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show all sequences of 1.6.1.4

Purification of a flavoprotein having NADPH-cytochrome c reductase and transhydrogenase activities from Nitrobacter winogradskyi and its molecular and enzymatic properties

Kurokawa, T.; Fukumori, Y.; Yamanaka, T.; Arch. Microbiol. 148, 95-99 (1987)
No PubMed abstract available

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Nitrobacter winogradskyi
-
-
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Nitrobacter winogradskyi ATCC 14123
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-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
flavoenzyme, additionally shows NADPH-cytochrome c reductase activity, EC 1.6.2.4
288551
Nitrobacter winogradskyi
?
-
-
-
-
additional information
flavoenzyme, additionally shows NADPH-cytochrome c reductase activity, EC 1.6.2.4
288551
Nitrobacter winogradskyi ATCC 14123
?
-
-
-
-
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
288551
Nitrobacter winogradskyi
NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster
0.064 mol of NAD + is reduced per mol of enzyme per s with NADPH produced continuously by glucose-6-phosphate dehydrogenase system
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-
?
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
-
Nitrobacter winogradskyi
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
-
Nitrobacter winogradskyi
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
flavoenzyme, additionally shows NADPH-cytochrome c reductase activity, EC 1.6.2.4
288551
Nitrobacter winogradskyi
?
-
-
-
-
additional information
flavoenzyme, additionally shows NADPH-cytochrome c reductase activity, EC 1.6.2.4
288551
Nitrobacter winogradskyi ATCC 14123
?
-
-
-
-
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
288551
Nitrobacter winogradskyi
NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster
0.064 mol of NAD + is reduced per mol of enzyme per s with NADPH produced continuously by glucose-6-phosphate dehydrogenase system
-
-
?
Other publictions for EC 1.6.1.4
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)
745371
Nguyen
Two functionally distinct NAD ...
Pyrococcus furiosus
J. Biol. Chem.
292
14603-14616
2017
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1
1
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745843
Lubner
Mechanistic insights into ene ...
Pyrococcus furiosus
Nat. Chem. Biol.
13
655-659
2017
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1
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1
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741703
Tian
Ferredoxin NAD+ oxidoreductas ...
Thermoanaerobacterium saccharolyticum, Thermoanaerobacterium saccharolyticum LL1025
Appl. Environ. Microbiol.
82
7134-7141
2016
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742880
Demmer
Insights into flavin-based el ...
Thermotoga maritima, Thermotoga maritima ATCC 43589
J. Biol. Chem.
290
21985-21995
2015
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1
1
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2
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1
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742779
Lewis
Role for ferredoxin NAD(P)H o ...
Pseudomonas putida, Pseudomonas putida DSM 3601
J. Bacteriol.
195
3876-3887
2013
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1
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734518
Cho
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Improvement of hydrogen produc ...
Escherichia coli
J. Nanoelectr. Optoelectr.
6
343-347
2011
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1
1
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731998
Wang
NADP+ reduction with reduced f ...
Clostridium kluyveri, Clostridium kluyveri DSM 555
J. Bacteriol.
192
5115-5123
2010
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1
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1
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6
1
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288551
Kurokawa
-
Purification of a flavoprotein ...
Nitrobacter winogradskyi, Nitrobacter winogradskyi ATCC 14123
Arch. Microbiol.
148
95-99
1987
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