichia coli

Cofactor

Commentary

Organism

Structure

3-acetylpyridine adenine dinucleotide

APAD

Escherichia coli

3-pyridinealdehyde adenine dinucleotide

PAAD

Escherichia coli

NAD+

-

Escherichia coli

thio-NAD+

-

Escherichia coli

Inhibitors

Commentary

Organism

Structure

oxalate

time-dependent inhibition

Escherichia coli

KM Value [mM]

KM Value Maximum [mM]

Substrate

Commentary

Organism

Structure

0.032

-

D-malate

thio-NAD+ as coenzyme

Escherichia coli

0.049

-

D-malate

NAD+ as coenzyme

Escherichia coli

0.092

-

(+)-tartrate

thio-NAD+ as coenzyme

Escherichia coli

0.111

-

(+)-tartrate

NAD+ as coenzyme

Escherichia coli

0.83

-

(+)-tartrate

-

Escherichia coli

0.99

-

D-malate

-

Escherichia coli

1.63

-

D-malate

3-acetylpyridine-NAD+ as coenzyme

Escherichia coli

2.62

-

(+)-tartrate

3-acetylpyridine-NAD+ as coenzyme

Escherichia coli

Turnover Number Minimum [1/s]

Turnover Number Maximum [1/s]

Substrate

Commentary

Organism

Structure

0.417

-

(+)-tartrate

-

Escherichia coli

13.3

-

D-malate

-

Escherichia coli

No.

1st author

Pub Med

title

organims

journal

volume

pages

year

Activating Compound

Application

Cloned(Commentary)

Crystallization (Commentary)

Engineering

General Stability

Inhibitors

KM Value [mM]

Localization

Metals/Ions

Molecular Weight [Da]

Natural Substrates/ Products (Substrates)

Organic Solvent Stability

Organism

Oxidation Stability

Posttranslational Modification

Purification (Commentary)

Reaction

Renatured (Commentary)

Source Tissue

Specific Activity [micromol/min/mg]

Storage Stability

Substrates and Products (Substrate)

Subunits

Temperature Optimum [°C]

Temperature Range [°C]

Temperature Stability [°C]

Turnover Number [1/s]

pH Optimum

pH Range

pH Stability

Cofactor

Ki Value [mM]

pI Value

IC50 Value

Activating Compound (protein specific)

Application (protein specific)

Cloned(Commentary) (protein specific)

Cofactor (protein specific)

Crystallization (Commentary) (protein specific)

Engineering (protein specific)

General Stability (protein specific)

IC50 Value (protein specific)

Inhibitors (protein specific)

Ki Value [mM] (protein specific)

KM Value [mM] (protein specific)

Localization (protein specific)

Metals/Ions (protein specific)

Molecular Weight [Da] (protein specific)

Natural Substrates/ Products (Substrates) (protein specific)

Organic Solvent Stability (protein specific)

Oxidation Stability (protein specific)

Posttranslational Modification (protein specific)

Purification (Commentary) (protein specific)

Renatured (Commentary) (protein specific)

Source Tissue (protein specific)

Specific Activity [micromol/min/mg] (protein specific)

Storage Stability (protein specific)

Substrates and Products (Substrate) (protein specific)

Subunits (protein specific)

Temperature Optimum [°C] (protein specific)

Temperature Range [°C] (protein specific)

Temperature Stability [°C] (protein specific)

Turnover Number [1/s] (protein specific)

pH Optimum (protein specific)

pH Range (protein specific)

pH Stability (protein specific)

pI Value (protein specific)

Expression

General Information

General Information (protein specific)

Expression (protein specific)

KCat/KM [mM/s]

KCat/KM [mM/s] (protein specific)

349359

Serfozo

Substrate determinants of the ...

Escherichia coli, Pseudomonas putida

Biochemistry

34

7517-7524

1995

-

-

1

-

-

-

-

13

-

-

-

-

-

2

-

-

1

-

-

-

-

-

17

-

-

-

-

-

-

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

-

13

-

-

-

-

-

-

-

1

-

-

-

-

17

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

349358

Beecher

Tartrate dehydrogenase-oxalate ...

Escherichia coli

Arch. Biochem. Biophys.

315

255-261

1994

-

-

1

-

-

-

1

8

-

-

-

-

-

1

-

-

1

1

-

-

-

-

4

-

-

-

-

2

-

-

-

4

-

-

-

-

-

1

4

-

-

-

-

1

-

8

-

-

-

-

-

-

-

1

-

-

-

-

4

-

-

-

-

2

-

-

-

-

-

-

-

-

-

-

287509

Do Nascimento

The stereospecificity of seque ...

Pseudomonas putida, Pseudomonas putida ATCC 17642

Biochem. J.

149

553-557

1975

-

-

-

-

-

-

-

-

-

-

-

-

-

2

-

-

1

-

-

-

-

-

2

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

1

-

-

-

-

2

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

349356

Kohn

-

L- and mesotartaric acid dehyd ...

Bos taurus, Pseudomonas putida, Pseudomonas sp., Pseudomonas sp. A, Rattus norvegicus

Methods Enzymol.

9

236-240

1966

1

-

-

1

-

-

-

4

2

1

-

3

-

9

-

-

1

-

-

-

1

-

5

-

-

-

-

-

2

-

-

-

-

-

-

1

-

-

-

1

-

-

-

-

-

4

2

1

-

3

-

-

-

1

-

-

1

-

5

-

-

-

-

-

2

-

-

-

-

-

-

-

-

-