show reference and datareference onlydata only

Enzymes of a novel autotrophic carbon dioxide fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle

Data extracted from this reference:

Cofactor

Commentary

Organism

Structure

NADPH

cofactor; no activity with NADH

Chloroflexus aurantiacus

Cofactor

Commentary

Organism

Structure

NADPH

cofactor; no activity with NADH

Chloroflexus aurantiacus

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)

741539

Wilding

X-ray crystal structure of a ...

Pseudomonas sp., Pseudomonas sp. AAC

Acta Crystallogr. Sect. F

73

24-28

2017

-

-

1

1

-

-

-

-

-

-

-

4

-

3

-

-

1

-

-

-

-

-

4

1

-

-

-

-

-

-

-

1

-

-

-

-

-

1

1

1

-

-

-

-

-

-

-

-

-

4

-

-

-

1

-

-

-

-

4

1

-

-

-

-

-

-

-

-

-

-

-

-

-

-

690142

Alnouti

Tissue distribution, ontogeny, ...

Mus musculus

Toxicol. Sci.

101

51-64

2008

-

-

-

-

-

-

-

-

2

-

-

-

-

1

-

-

-

-

-

15

-

-

1

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

1

-

-

-

-

-

-

-

2

-

-

-

-

-

-

-

-

15

-

-

1

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

689379

Marchitti

Neurotoxicity and metabolism o ...

Homo sapiens

Pharmacol. Rev.

59

125-150

2007

-

-

-

-

-

-

1

-

1

-

-

-

-

1

-

-

-

-

-

2

-

-

-

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

1

-

-

-

-

1

-

-

1

-

-

-

-

-

-

-

-

2

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

288061

Strauss

Enzymes of a novel autotrophic ...

Chloroflexus aurantiacus

Eur. J. Biochem.

215

633-643

1993

-

-

-

-

-

-

-

-

-

-

-

1

-

1

-

-

-

-

-

-

-

-

2

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

1

-

-

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

-

-

2

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

288055

Goodwin

Purification and characterizat ...

Rattus norvegicus

J. Biol. Chem.

264

14965-14971

1989

-

-

-

-

-

-

1

4

1

-

2

-

-

3

-

-

1

-

-

2

1

-

2

1

-

-

-

-

1

-

-

1

-

-

-

-

-

-

1

-

-

-

-

1

-

4

1

-

2

-

-

-

-

1

-

2

1

-

2

1

-

-

-

-

1

-

-

-

-

-

-

-

-

-

288056

Waters

-

A complete pathway for beta-al ...

Pseudomonas aeruginosa

FEMS Microbiol. Lett.

34

279-282

1986

-

-

-

-

-

-

-

-

-

-

-

1

-

1

-

-

-

-

-

-

-

-

2

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

1

-

-

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

-

-

2

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

288057

Maentsaelae

-

Formation of malonate-semialde ...

Pseudomonas fluorescens

Acta Chem. Scand.

1

395-396

1972

-

-

-

-

-

-

-

-

-

-

-

1

-

1

-

-

1

-

-

-

-

-

2

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

1

-

-

-

-

-

-

-

-

-

-

1

-

-

-

1

-

-

-

-

2

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

288058

Jakoby

-

Aldehyde dehydrogenase ...

Pseudomonas sp.

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

7

203-221

1963

-

-

-

-

-

-

-

3

-

-

-

-

-

1

-

-

-

-

-

-

-

-

2

-

-

-

-

-

2

-

-

2

-

-

-

-

-

-

2

-

-

-

-

-

-

3

-

-

-

-

-

-

-

-

-

-

-

-

2

-

-

-

-

-

2

-

-

-

-

-

-

-

-

-

288059

Hayaishi

Enzymatic studies on the metab ...

Pseudomonas fluorescens

J. Biol. Chem.

236

781-790

1961

1

-

-

-

-

2

-

-

-

-

-

-

-

1

-

-

1

-

-

-

1

1

1

-

-

-

-

-

2

-

-

2

-

-

-

1

-

-

2

-

-

2

-

-

-

-

-

-

-

-

-

-

-

1

-

-

1

1

1

-

-

-

-

-

2

-

-

-

-

-

-

-

-

-

288060

Yamada

Aldehyde oxidation ...

Pseudomonas fluorescens

J. Biol. Chem.

235

589-594

1960

-

-

-

-

-

-

2

-

-

-

-

-

-

1

-

-

1

-

-

-

1

-

1

-

-

-

-

-

2

2

-

2

-

-

-

-

-

-

2

-

-

-

-

2

-

-

-

-

-

-

-

-

-

1

-

-

1

-

1

-

-

-

-

-

2

2

-

-

-

-

-

-

-

-