2.6.1.42: branched-chain-amino-acid transaminase This is an abbreviated version! For detailed information about branched-chain-amino-acid transaminase, go to the full flat file .
Reaction
L-leucine +
2-oxoglutarate =
4-methyl-2-oxopentanoate +
L-glutamate
Synonyms (R)-selective omega-aminotransferase, AGT, alpha-KGA, At1g50110, At5g17310, Bat1, Bat1p, BAT2, Bat2p, BCAA, BCAA aminotransferase, BCAA-AT, BCAATase, BcaT, BCAT-1, BCAT1, Bcat2, BCAT4, Bcat6, BCAT7, BCATc, BCATm, branched chain amino acid: 2-oxoglutarate aminotransferase EC 2.6.1, branched chain aminotransferase, branched chain aminotransferase IlvE, branched chain aminotransferase, cytosolic isoform, branched chain aminotransferase, mitochondrial isoform, branched-chain amino acid aminotransferase, branched-chain amino acid aminotransferase 1, branched-chain amino acid aminotransferase 2, branched-chain amino acid aminotransferase 3, branched-chain amino acid aminotransferase 4, branched-chain amino acid aminotransferase 5, branched-chain amino acid aminotransferase 6, branched-chain amino acid transaminase, branched-chain amino acid transaminase 1, branched-chain amino acid transferase, branched-chain amino acid-glutamate transaminase, branched-chain amino-acid aminotransferase, branched-chain amino-acid transaminase, branched-chain aminotransferase, branched-chain aminotransferase 7, branched-chain aminotransferase4, CsBCAT2, CsBCAT3, CsBCAT7, eBCAT, EC 2.6.1.6, glutamate-branched-chain amino acid transaminase, hBCAT, hBCATm, Hoch3033, IlvE, IlvE aminotransferase, ilvE1, L-branched chain amino acid aminotransferase, L-leucine-alpha-ketoglutarate transaminase, leucine aminotransferase, leucine transaminase, Mevan_0408, mitochondrial branched chain aminotransferase, More, MtIlvE, PsBCAT, R-omegaAT, R-omegaAT_Bcel, R-omegaAT_Bthu, Rv2210c, SlBCAT1, SlBCAT2, SlBCAT3, SlBCAT4, SlBCAT5, SlBCAT6, SpBCAT1, TA-B, transaminase B, trd_1610, Tter_1720, TUZN1299, VMUT0738, VMUT_0738
ECTree
Subunits
Subunits on EC 2.6.1.42 - branched-chain-amino-acid transaminase
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x * 41000, SDS-PAGE, x * 40891, calculated
dimer
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2 * 47000, SDS-PAGE
dimer
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2 * 43000, isoenzyme III, SDS-PAGE
dimer
-
2 * 39000, isoenzyme I, SDS-PAGE
dimer
2 * 37539, calculated, 2 * 36000, SDS-PAGE
dimer
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2 * 37539, calculated, 2 * 36000, SDS-PAGE
-
dimer
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2 * 43400, recombinant BCATc, homodimer
dimer
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2 * 41730, recombinant BCATm, homodimer
dimer
2 * 38000, homodimer, SDS-PAGE
dimer
2 * 41000, homodimer, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE
dimer
2 * 32800, calculated
dimer
-
2 * 32800, calculated
-
hexamer
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-
hexamer
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6 * 34000, SDS-PAGE
hexamer
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6 * 31500, SDS-PAGE
hexamer
6 * 31500, trimer of dimers
hexamer
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6 * 34000, SDS-PAGE
-
hexamer
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6 * 33920, calculated from amino acid sequence
hexamer
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6 * 31500, SDS-PAGE
homodimer
2 * 40100, SDS-PAGE
homodimer
crystal structure
homodimer
2 * 39000, SDS-PAGE
homodimer
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2 * 39000, SDS-PAGE
-
homodimer
2 * 37500, SDS-PAGE
homodimer
-
2 * 37500, SDS-PAGE
-
homodimer
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2 * 37500, SDS-PAGE
-
homodimer
2 * 41350, recombinant mutant T186R enzyme, mass spectrometry
homodimer
2 * 41730, sequence calculation
homodimer
2* 42800, about, sequence calculation
homodimer
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2 * 37400, SDS-PAGE
homodimer
2 * 34000, SDS-PAGE
homodimer
2 * 40000, SDS-PAGE
homodimer
2 * 39700, calculated from amino acid sequence
homodimer
2 * 40000, the biologically active form of IlvE is a homodimer, SDS-PAGE
homodimer
-
2 * 34000, SDS-PAGE
-
homodimer
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2 * 40000, SDS-PAGE
-
homodimer
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2 * 39700, calculated from amino acid sequence
-
homodimer
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2 * 40000, the biologically active form of IlvE is a homodimer, SDS-PAGE
-
homodimer
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2 * 34000, SDS-PAGE
-
homodimer
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2 * 40000, SDS-PAGE
-
homodimer
-
gel filtration
-
homodimer
-
2 * 47500, SDS-PAGE
homodimer
2 * 32800, SDS-PAGE
homodimer
-
2 * 32800, SDS-PAGE
-
homohexamer
6 * 34000, SDS-PAGE
homohexamer
6 * 31800, SDS-PAGE
homohexamer
-
6 * 31800, SDS-PAGE
-
homohexamer
-
6 * 31800, SDS-PAGE
-
homohexamer
-
6 * 31800, SDS-PAGE
-
homohexamer
-
6 * 31800, SDS-PAGE
-
homotetramer
4 * 34000, SDS-PAGE
homotetramer
-
4 * 34000, SDS-PAGE
-
homotetramer
-
4 * 34000, SDS-PAGE
-
homotetramer
-
4 * 34000, SDS-PAGE
-
homotetramer
-
4 * 34000, SDS-PAGE
-
homotetramer
-
4 * 34000, SDS-PAGE
-
homotetramer
-
4 * 34000, SDS-PAGE
-
homotetramer
-
4 * 34000, SDS-PAGE
-
homotetramer
4 * 35300, SDS-PAGE
homotetramer
4 * 36800, a dimer of dimers, recombinant His6-tagged enzyme, SDS-PAGE
homotetramer
-
4 * 35300, SDS-PAGE
-
homotetramer
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4 * 36800, a dimer of dimers, recombinant His6-tagged enzyme, SDS-PAGE
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monomer
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1 * 41000, SDS-PAGE
monomer
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1 * 43000, SDS-PAGE
monomer
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1 * 47000, BCATm, SDS-PAGE
monomer
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1 * 41000, BCATc, SDS-PAGE
monomer
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1 * 43000, SDS-PAGE
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additional information
BCATm has an interdomain loop. Each monomer of BCATm is composed of a small (residues 1-175) and a large domain (residues 176-365) with an interdomain loop. At the dimer interface two PLP cofactors reside
additional information
BCATm has an interdomain loop. Each monomer of BCATm is composed of a small (residues 1-175) and a large domain (residues 176-365) with an interdomain loop. At the dimer interface two PLP cofactors reside
additional information
the BCATc polypeptide consists of a small (residues 1-188) and large domain (residues 202-C-terminus), connected by an interdomain loop (residues 189-201). Three-dimensional enzyme structure complexed with gabapentin in the oxidised and reduced state
additional information
the BCATc polypeptide consists of a small (residues 1-188) and large domain (residues 202-C-terminus), connected by an interdomain loop (residues 189-201). Three-dimensional enzyme structure complexed with gabapentin in the oxidised and reduced state
additional information
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N-terminal amino acid sequence
additional information
the three-dimensional structure reveals that each monomer is tethered by a substrate specificity loop to its partner molecule
additional information
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the three-dimensional structure reveals that each monomer is tethered by a substrate specificity loop to its partner molecule
additional information
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the three-dimensional structure reveals that each monomer is tethered by a substrate specificity loop to its partner molecule
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additional information
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the three-dimensional structure reveals that each monomer is tethered by a substrate specificity loop to its partner molecule
-
additional information
the catalytically competent unit of BCATs is a dimer
additional information
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the catalytically competent unit of BCATs is a dimer
additional information
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the catalytically competent unit of BCATs is a dimer
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