BRENDA - Enzyme Database
show all sequences of 1.1.1.286

Characterization of two ?-decarboxylating dehydrogenases from Sulfolobus acidocaldarius

Takahashi, K.; Nakanishi, F.; Tomita, T.; Akiyama, N.; Lassak, K.; Albers, S.V.; Kuzuyama, T.; Nishiyama, M.; Extremophiles 20, 843-853 (2016)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene saci_2375, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain BL21(DE3)Codon-Plus-RIL
Sulfolobus acidocaldarius
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.011
-
homoisocitrate
pH 8.0, 60°C, recombinant enzyme
Sulfolobus acidocaldarius
0.027
-
isocitrate
pH 8.0, 60°C, recombinant enzyme
Sulfolobus acidocaldarius
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
homoisocitrate + NADP+
Sulfolobus acidocaldarius
-
2-oxoadipate + CO2 + NADPH + H+
-
-
r
homoisocitrate + NADP+
Sulfolobus acidocaldarius MW001
-
2-oxoadipate + CO2 + NADPH + H+
-
-
r
isocitrate + NADP+
Sulfolobus acidocaldarius
-
2-oxoglutarate + CO2 + NADPH
-
-
r
isocitrate + NADP+
Sulfolobus acidocaldarius MW001
-
2-oxoglutarate + CO2 + NADPH
-
-
r
additional information
Sulfolobus acidocaldarius
Saci_2375 exhibits distinct and similar activities for isocitrate and homoisocitrate, but no detectable activity for 3-isopropylmalate. Saci_2375 is a dual function enzyme serving as isocitrate-homoisocitrate dehydrogenase
?
-
-
-
additional information
Sulfolobus acidocaldarius MW001
Saci_2375 exhibits distinct and similar activities for isocitrate and homoisocitrate, but no detectable activity for 3-isopropylmalate. Saci_2375 is a dual function enzyme serving as isocitrate-homoisocitrate dehydrogenase
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sulfolobus acidocaldarius
Q4J6C9
-
-
Sulfolobus acidocaldarius MW001
Q4J6C9
-
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme from Escherichia coli strain BL21(DE3)Codon-Plus-RIL b anion exchange chromatography, ammonium sulfate fractionation, hydropobic interaction chromatography, ultrafiltration, and gel filtration
Sulfolobus acidocaldarius
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
homoisocitrate + NADP+
-
738195
Sulfolobus acidocaldarius
2-oxoadipate + CO2 + NADPH + H+
-
-
-
r
homoisocitrate + NADP+
-
738195
Sulfolobus acidocaldarius MW001
2-oxoadipate + CO2 + NADPH + H+
-
-
-
r
isocitrate + NADP+
-
738195
Sulfolobus acidocaldarius
2-oxoglutarate + CO2 + NADPH
-
-
-
r
isocitrate + NADP+
-
738195
Sulfolobus acidocaldarius MW001
2-oxoglutarate + CO2 + NADPH
-
-
-
r
additional information
Saci_2375 exhibits distinct and similar activities for isocitrate and homoisocitrate, but no detectable activity for 3-isopropylmalate. Saci_2375 is a dual function enzyme serving as isocitrate-homoisocitrate dehydrogenase
738195
Sulfolobus acidocaldarius
?
-
-
-
-
additional information
Saci_2375 exhibits distinct and similar activities for isocitrate and homoisocitrate, but no detectable activity for 3-isopropylmalate. Saci_2375 is a dual function enzyme serving as isocitrate-homoisocitrate dehydrogenase
738195
Sulfolobus acidocaldarius MW001
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
tetramer
dimer of dimers
Sulfolobus acidocaldarius
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
60
-
assay at
Sulfolobus acidocaldarius
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
37
-
homoisocitrate
pH 8.0, 60°C, recombinant enzyme
Sulfolobus acidocaldarius
61
-
isocitrate
pH 8.0, 60°C, recombinant enzyme
Sulfolobus acidocaldarius
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Sulfolobus acidocaldarius
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
Saci_2375 is an NADP+-dependent enzyme with the ability to function as ICDH, EC 1.1.1.42, and HICDH, EC 1.1.1.87
Sulfolobus acidocaldarius
NADPH
Saci_2375 is an NADP+-dependent enzyme with the ability to function as ICDH, EC 1.1.1.42, and HICDH, EC 1.1.1.87
Sulfolobus acidocaldarius
Cloned(Commentary) (protein specific)
Commentary
Organism
gene saci_2375, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain BL21(DE3)Codon-Plus-RIL
Sulfolobus acidocaldarius
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
Saci_2375 is an NADP+-dependent enzyme with the ability to function as ICDH, EC 1.1.1.42, and HICDH, EC 1.1.1.87
Sulfolobus acidocaldarius
NADPH
Saci_2375 is an NADP+-dependent enzyme with the ability to function as ICDH, EC 1.1.1.42, and HICDH, EC 1.1.1.87
Sulfolobus acidocaldarius
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.011
-
homoisocitrate
pH 8.0, 60°C, recombinant enzyme
Sulfolobus acidocaldarius
0.027
-
isocitrate
pH 8.0, 60°C, recombinant enzyme
Sulfolobus acidocaldarius
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
homoisocitrate + NADP+
Sulfolobus acidocaldarius
-
2-oxoadipate + CO2 + NADPH + H+
-
-
r
homoisocitrate + NADP+
Sulfolobus acidocaldarius MW001
-
2-oxoadipate + CO2 + NADPH + H+
-
-
r
isocitrate + NADP+
Sulfolobus acidocaldarius
-
2-oxoglutarate + CO2 + NADPH
-
-
r
isocitrate + NADP+
Sulfolobus acidocaldarius MW001
-
2-oxoglutarate + CO2 + NADPH
-
-
r
additional information
Sulfolobus acidocaldarius
Saci_2375 exhibits distinct and similar activities for isocitrate and homoisocitrate, but no detectable activity for 3-isopropylmalate. Saci_2375 is a dual function enzyme serving as isocitrate-homoisocitrate dehydrogenase
?
-
-
-
additional information
Sulfolobus acidocaldarius MW001
Saci_2375 exhibits distinct and similar activities for isocitrate and homoisocitrate, but no detectable activity for 3-isopropylmalate. Saci_2375 is a dual function enzyme serving as isocitrate-homoisocitrate dehydrogenase
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme from Escherichia coli strain BL21(DE3)Codon-Plus-RIL b anion exchange chromatography, ammonium sulfate fractionation, hydropobic interaction chromatography, ultrafiltration, and gel filtration
Sulfolobus acidocaldarius
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
homoisocitrate + NADP+
-
738195
Sulfolobus acidocaldarius
2-oxoadipate + CO2 + NADPH + H+
-
-
-
r
homoisocitrate + NADP+
-
738195
Sulfolobus acidocaldarius MW001
2-oxoadipate + CO2 + NADPH + H+
-
-
-
r
isocitrate + NADP+
-
738195
Sulfolobus acidocaldarius
2-oxoglutarate + CO2 + NADPH
-
-
-
r
isocitrate + NADP+
-
738195
Sulfolobus acidocaldarius MW001
2-oxoglutarate + CO2 + NADPH
-
-
-
r
additional information
Saci_2375 exhibits distinct and similar activities for isocitrate and homoisocitrate, but no detectable activity for 3-isopropylmalate. Saci_2375 is a dual function enzyme serving as isocitrate-homoisocitrate dehydrogenase
738195
Sulfolobus acidocaldarius
?
-
-
-
-
additional information
Saci_2375 exhibits distinct and similar activities for isocitrate and homoisocitrate, but no detectable activity for 3-isopropylmalate. Saci_2375 is a dual function enzyme serving as isocitrate-homoisocitrate dehydrogenase
738195
Sulfolobus acidocaldarius MW001
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
dimer of dimers
Sulfolobus acidocaldarius
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
60
-
assay at
Sulfolobus acidocaldarius
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
37
-
homoisocitrate
pH 8.0, 60°C, recombinant enzyme
Sulfolobus acidocaldarius
61
-
isocitrate
pH 8.0, 60°C, recombinant enzyme
Sulfolobus acidocaldarius
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Sulfolobus acidocaldarius
General Information
General Information
Commentary
Organism
physiological function
the failure to isolate a knockout mutant of saci_2375 suggests the indispensable role of Saci_2375 in cell viability
Sulfolobus acidocaldarius
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the failure to isolate a knockout mutant of saci_2375 suggests the indispensable role of Saci_2375 in cell viability
Sulfolobus acidocaldarius
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
2259
-
isocitrate
pH 8.0, 60°C, recombinant enzyme
Sulfolobus acidocaldarius
3364
-
homoisocitrate
pH 8.0, 60°C, recombinant enzyme
Sulfolobus acidocaldarius
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
2259
-
isocitrate
pH 8.0, 60°C, recombinant enzyme
Sulfolobus acidocaldarius
3364
-
homoisocitrate
pH 8.0, 60°C, recombinant enzyme
Sulfolobus acidocaldarius
Other publictions for EC 1.1.1.286
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)
740021
Shimizu
Structure and function of an a ...
Thermococcus kodakarensis, Thermococcus kodakarensis KRD1
Biochem. J.
474
105-122
2017
-
-
1
1
6
-
-
32
-
1
-
4
-
5
-
-
1
-
-
-
-
-
8
1
1
-
-
16
1
-
-
1
-
-
-
-
-
1
1
1
6
-
-
-
-
32
-
1
-
4
-
-
-
1
-
-
-
-
8
1
1
-
-
16
1
-
-
-
-
3
3
-
31
31
738195
Takahashi
Characterization of two ?-deca ...
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius MW001
Extremophiles
20
843-853
2016
-
-
1
-
-
-
-
2
-
-
-
6
-
5
-
-
1
-
-
-
-
-
6
1
1
-
-
2
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
2
-
-
-
6
-
-
-
1
-
-
-
-
6
1
1
-
-
2
1
-
-
-
-
1
1
-
2
2
740000
Takahashi
Determinants of dual substrate ...
Thermus thermophilus, Thermus thermophilus DSM 7039
Biochem. Biophys. Res. Commun.
478
1688-1693
2016
-
-
1
1
-
-
1
2
-
1
-
6
-
2
-
-
1
-
-
-
-
-
8
1
1
-
-
2
1
-
-
2
-
-
-
-
-
1
2
1
-
-
-
1
-
2
-
1
-
6
-
-
-
1
-
-
-
-
8
1
1
-
-
2
1
-
-
-
-
3
3
-
2
2
685232
Lin
Chemical mechanism of homoisoc ...
Saccharomyces cerevisiae
Biochemistry
47
4169-4180
2008
-
-
-
-
-
-
3
1
-
-
-
1
-
1
-
-
-
2
-
-
-
-
3
-
1
-
-
-
1
1
-
1
1
-
-
-
-
-
1
-
-
-
-
3
1
1
-
-
-
1
-
-
-
-
-
-
-
-
3
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
696220
Lin
Potassium is an activator of h ...
Saccharomyces cerevisiae
Biochemistry
47
10809-10815
2008
-
-
-
-
-
-
4
-
-
4
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
3
-
-
-
-
-
1
-
-
-
-
4
3
-
-
4
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
660907
Miyazaki
Bifunctional isocitrate-homois ...
Pyrococcus horikoshii
Biochem. Biophys. Res. Commun.
331
341-346
2005
-
-
1
-
-
-
-
3
-
-
-
-
-
3
-
-
1
-
-
-
-
-
4
-
-
-
-
3
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
1
-
-
-
-
4
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
660918
Miyazaki
Identification of a novel trif ...
Deinococcus radiodurans
Biochem. Biophys. Res. Commun.
336
596-602
2005
-
-
-
-
4
-
3
8
-
3
3
-
-
1
-
-
-
-
-
-
-
-
5
1
-
-
-
8
-
-
-
1
-
-
-
-
-
-
1
-
4
-
-
3
-
8
-
3
3
-
-
-
-
-
-
-
-
-
5
1
-
-
-
8
-
-
-
-
-
-
-
-
-
-
656127
Miyazaki
Characterization of homoisocit ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
J. Biol. Chem.
278
1864-1871
2003
-
-
1
-
1
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
6
1
-
-
1
2
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
6
1
-
-
1
2
-
-
-
-
-
-
-
-
-
-