BRENDA - Enzyme Database
show all sequences of 1.8.1.6

Cystine reductase in the dimorphic fungus Histoplasma capsulatum

Maresca, B.; Jacobson, E.; Medoff, G.; Kobayashi, G.; J. Bacteriol. 135, 987-992 (1978)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
p-chloromercuriphenylsulfonic acid
strong
Histoplasma capsulatum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.11
-
L-cystine
-
Histoplasma capsulatum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
NADH + L-cystine
Histoplasma capsulatum
the enzyme may provide reduced sulfhydryl groups involved in the transition of mycelium to yeast form
?
-
-
-
Organism
Organism
UniProt
Commentary
Textmining
Histoplasma capsulatum
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
additional information
the enzyme is phase specific it is not present in mycelium appears early in the transition of mycelium to yeast
Histoplasma capsulatum
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
NADH + L-cystine
-
440354
Histoplasma capsulatum
NAD+ + L-cysteine
-
440354
Histoplasma capsulatum
?
NADH + L-cystine
the enzyme may provide reduced sulfhydryl groups involved in the transition of mycelium to yeast form
440354
Histoplasma capsulatum
?
-
-
-
-
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
-
Histoplasma capsulatum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Histoplasma capsulatum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
p-chloromercuriphenylsulfonic acid
strong
Histoplasma capsulatum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.11
-
L-cystine
-
Histoplasma capsulatum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
NADH + L-cystine
Histoplasma capsulatum
the enzyme may provide reduced sulfhydryl groups involved in the transition of mycelium to yeast form
?
-
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
additional information
the enzyme is phase specific it is not present in mycelium appears early in the transition of mycelium to yeast
Histoplasma capsulatum
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
NADH + L-cystine
-
440354
Histoplasma capsulatum
NAD+ + L-cysteine
-
440354
Histoplasma capsulatum
?
NADH + L-cystine
the enzyme may provide reduced sulfhydryl groups involved in the transition of mycelium to yeast form
440354
Histoplasma capsulatum
?
-
-
-
-
Other publictions for EC 1.8.1.6
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
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1
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3
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2
1
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2
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2
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1
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2
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3
-
6
1
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1
1
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1
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1
1
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3
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2
1
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2
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1
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2
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3
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1
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1
1
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2
2
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1
1
673491
Ondarza
The effects by neuroleptics, a ...
Acanthamoeba polyphaga, Naegleria fowleri
Exp. Parasitol.
115
41-47
2007
4
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11
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5
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2
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2
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4
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11
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2
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667725
Kim
Properties of the cysteine res ...
Ulva intestinalis
Biochemistry
45
5010-5018
2006
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1
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4
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1
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1
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1
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1
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1
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1
-
1
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-
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-
-
-
-
-
-
-
-
-
440354
Maresca
Cystine reductase in the dimor ...
Histoplasma capsulatum
J. Bacteriol.
135
987-992
1978
-
-
-
-
-
-
1
1
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-
-
1
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3
-
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1
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2
-
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1
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1
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1
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1
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1
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1
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2
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440356
Carroll
alpha-Substituted cystines as ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
198
601-603
1970
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2
-
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-
-
-
1
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-
1
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1
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1
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2
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1
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440355
Thibert
-
Simultaneous determination of ...
Saccharomyces cerevisiae
Mikrochim. Acta
3
615-624
1969
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1
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1
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1
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1
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1
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440353
Romano
Cystine reductase of pea seeds ...
Candida albicans, Pisum sativum, Saccharomyces cerevisiae
J. Biol. Chem.
208
409-416
1954
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5
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3
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3
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3
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3
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3
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3
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