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Literature summary extracted from

  • Hammer, S.K.; Avalos, J.L.
    Uncovering the role of branched-chain amino acid transaminases in Saccharomyces cerevisiae isobutanol biosynthesis (2017), Metab. Eng., 44, 302-312 .
    View publication on PubMed

Application

EC Number Application Comment Organism
2.6.1.42 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) Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.6.1.42 cytosol
-
 Saccharomyces cerevisiae 5829
-
2.6.1.42 mitochondrion
-
 Saccharomyces cerevisiae 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.42 L-valine + 2-oxoglutarate Saccharomyces cerevisiae
-
 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate Saccharomyces cerevisiae ATCC 204508
-
 3-methyl-2-oxobutanoate + L-glutamate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.42 Saccharomyces cerevisiae P38891
-
-
2.6.1.42 Saccharomyces cerevisiae P47176
-
-
2.6.1.42 Saccharomyces cerevisiae ATCC 204508 P38891
-
-
2.6.1.42 Saccharomyces cerevisiae ATCC 204508 P47176
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.42 L-valine + 2-oxoglutarate
-
 Saccharomyces cerevisiae 3-methyl-2-oxobutanoate + L-glutamate
-
 r
2.6.1.42 L-valine + 2-oxoglutarate
-
 Saccharomyces cerevisiae ATCC 204508 3-methyl-2-oxobutanoate + L-glutamate
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.6.1.42 Bat1
-
 Saccharomyces cerevisiae
2.6.1.42 Bat1p
-
 Saccharomyces cerevisiae
2.6.1.42 BAT2
-
 Saccharomyces cerevisiae
2.6.1.42 Bat2p
-
 Saccharomyces cerevisiae
2.6.1.42 branched-chain amino acid transaminase
-
 Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.42 pyridoxal 5'-phosphate
-
 Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
2.6.1.42 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 Saccharomyces cerevisiae
2.6.1.42 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 Saccharomyces cerevisiae
2.6.1.42 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 Saccharomyces cerevisiae
2.6.1.42 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 Saccharomyces cerevisiae
2.6.1.42 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 Saccharomyces cerevisiae