BRENDA - Enzyme Database show
show all sequences of 5.3.1.20

Induction of D-ribose isomerase by L-ribose in Mycobacterium smegmatis

Izumori, K.; Sugimoto, S.; Kraska, B.; Agric. Biol. Chem. 44, 223-225 (1980)
No PubMed abstract available

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mycolicibacterium smegmatis
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Source Tissue
Source Tissue
Commentary
Organism
Textmining
culture condition:D-ribose-induced cell
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Mycolicibacterium smegmatis
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culture condition:L-ribose-grown cell
-
Mycolicibacterium smegmatis
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
culture condition:D-ribose-induced cell
-
Mycolicibacterium smegmatis
-
culture condition:L-ribose-grown cell
-
Mycolicibacterium smegmatis
-
Other publictions for EC 5.3.1.20
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)
2649
Shukla
-
Studies on sugar isomerases of ...
Lactobacillus sp.
J. Basic Microbiol.
25
273-277
1985
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1
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1
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1
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1
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2648
Elbein
D-Ribose isomerase ...
Mycolicibacterium smegmatis
Methods Enzymol.
89
547-550
1982
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1
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3
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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
4
1
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1
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2650
Izumori
-
Induction of D-ribose isomeras ...
Mycolicibacterium smegmatis
Agric. Biol. Chem.
44
223-225
1980
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2629
Izumori
Evidence that the isomerizatio ...
Mycolicibacterium smegmatis
J. Bacteriol.
126
553-555
1976
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2
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1
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2647
Izumori
Pentose metabolism in Mycobact ...
Mycolicibacterium smegmatis
J. Bacteriol.
128
587-591
1976
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2645
Izumori
Purification, crystallization, ...
Mycolicibacterium smegmatis
J. Biol. Chem.
250
8085-8087
1975
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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
1
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3
1
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1
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1
1
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