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Information on EC 2.6.1.42 - branched-chain-amino-acid transaminase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P47176
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2.6.1.42 branched-chain-amino-acid transaminaseIUBMB Comments
Also acts on L-isoleucine and L-valine, and thereby differs from EC 2.6.1.6, leucine transaminase, which does not. It also differs from EC 2.6.1.66, valine---pyruvate transaminase.
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Word Map
- 2.6.1.42
-
bcats
- isoleucine
-
transamination
- aminotransferases
- pyridoxal
-
ketoacids
- alpha-ketoisocaproate
- transaminases
- l-valine
-
isomeroreductase
- gabapentin
-
acetohydroxy
- alpha-ketoacids
- nutrition
- synthesis
-
acetohydroxyacid
- medicine
- drug development
- analysis
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
bcat1, bcatm, branched-chain aminotransferase, bcatc, bcat2, branched-chain amino acid aminotransferase, branched chain aminotransferase, hbcat, hbcatm, branched-chain amino acid transaminase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Bat1
branched-chain amino acid aminotransferase
branched-chain amino acid transaminase
branched-chain amino acid-glutamate transaminase
-
-
-
-
branched-chain aminotransferase
-
-
-
-
glutamate-branched-chain amino acid transaminase
-
-
-
-
L-branched chain amino acid aminotransferase
-
-
-
-
transaminase B
-
-
-
-
branched-chain amino acid aminotransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
branched-chain-amino-acid:2-oxoglutarate aminotransferase
Also acts on L-isoleucine and L-valine, and thereby differs from EC 2.6.1.6, leucine transaminase, which does not. It also differs from EC 2.6.1.66, valine---pyruvate transaminase.
CAS REGISTRY NUMBER
COMMENTARY
9054-65-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxo-3-methylpentanoate
2-oxoisohexanoate + L-isoleucine
-
-
-
r
L-leucine + 2-oxoisohexanoate
2-oxoisohexanoate + L-leucine
-
-
-
r
L-leucine + 3-methyl-2-oxobutanoate
4-methyl-2-oxopentanoate + L-valine
-
-
-
r
L-leucine + pyruvate
2-oxoisohexanoate + L-alanine
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
involved in production of fusel alcohols during fermentation
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
involved in production of fusel alcohols during fermentation
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
YR6a, YPH501, Bat2p, amino acid sequence accession number
SwissProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
subcellular localization of wild-type and mutant enzymes, overview
-
additional information
subcellular localization of wild-type and mutant enzymes, overview
-
additional information
-
subcellular localization of wild-type and mutant enzymes, overview
-
additional information
subcellular localization of wild-type and mutant enzymes, overview
-
additional information
subcellular localization of wild-type and mutant enzymes, overview
-
additional information
-
subcellular localization of wild-type and mutant enzymes, overview
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
metabolism
physiological function
malfunction
because deletion of BAT1 only slightly affects cell growth in the absence of externally supplied BCAAs (isoleucine, leucine, valine) and deletion of BAT2 has no effect, mitochondrial carriers must exist to transport branched-chain 2-oxo acids and amino acids from the mitochondria to the cytosol. In contrast, strains with both BAT1 and BAT2 deleted are auxotrophic for BCAAs
malfunction
mutation of BCATs results in perturbed TCA-cycle intermediate levels, which in turn lead to reduced ATP levels and inhibition of TORC1
malfunction
yeast strains with a single gene disruption of BAT1 or BAT2 are constructed and only DELTAbat1 cells show the slow-growth phenotype. There is no mitochondrial localization in mutant Bat1-MTS, whereas mutant Bat2+MTS is relocalized into the mitochondria. Bat1 and Bat2 isozymes deletion mutants phenotype analysis and comparison, detailed overview
metabolism
the enzyme is involved in branched-chain amino acids (BCAAs) biosynthesis. Degradation of BCAAs begins with transamination reactions, catalyzed by branched-chain amino acid transaminases (BCATs) located in the mitochondria (Bat1p) and cytosol (Bat2p). Two competing isobutanol pathways can be manipulated by overexpressing or deleting BAT1 or BAT2. Interactions between valine and the regulatory protein Ilv6p affect isobutanol production. While valine inhibits isobutanol production, it boosts 2-methyl-1-butanol production
metabolism
the enzyme is involved in the branched-chain amino acid biosynthesis. The mitochondria are the major site of valine biosynthesis, and mitochondrial BCAT, Bat1, is important for valine biosynthesis in Saccharomyces cerevisiae. Unlike in higher eukaryotes, the Saccharomyces cerevisiae BCATs, Bat1 and Bat2, can function in both anabolic and catabolic pathways as the final step in the biosynthesis and the first step in the degradation of BCAAs
physiological function
isozyme BCAT2 is a suppressor of the taz1DELTA growth defect in yeast cells. Abolishing yeast Taz1 results in decreased total CL amounts, increased levels of MLCL, and mitochondrial dysfunction. The mitochondrial dysfunction leads to the Barth syndrome (BTHS), a metabolic and neuromuscular disorder. But elevated levels of isozymes Bat1 (BCAT1) or Bat2 (BCAT2) do not restore the reduced membrane potential, altered stability of respiratory complexes, or the defective accumulation of MLCL species in yeast taz1DELTA cells. Multi-copy suppressor screening. The growth defect rescue in both yeast and mammalian taz1-defective cells with the two different BCAT isoforms is similar. In both cell types, the mitochondrial isoform has a higher rescue capacity. Hence, although the mitochondrial and cytosolic isoforms have overlapping functions in transamination reactions, it appears that their products are required more in mitochondria and that they are not completely free to equilibrate between the matrix of mitochondria and the cytosol
physiological function
isozymes Bat1 and Bat2 play distinct roles in branched-chain amino acid aminotransferase (BCAT) BCAAs biosynthesis
physiological function
role of branched-chain amino acid transaminases in Saccharomyces cerevisiae isobutanol biosynthesis, analysis of the isobutanol production in two genetic backgrounds, i.e. CEN.PK2-1C and BY4741, pathways overview
malfunction
deletion of BAT1 alone increases isobutanol production by 14.2fold compared to wild-type strains in media lacking valine, interactions between valine and the regulatory protein Ilv6p affect isobutanol production. Compartmentalizing the five-gene isobutanol biosynthetic pathway in mitochondria of BAT1 deletion strains results in an additional 2.1-fold increase in isobutanol production in the absence of valine. While valine inhibits isobutanol production, it boosts 2-methyl-1-butanol production. Because deletion of BAT1 only slightly affects cell growth in the absence of externally supplied BCAAs (isoleucine, leucine, valine) and deletion of BAT2 has no effect, mitochondrial carriers must exist to transport branched-chain 2-oxo acids and amino acids from the mitochondria to the cytosol. In contrast, strains with both BAT1 and BAT2 deleted are auxotrophic for BCAAs. Bat1 overexpression phenotype, overview
malfunction
mutation of BCATs results in perturbed TCA-cycle intermediate levels, which in turn lead to reduced ATP levels and inhibition of TORC1
malfunction
the phenotypes of mutant A234D and bat1 deletion mutant are similar with a repressive growth rate in the logarithmic phase, decreases in intracellular valine and leucine content in the logarithmic and stationary growth phases, respectively, an increase in fusel alcohol content in culture medium, and a decrease in the carbon dioxide productivity, overview. Effect of hyperosmotic stress on yeast cells expressing Bat1
malfunction
yeast strains with a single gene disruption of BAT1 or BAT2 are constructed and only DELTAbat1 cells show the slow-growth phenotype. There is no mitochondrial localization in mutant Bat1-MTS, whereas mutant Bat2+MTS is relocalized into the mitochondria. Bat1 and Bat2 isozymes deletion mutants phenotype analysis and comparison, detailed overview. The bat1 mutations affect valine but not leucine and isoleucine biosynthesis, lacking of Bat1 has the less effect on leucine biosynthesis
metabolism
inside the yeast mitochondria, both valine (Val) and leucine (Leu) are primarily biosynthesized from two pyruvates while isoleucine (Ile) is produced from an initial alpha-ketobutyrate molecule. Pyruvate and alpha-ketobutyrate are then converted into alpha-ketoisovalerate (KIV) and alpha-keto-beta-methylvalerate (KMV), respectively, through the same pathway. In contrast, alpha-ketoisocaproate (KIC) is synthesized from KIV. KIV, KMV, and KIC are finally transaminated to Val, Ile, and Leu, respectively, by the mitochondrial and cytoplasmic BCAA aminotransferases (BCATs) Bat1 and Bat2, respectively
metabolism
the enzyme is involved in branched-chain amino acids (BCAAs) biosynthesis. Two competing isobutanol pathways can be manipulated by overexpressing or deleting BAT1 or BAT2. Degradation of BCAAs begins with transamination reactions, catalyzed by branched-chain amino acid transaminases (BCATs) located in the mitochondria (Bat1p) and cytosol (Bat2p). Interactions between valine and the regulatory protein Ilv6p affect isobutanol production. While valine inhibits isobutanol production, it boosts 2-methyl-1-butanol production
metabolism
the enzyme is involved in the branched-chain amino acid biosynthesis. The mitochondria are the major site of valine biosynthesis, and mitochondrial BCAT, Bat1, is important for valine biosynthesis in Saccharomyces cerevisiae. Unlike in higher eukaryotes, the Saccharomyces cerevisiae BCATs, Bat1 and Bat2, can function in both anabolic and catabolic pathways as the final step in the biosynthesis and the first step in the degradation of BCAAs
physiological function
-
branched-chain aminotransferase yeast mutants exhibit severely compromised target of rapamycin complex TORC1 activity, which is partially restored by expression of isoofrm Bat1 active site mutants, implicating both catalytic and structural roles of branched-chain aminotransferases in TORC1 control. Bat1 interacts with branched-chain amino acid metabolic enzymes and, in a leucine-dependent fashion, with the tricarboxylic acid-cycle enzyme aconitase. Branched-chain aminotransferase mutation perturbs tricarboxylic acid-cycle intermediate levels, consistent with a tricarboxylic acid-cycle block, and results in low ATP levels, activation of AMPK, and TORC1 inhibition
physiological function
isozyme BCAT1 is a suppressor of the taz1DELTA growth defect in yeast cells. Abolishing yeast Taz1 results in decreased total CL amounts, increased levels of MLCL, and mitochondrial dysfunction. The mitochondrial dysfunction leads to the Barth syndrome (BTHS), a metabolic and neuromuscular disorder. But elevated levels of Bat1 (BCAT1) or Bat2 (BCAT2) do not restore the reduced membrane potential, altered stability of respiratory complexes, or the defective accumulation of MLCL species in yeast taz1DELTA cells. Multi-copy suppressor screening. The growth defect rescue in both yeast and mammalian taz1-defective cells with the two different BCAT isoforms is similar. In both cell types, the mitochondrial isoform has a higher rescue capacity. Hence, although the mitochondrial and cytosolic isoforms have overlapping functions in transamination reactions, it appears that their products are required more in mitochondria and that they are not completely free to equilibrate between the matrix of mitochondria and the cytosol. Bat1 has been reported to interact with the TCA cycle enzyme aconitase
physiological function
isozymes Bat1 and Bat2 play distinct roles in branched-chain amino acid aminotransferase (BCAT) BCAAs biosynthesis
physiological function
role of branched-chain amino acid transaminases in Saccharomyces cerevisiae isobutanol biosynthesis, analysis of the isobutanol production in two genetic backgrounds, i.e. CEN.PK2-1C and BY4741, pathways overview
physiological function
the mitochondrial branched-chain amino acid (BCAA) aminotransferase Bat1 plays an important role in the synthesis of branched-chain amino acids, i.e. valine, leucine, and isoleucine
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
additional information
K219A
-
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
additional information
construction of two artificial genes encoding the mitochondrial-targeting signal (MTS)-deleted Bat1 (Bat1-MTS) and the MTS of Bat1-fused Bat2 (Bat2+MTS) from originating Bat1 and Bat2 genes. Bat2+MTS is relocalized into the mitochondria, because Bat2 localization is changed from cytosol to the mitochondria by addition of MTS, and can partially restore the valine content and growth in DELTAbat1DELTAbat2 cells. Bat1-MTS and Bat2+MTS function properly in DELTAbat1DELTAbat2 cells. Mutant DELTAbat1DELTAbat2 cells harboring Bat1-MTS grow similarly to DELTAbat1 cells
additional information
construction of two artificial genes encoding the mitochondrial-targeting signal (MTS)-deleted Bat1 (Bat1-MTS) and the MTS of Bat1-fused Bat2 (Bat2+MTS) from originating Bat1 and Bat2 genes. Bat2+MTS is relocalized into the mitochondria, because Bat2 localization is changed from cytosol to the mitochondria by addition of MTS, and can partially restore the valine content and growth in DELTAbat1DELTAbat2 cells. Bat1-MTS and Bat2+MTS function properly in DELTAbat1DELTAbat2 cells. Mutant DELTAbat1DELTAbat2 cells harboring Bat1-MTS grow similarly to DELTAbat1 cells
additional information
-
construction of two artificial genes encoding the mitochondrial-targeting signal (MTS)-deleted Bat1 (Bat1-MTS) and the MTS of Bat1-fused Bat2 (Bat2+MTS) from originating Bat1 and Bat2 genes. Bat2+MTS is relocalized into the mitochondria, because Bat2 localization is changed from cytosol to the mitochondria by addition of MTS, and can partially restore the valine content and growth in DELTAbat1DELTAbat2 cells. Bat1-MTS and Bat2+MTS function properly in DELTAbat1DELTAbat2 cells. Mutant DELTAbat1DELTAbat2 cells harboring Bat1-MTS grow similarly to DELTAbat1 cells
additional information
construction of two artificial genes encoding the mitochondrial-targeting signal (MTS)-deleted Bat1 (Bat1-MTS) and the MTS of Bat1-fused Bat2 (Bat2+MTS) from originating Bat1 and Bat2 genes. Bat2+MTS is relocalized into the mitochondria, because Bat2 localization is changed from cytosol to the mitochondria by addition of MTS, and can partially restore the valine content and growth in DELTAbat1DELTAbat2 cells. Bat1-MTS and Bat2+MTS function properly in DELTAbat1DELTAbat2 cells. Mutant DELTAbat1DELTAbat2 cells harboring Bat1-MTS grow similarly to DELTAbat1 cells
additional information
construction of two artificial genes encoding the mitochondrial-targeting signal (MTS)-deleted Bat1 (Bat1-MTS) and the MTS of Bat1-fused Bat2 (Bat2+MTS) from originating Bat1 and Bat2 genes. Bat2+MTS is relocalized into the mitochondria, because Bat2 localization is changed from cytosol to the mitochondria by addition of MTS, and can partially restore the valine content and growth in DELTAbat1DELTAbat2 cells. Bat1-MTS and Bat2+MTS function properly in DELTAbat1DELTAbat2 cells. Mutant DELTAbat1DELTAbat2 cells harboring Bat1-MTS grow similarly to DELTAbat1 cells
additional information
-
construction of two artificial genes encoding the mitochondrial-targeting signal (MTS)-deleted Bat1 (Bat1-MTS) and the MTS of Bat1-fused Bat2 (Bat2+MTS) from originating Bat1 and Bat2 genes. Bat2+MTS is relocalized into the mitochondria, because Bat2 localization is changed from cytosol to the mitochondria by addition of MTS, and can partially restore the valine content and growth in DELTAbat1DELTAbat2 cells. Bat1-MTS and Bat2+MTS function properly in DELTAbat1DELTAbat2 cells. Mutant DELTAbat1DELTAbat2 cells harboring Bat1-MTS grow similarly to DELTAbat1 cells
additional information
generation of a BY4741 bat1 deletion strain, phenotype, overview
additional information
-
generation of a BY4741 bat1 deletion strain, phenotype, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene BAT2, overexpression in Saccharomyces cerevisiae taz1DELTA mutant strain
expressed in the industrial wine yeast strain Saccharomyces cerevisiae VIN13
-
gene BAT1, overexpression in Saccharomyces cerevisiae taz1DELTA mutant strain
recombinant expression of C-terminally GFP-tagged wild-type Bat1 and A234D mutant Bat1 in the Bat1-deletion strain
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
isobutanol and other branched-chain higher alcohols (BCHAs) are promising advanced biofuels derived from the degradation of branched-chain amino acids (BCAAs). The yeast Saccharomyces cerevisiae is a particularly attractive host for the production of BCHAs due to its high tolerance to alcohols and prevalent use in the bioethanol industry. Degradation of BCAAs begins with transamination reactions, catalyzed by branched-chain amino acid transaminases (BCATs) located in the mitochondria (Bat1p) and cytosol (Bat2p)
nutrition
-
influences aroma and flavour compound formation and the sensory characteristics of wines and distillates
synthesis
isobutanol and other branched-chain higher alcohols (BCHAs) are promising advanced biofuels derived from the degradation of branched-chain amino acids (BCAAs). The yeast Saccharomyces cerevisiae is a particularly attractive host for the production of BCHAs due to its high tolerance to alcohols and prevalent use in the bioethanol industry. Degradation of BCAAs begins with transamination reactions, catalyzed by branched-chain amino acid transaminases (BCATs) located in the mitochondria (Bat1p) and cytosol (Bat2p)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kispal, G.; Steiner, H.; Court, D.A.; Rolinski, B.; Lill, R.
Mitochondrial and cytosolic branched-chain amino acid transaminases from yeast, homologs of the myc oncogene-regulated Eca39 protein
J. Biol. Chem.
271
24458-24464
1996
Saccharomyces cerevisiae (P38891), Saccharomyces cerevisiae (P47176), Saccharomyces cerevisiae
Eden, A.; Van Nedervelde, L.; Drukker, M.; Benvenisty, N.; Debourg, A.
Involvement of branched-chain amino acid aminotransferases in the production of fusel alcohols during fermentation in yeast
Appl. Microbiol. Biotechnol.
55
296-300
2001
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P47176)
Lin, H.M.; Kaneshige, M.; Zhao, L.; Zhang, X.; Hanover, J.A.; Cheng, S.Y.
An isoform of branched-chain aminotransferase is a novel co-repressor for thyroid hormone nuclear receptors
J. Biol. Chem.
276
48196-48205
2001
Homo sapiens, Homo sapiens (O15382), Saccharomyces cerevisiae (P47176), Saccharomyces cerevisiae
Lilly, M.; Bauer, F.F.; Styger, G.; Lambrechts, M.G.; Pretorius, I.S.
The effect of increased branched-chain amino acid transaminase activity in yeast on the production of higher alcohols and on the flavour profiles of wine and distillates
FEMS Yeast Res.
6
726-743
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
Kingsbury, J.M.; Sen, N.D.; Cardenas, M.E.
Branched-chain aminotransferases control TORC1 signaling in Saccharomyces cerevisiae
PLoS Genet.
11
e1005714
2015
Saccharomyces cerevisiae
Koonthongkaew, J.; Toyokawa, Y.; Ohashi, M.; Large, C.R.L.; Dunham, M.J.; Takagi, H.
Effect of the Ala234Asp replacement in mitochondrial branched-chain amino acid aminotransferase on the production of BCAAs and fusel alcohols in yeast
Appl. Microbiol. Biotechnol.
104
7915-7925
2020
Saccharomyces cerevisiae (P38891), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P38891)
Antunes, D.; Chowdhury, A.; Aich, A.; Saladi, S.; Harpaz, N.; Stahl, M.; Schuldiner, M.; Herrmann, J.M.; Rehling, P.; Rapaport, D.
Overexpression of branched-chain amino acid aminotransferases rescues the growth defects of cells lacking the Barth syndrome-related gene TAZ1
J. Mol. Med.
97
269-279
2019
Saccharomyces cerevisiae (P38891), Saccharomyces cerevisiae (P47176), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P38891), Saccharomyces cerevisiae ATCC 204508 (P47176)
Hammer, S.K.; Avalos, J.L.
Uncovering the role of branched-chain amino acid transaminases in Saccharomyces cerevisiae isobutanol biosynthesis
Metab. Eng.
44
302-312
2017
Saccharomyces cerevisiae (P38891), Saccharomyces cerevisiae (P47176), Saccharomyces cerevisiae ATCC 204508 (P38891), Saccharomyces cerevisiae ATCC 204508 (P47176)
Takpho, N.; Watanabe, D.; Takagi, H.
Valine biosynthesis in Saccharomyces cerevisiae is regulated by the mitochondrial branched-chain amino acid aminotransferase Bat1
Microb. Cell
5
293-299
2018
Saccharomyces cerevisiae (P38891), Saccharomyces cerevisiae (P47176), Saccharomyces cerevisiae
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Release 2023.1 (January 2023)
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