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show all sequences of 2.6.1.6

Purification and properties of leucine aminotransferase from soybean seedlings

Pathre, U.; Singh, A.K.; Viswanathan, P.N.; Sane, P.V.; Phytochemistry 26, 2913-2917 (1987)
No PubMed abstract available

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
adipic acid
-
Glycine max
Fumaric acid
-
Glycine max
Glutaric acid
-
Glycine max
hydroxylamine
inhibits the aldehyde form of the enzyme while the amino form is found to be inert
Glycine max
Maleate
-
Glycine max
Maleic acid
-
Glycine max
phenylhydrazine
-
Glycine max
potassium cyanide
-
Glycine max
Sodium bisulfite
-
Glycine max
succinic acid
-
Glycine max
Thiosemicarbazide
-
Glycine max
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.67
-
L-leucine
isozyme LAT II, pH 9, 37°C
Glycine max
2.3
-
2-oxoglutarate
isozyme LAT II, pH 9, 37°C
Glycine max
2.5
-
L-leucine
isozyme LAT I, pH 9, 37°C
Glycine max
3.3
-
2-oxoglutarate
isozyme LAT I, pH 9, 37°C
Glycine max
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
68000
-
gel filtration, isoenzyme LAT I
Glycine max
93300
-
gel filtration, isoenzyme LAT II
Glycine max
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-leucine + 2-oxoglutarate
Glycine max
-
4-methyl-2-oxopentanoate + L-glutamate
-
Glycine max
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Glycine max
-
soybean, var. Kali tur
-
Purification (Commentary)
Commentary
Organism
partially, 2 isoenzymes, LAT I and LAT II
Glycine max
Source Tissue
Source Tissue
Commentary
Organism
Textmining
seedling
-
Glycine max
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
7.4
-
isoenzyme LAT I
Glycine max
8.7
-
isoenzyme LAT II
Glycine max
Storage Stability
Storage Stability
Organism
4°C, concentrated enzyme, activity is stable for 2 months
Glycine max
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-leucine + 2-oxoglutarate
-
640167
Glycine max
4-methyl-2-oxopentanoate + L-glutamate
-
640167
Glycine max
?
L-leucine + 2-oxoglutarate
-
640167
Glycine max
4-methyl-2-oxopentanoate + L-glutamate
-
640167
Glycine max
r
L-leucine + 4-methyl-2-oxopentanoate
-
640167
Glycine max
4-methyl-2-oxopentanoate + L-leucine
-
-
-
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.9
-
-
Glycine max
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
adipic acid
-
Glycine max
Fumaric acid
-
Glycine max
Glutaric acid
-
Glycine max
hydroxylamine
inhibits the aldehyde form of the enzyme while the amino form is found to be inert
Glycine max
Maleate
-
Glycine max
Maleic acid
-
Glycine max
phenylhydrazine
-
Glycine max
potassium cyanide
-
Glycine max
Sodium bisulfite
-
Glycine max
succinic acid
-
Glycine max
Thiosemicarbazide
-
Glycine max
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.67
-
L-leucine
isozyme LAT II, pH 9, 37°C
Glycine max
2.3
-
2-oxoglutarate
isozyme LAT II, pH 9, 37°C
Glycine max
2.5
-
L-leucine
isozyme LAT I, pH 9, 37°C
Glycine max
3.3
-
2-oxoglutarate
isozyme LAT I, pH 9, 37°C
Glycine max
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
68000
-
gel filtration, isoenzyme LAT I
Glycine max
93300
-
gel filtration, isoenzyme LAT II
Glycine max
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-leucine + 2-oxoglutarate
Glycine max
-
4-methyl-2-oxopentanoate + L-glutamate
-
Glycine max
?
Purification (Commentary) (protein specific)
Commentary
Organism
partially, 2 isoenzymes, LAT I and LAT II
Glycine max
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
seedling
-
Glycine max
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
7.4
-
isoenzyme LAT I
Glycine max
8.7
-
isoenzyme LAT II
Glycine max
Storage Stability (protein specific)
Storage Stability
Organism
4°C, concentrated enzyme, activity is stable for 2 months
Glycine max
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-leucine + 2-oxoglutarate
-
640167
Glycine max
4-methyl-2-oxopentanoate + L-glutamate
-
640167
Glycine max
?
L-leucine + 2-oxoglutarate
-
640167
Glycine max
4-methyl-2-oxopentanoate + L-glutamate
-
640167
Glycine max
r
L-leucine + 4-methyl-2-oxopentanoate
-
640167
Glycine max
4-methyl-2-oxopentanoate + L-leucine
-
-
-
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.9
-
-
Glycine max
Other publictions for EC 2.6.1.6
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
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)
640169
Singh
-
Purification and characterizat ...
Amaranthus dubius
Biochem. Physiol. Pflanz.
187
337-345
1991
-
-
-
-
-
-
-
-
-
-
-
-
2
1
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
640014
Korpela
Purification of branched-chain ...
Rattus norvegicus
Methods Enzymol.
166
269-274
1988
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
1
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
640167
Pathre
-
Purification and properties of ...
Glycine max
Phytochemistry
26
2913-2917
1987
-
-
-
-
-
-
11
4
-
-
2
1
-
1
-
-
1
-
-
1
2
1
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
11
-
4
-
-
2
1
-
-
-
1
-
1
2
1
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
640166
Ikeda
Transaminase of branched chain ...
Rattus norvegicus
Biochim. Biophys. Acta
445
622-631
1976
-
-
-
-
-
-
-
-
1
-
1
2
-
1
-
-
1
-
-
1
-
-
4
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
2
-
-
-
1
-
1
-
-
4
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
639996
Aki
Transaminases of branched chai ...
Rattus norvegicus
Biochim. Biophys. Acta
159
276-284
1968
-
-
-
-
-
-
2
2
4
-
-
1
-
1
-
-
1
-
-
1
1
-
4
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
2
-
2
4
-
-
1
-
-
-
1
-
1
1
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-