alpha-Substituted cystines as possible substrates for cystine reductase and L-amino acid oxidase

Carroll, J.E.; Kosicki, G.W.; Thibert, R.J.; Biochim. Biophys. Acta 198, 601-603 (1970)

Data extracted from this reference:

KM Value [mM]

KM Value Maximum [mM]

Substrate

Commentary

Organism

Structure

additional information

-

additional information

-

Saccharomyces cerevisiae

0.9

-

L-cystine

-

Saccharomyces cerevisiae

Substrates

Commentary Substrates

Literature (Substrates)

Organism

Products

Commentary (Products)

Literature (Products)

Organism (Products)

Reversibility

Substrate Product ID

NADH + L-cystine

-

440356

Saccharomyces cerevisiae

NAD+ + L-cysteine

-

440356

Saccharomyces cerevisiae

?

Cofactor

Commentary

Organism

Structure

NADH

-

Saccharomyces cerevisiae

Cofactor

Commentary

Organism

Structure

NADH

-

Saccharomyces cerevisiae

KM Value [mM]

KM Value Maximum [mM]

Substrate

Commentary

Organism

Structure

additional information

-

additional information

-

Saccharomyces cerevisiae

0.9

-

L-cystine

-

Saccharomyces cerevisiae

Substrates

Commentary Substrates

Literature (Substrates)

Organism

Products

Commentary (Products)

Literature (Products)

Organism (Products)

Reversibility

ID

NADH + L-cystine

-

440356

Saccharomyces cerevisiae

NAD+ + L-cysteine

-

440356

Saccharomyces cerevisiae

?

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

Synonyms

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)

743682

Pader

Thioredoxin-related protein o ...

Homo sapiens

Proc. Natl. Acad. Sci. USA

111

6964-6969

2014

-

-

1

-

3

-

-

2

1

-

-

2

-

2

-

-

1

-

-

2

-

-

3

-

6

1

-

-

1

1

-

-

1

-

-

-

-

-

1

1

-

3

-

-

-

-

2

1

-

-

2

-

-

-

1

-

2

-

-

3

-

1

-

-

1

1

-

-

-

-

2

2

-

1

1

673491

Ondarza

The effects by neuroleptics, a ...

Acanthamoeba polyphaga, Naegleria fowleri

Exp. Parasitol.

115

41-47

2007

4

-

-

-

-

-

11

-

-

-

-

-

-

5

-

-

-

-

-

-

-

-

2

-

2

-

-

-

-

-

-

-

-

-

-

-

4

-

-

-

-

-

-

-

11

-

-

-

-

-

-

-

-

-

-

-

-

-

-

2

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

667725

Kim

Properties of the cysteine res ...

Ulva intestinalis

Biochemistry

45

5010-5018

2006

-

-

1

-

-

-

-

-

-

-

-

-

-

4

-

-

1

-

-

-

1

-

1

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

1

-

-

1

-

1

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

440354

Maresca

Cystine reductase in the dimor ...

Histoplasma capsulatum

J. Bacteriol.

135

987-992

1978

-

-

-

-

-

-

1

1

-

-

-

1

-

3

-

-

-

-

-

1

-

-

2

-

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

1

-

-

-

-

1

-

1

-

-

-

1

-

-

-

-

-

1

-

-

2

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

440356

Carroll

alpha-Substituted cystines as ...

Saccharomyces cerevisiae

Biochim. Biophys. Acta

198

601-603

1970

-

-

-

-

-

-

-

2

-

-

-

-

-

1

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

1

-

-

-

-

-

-

2

-

-

-

-

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

440355

Thibert

-

Simultaneous determination of ...

Saccharomyces cerevisiae

Mikrochim. Acta

3

615-624

1969

-

-

-

-

-

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

1

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

1

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

440353

Romano

Cystine reductase of pea seeds ...

Candida albicans, Pisum sativum, Saccharomyces cerevisiae

J. Biol. Chem.

208

409-416

1954

-

-

-

-

-

-

-

-

-

-

-

-

-

5

-

-

-

-

-

3

-

-

3

-

-

-

-

-

-

-

-

-

3

-

-

-

-

-

-

3

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-

3

-

-

3

-

-

-

-

-

-

-

-

-

-

-

-

-

-

-