Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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.

Word Map on EC 2.6.1.42

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

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.42 branched-chain-amino-acid transaminase

Engineering

Engineering on EC 2.6.1.42 - branched-chain-amino-acid transaminase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K202R
active site residue, no activity detected
R145E
no activity detected
Y71A/R145A
no activity detected
H106Y/Y108R
C221S
-
the mutant shows strongly decreased kcat values compared to the wild type enzyme
C235S
-
the mutant enzyme exhibits kcat values that are within 20-30% of wild type BCATc values, but also have lower Km values, hence higher calculated kcat/Km values than those of the wild type enzyme
C242S
-
the mutant shows strongly decreased kcat values compared to the wild type enzyme
C293S
-
the C293S mutant and wild type BCATc have similar kinetic constants with L-valine, L-leucine, and L-glutamate
C315A
C315A/C318A
contains changes in the structure of the beta-turn preceding the CXXC motif when compared with wild type protein, the oxidized mutant enzyme shows limited activity
C318A
C318A/C315CSD
the overall structure of the C318A/C315CSD variant overlays very well with that of the C318A mutant and the oxidized form of wild-type hBCATm, with a few exceptions in the interdomain loop (residues 171-181) and the N-terminal loop (residues 15-32)
C335S
-
for all amino acid substrates, there is a significant decrease (70% to 80%) in kcat with the C335S mutant, the Km value for glutamate with the C335S mutant enzyme is approximately 3fold lower than that observed with wild type enzyme
C335S/C3388S
-
the mutant shows kcat values that are similar to values observed with the single C335 mutant enzymes, Km values are largely unchanged compared to those of wild type BCATc, kcat/Km values are significantly lower than wild type values
C335S/C338S
dimerization of BCATc occurs concurrently with GSNO-mediated S-glutathionylation, which is abolished when substituted with the double mutant C335S/C338S
C338S
-
the mutant enzyme exhibits kcat values for the BCAAs that were 50% lower than that observed with wild type enzyme. With the exception of L-glutamate, where the Km value is not changed and L-valine, where the Km value is 50% lower than the value for wild type BCATc, Km values for L-isoleucine and L-leucine are largely unaffected for the C338S mutant
E264K
-
heterogeneous BCAT2 gene mutation, in combination heterogeneous BCAT2 gene mutation R170Q, found in a 25-year-old patient presenting with headache complaints and mild memory impairment for about six years
R170Q
-
heterogeneous BCAT2 gene mutation, in combination heterogeneous BCAT2 gene mutation E264K, found in a 25-year-old patient presenting with headache complaints and mild memory impairment for about six years
T186R
site-directed mutagenesis, structure determination and comparison with wild-type enzyme
A234D
site-directed mutagenesis of strain BY4741, both deletion mutant bat1DELTA and point mutant bat1A234D cells exhibit the same phenotypes relative to the wild-type Bat1 strain, namely, a repressive growth rate in the logarithmic phase, decreases in intracellular valine and leucine content in the logarithmic and stationary growth phases, respectively, and an increase in fusel alcohol content in culture medium, and a decrease in the carbon dioxide productivity. These results indicate that amino acid change from Ala to Asp at position 234 leads to a functional impairment of Bat1, although homology modeling suggests that Asp234 in the variant Bat1 does not inhibit enzymatic activity directly
K202A
site-directed mutagenesis, inactive mutant
K219A
K219R
-
mutation in conserved pyridoxal phosphate-binding site, loss of activity. Mutant is nearly as effective aswild-type Bat1 or Bat2 at partially suppressing the rapamycin recovery and TORC1 activity defects of the Bat1 bat2 mutant
A234D
-
site-directed mutagenesis of strain BY4741, both deletion mutant bat1DELTA and point mutant bat1A234D cells exhibit the same phenotypes relative to the wild-type Bat1 strain, namely, a repressive growth rate in the logarithmic phase, decreases in intracellular valine and leucine content in the logarithmic and stationary growth phases, respectively, and an increase in fusel alcohol content in culture medium, and a decrease in the carbon dioxide productivity. These results indicate that amino acid change from Ala to Asp at position 234 leads to a functional impairment of Bat1, although homology modeling suggests that Asp234 in the variant Bat1 does not inhibit enzymatic activity directly
-
additional information