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IUBMB Comments A pyridoxal-phosphate protein. This enzyme differs from EC 2.6.1.42 , branched-chain-amino-acid transaminase, in that it does not act on L -valine or L -isoleucine, although it does act on L -methionine. The mitochondrial form from rat liver differs in physical characteristics from the cytoplasmic form.
Synonyms
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L-leucine aminotransferase
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leucine 2-oxoglutarate transaminase
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leucine aminotransferase
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leucine-alpha-ketoglutarate transaminase
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L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
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amino group transfer
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MetaCyc
L-leucine biosynthesis, L-leucine degradation I, L-leucine degradation III, L-leucine degradation IV (reductive Stickland reaction), L-leucine degradation V (oxidative Stickland reaction), odd iso-branched-chain fatty acid biosynthesis
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L-leucine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. This enzyme differs from EC 2.6.1.42, branched-chain-amino-acid transaminase, in that it does not act on L-valine or L-isoleucine, although it does act on L-methionine. The mitochondrial form from rat liver differs in physical characteristics from the cytoplasmic form.
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L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 4-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-leucine
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Substrates: -
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L-leucine + oxaloacetate
4-methyl-2-oxopentanoate + L-aspartate
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Substrates: -
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L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
additional information
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Substrates: specific for leucine, isoleucine or valine, no other amino acid would serve as an amino donor, pyruvate is no amino acid acceptor
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L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
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Substrates: -
?, r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
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Substrates: -
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
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Substrates: -
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
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Substrates: leucine metabolism and hence of cholesterogenesis and ketogenesis, not present in fetal rat liver, but after birth activity appears and increases rapidly
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L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
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Substrates: -
?, r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
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Substrates: mitochondrial isoenzyme
r
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L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
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Substrates: -
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L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
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Substrates: -
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L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
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Substrates: -
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L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
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Substrates: leucine metabolism and hence of cholesterogenesis and ketogenesis, not present in fetal rat liver, but after birth activity appears and increases rapidly
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pyridoxal 5'-phosphate
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Km 0.004 mM
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2-mercaptoethanol
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slight inhibition
hydroxylamine
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inhibits the aldehyde form of the enzyme while the amino form is found to be inert
p-chloromercuribenzoate
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1.0 mM, complete inhibition
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Starvation
Modulation of leucine transaminase activity by dietary means.
Vitamin B 6 Deficiency
Effect of vitamin B6 deficiency on leucine transaminase activity in chick tissue.
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0.065 - 3.3
2-oxoglutarate
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leucine
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pH 8.2, 37°C
0.065
2-oxoglutarate
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pH 8.2, 37°C
2.3
2-oxoglutarate
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isozyme LAT II, pH 9, 37°C
3.3
2-oxoglutarate
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isozyme LAT I, pH 9, 37°C
1.67
L-leucine
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isozyme LAT II, pH 9, 37°C
2.5
L-leucine
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isozyme LAT I, pH 9, 37°C
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8.7
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brenda
soybean, var. Kali tur
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rat, strain Wistar
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brenda
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brenda
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predominantly found in mitochondrion
brenda
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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A0A6J4PZ87_9BURK
uncultured Ramlibacter sp
314
0
33668
TrEMBL
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A0A6J4X2L8_9DELT
393
0
43550
TrEMBL
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A0A6J4YBW8_9DELT
394
0
43505
TrEMBL
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68000
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gel filtration, isoenzyme LAT I
93300
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gel filtration, isoenzyme LAT II
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45
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quite stable on heating for 1 h
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guanidine hydrochloride
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shows sensitivity towards
urea
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shows sensitivity towards
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4°C, concentrated enzyme, activity is stable for 2 months
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partially, 2 isoenzymes, LAT I and LAT II
partially, 2 isoenzymes, LAT I and LAT II
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partially, 2 isoenzymes, LAT I and LAT II
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Aki, K.; Ogawa, K.; Ichihara, A.
Transaminases of branched chain amino acids. IV. Purification and properties of two enzymes from rat liver
Biochim. Biophys. Acta
159
276-284
1968
Rattus norvegicus
brenda
Korpela, T.K.
Purification of branched-chain-amino-acid aminotransferase from pig heart
Methods Enzymol.
166
269-274
1988
Rattus norvegicus
brenda
Ikeda, T.; Konishi, Y.; Ichihara, A.
Transaminase of branched chain amino acids. XI. Leucine (methionine) transaminase of rat liver mitochondria
Biochim. Biophys. Acta
445
622-631
1976
Rattus norvegicus
brenda
Pathre, U.; Singh, A.K.; Viswanathan, P.N.; Sane, P.V.
Purification and properties of leucine aminotransferase from soybean seedlings
Phytochemistry
26
2913-2917
1987
Glycine max
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brenda
Singh, A.K.; Pathre, U.; Sane, P.V.
Purification and characterization of leucine aminotransferase from green leaves of Amaranthus dubius
Biochem. Physiol. Pflanz.
187
337-345
1991
Amaranthus dubius
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brenda
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