BRENDA - Enzyme Database
show all sequences of 1.1.1.369

Novel inositol catabolic pathway in Thermotoga maritima

Rodionova, I.A.; Leyn, S.A.; Burkart, M.D.; Boucher, N.; Noll, K.M.; Osterman, A.L.; Rodionov, D.A.; Environ. Microbiol. 15, 2254-2266 (2013)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.9
-
1D-chiro-inositol
pH 8.8, 60°C
Thermotoga maritima
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermotoga maritima
Q9WYP5
-
-
Thermotoga maritima DSM 3109
Q9WYP5
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1D-chiro-inositol + NAD+
-
727372
Thermotoga maritima
2D-2,3,5/4,6-pentahydroxycyclohexanone + NADH + H+
-
-
-
?
1D-chiro-inositol + NAD+
-
727372
Thermotoga maritima DSM 3109
2D-2,3,5/4,6-pentahydroxycyclohexanone + NADH + H+
-
-
-
?
additional information
The enzyme also catalyses the reaction of EC 1.1.1.18, inositol 2-dehydrogenase, and can also use D-glucose and D-xylose. Inositol is the preferred substrate
727372
Thermotoga maritima
?
-
-
-
-
additional information
The enzyme also catalyses the reaction of EC 1.1.1.18, inositol 2-dehydrogenase, and can also use D-glucose and D-xylose. Inositol is the preferred substrate
727372
Thermotoga maritima DSM 3109
?
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1
-
1D-chiro-inositol
pH 8.8, 60°C
Thermotoga maritima
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.9
-
1D-chiro-inositol
pH 8.8, 60°C
Thermotoga maritima
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1D-chiro-inositol + NAD+
-
727372
Thermotoga maritima
2D-2,3,5/4,6-pentahydroxycyclohexanone + NADH + H+
-
-
-
?
1D-chiro-inositol + NAD+
-
727372
Thermotoga maritima DSM 3109
2D-2,3,5/4,6-pentahydroxycyclohexanone + NADH + H+
-
-
-
?
additional information
The enzyme also catalyses the reaction of EC 1.1.1.18, inositol 2-dehydrogenase, and can also use D-glucose and D-xylose. Inositol is the preferred substrate
727372
Thermotoga maritima
?
-
-
-
-
additional information
The enzyme also catalyses the reaction of EC 1.1.1.18, inositol 2-dehydrogenase, and can also use D-glucose and D-xylose. Inositol is the preferred substrate
727372
Thermotoga maritima DSM 3109
?
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1
-
1D-chiro-inositol
pH 8.8, 60°C
Thermotoga maritima
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
345
-
1D-chiro-inositol
pH 8.8, 60°C
Thermotoga maritima
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
345
-
1D-chiro-inositol
pH 8.8, 60°C
Thermotoga maritima
Other publictions for EC 1.1.1.369
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)
727372
Rodionova
Novel inositol catabolic pathw ...
Thermotoga maritima, Thermotoga maritima DSM 3109
Environ. Microbiol.
15
2254-2266
2013
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723995
Yoshida
Genetic modification of Bacill ...
Bacillus subtilis, Bacillus subtilis 168
Appl. Environ. Microbiol.
72
1310-1315
2006
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727731
Yoshida
Organization and transcription ...
Bacillus subtilis 168, Bacillus subtilis
J. Bacteriol.
179
4591-4598
1997
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1
1
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389431
Ramaley
Purification and properties of ...
Bacillus subtilis, Bacillus subtilis 168
J. Biol. Chem.
254
7684-7690
1979
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