BRENDA - Enzyme Database show
show all sequences of 2.6.1.6

Purification and characterization of leucine aminotransferase from green leaves of Amaranthus dubius

Singh, A.K.; Pathre, U.; Sane, P.V.; Biochem. Physiol. Pflanz. 187, 337-345 (1991)
No PubMed abstract available

Data extracted from this reference:

Organic Solvent Stability
Organic Solvent
Commentary
Organism
guanidine hydrochloride
shows sensitivity towards
Amaranthus dubius
urea
shows sensitivity towards
Amaranthus dubius
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Amaranthus dubius
-
-
-
Purification (Commentary)
Commentary
Organism
partially, 2 isoenzymes, LAT I and LAT II
Amaranthus dubius
Source Tissue
Source Tissue
Commentary
Organism
Textmining
leaf
-
Amaranthus dubius
-
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.7
-
-
Amaranthus dubius
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
guanidine hydrochloride
shows sensitivity towards
Amaranthus dubius
urea
shows sensitivity towards
Amaranthus dubius
Purification (Commentary) (protein specific)
Commentary
Organism
partially, 2 isoenzymes, LAT I and LAT II
Amaranthus dubius
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
leaf
-
Amaranthus dubius
-
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.7
-
-
Amaranthus dubius
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
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-
-
-
-
-
-
-
1
-
1
2
-
1
-
-
1
-
-
1
-
-
4
-
-
-
1
-
1
-
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-
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-
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-
1
-
1
2
-
-
-
1
-
1
-
-
4
-
-
-
1
-
1
-
-
-
-
-
-
-
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-
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
-
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-
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