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Literature summary extracted from

  • Wang, J.; Wu, Y.; Sun, X.; Yuan, Q.; Yan, Y.
    De novo biosynthesis of glutarate via alpha-keto acid carbon chain extension and decarboxylation pathway in Escherichia coli (2017), ACS Synth. Biol., 6, 1922-1930 .
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.1.87 synthesis novel glutarate biosynthetic pathway by incorporation of a +1 carbon chain extension pathway from 2-oxoglutarate in combination with 2-oxo acid decarboxylation pathway in Escherichia coli. Introduction of homocitrate synthase, homoaconitase and homoisocitrate dehydrogenase from Saccharomyces cerevisiae into Escherichia coli enables +1 carbon extension from 2-oxoglutarate to 2-oxoadipate, which is subsequently converted into glutarate by a promiscuous 2-oxo acid decarboxylase (KivD) and a succinate semialdehyde dehydrogenase (GabD). The recombinant Escherichia coli coexpressing all five genes produces 0.3 g/l glutarate from glucose. To further improve the titers, 2-oxoglutarate is rechanneled into carbon chain extension pathway via the clustered regularly interspersed palindromic repeats system mediated interference (CRISPRi) of essential genes sucA and sucB in tricarboxylic acid cycle. The final strain can produce 0.42 g/l glutarate, which is increased by 40% compared with the parental strain. Glutarate is one of the most potential building blocks for bioplastics Saccharomyces cerevisiae
2.3.3.14 synthesis novel glutarate biosynthetic pathway by incorporation of a +1 carbon chain extension pathway from 2-oxoglutarate in combination with 2-oxo acid decarboxylation pathway in Escherichia coli. Introduction of homocitrate synthase, homoaconitase and homoisocitrate dehydrogenase from Saccharomyces cerevisiae into Escherichia coli enables +1 carbon extension from 2-oxoglutarate to 2-oxoadipate, which is subsequently converted into glutarate by a promiscuous 2-oxo acid decarboxylase (KivD) and a succinate semialdehyde dehydrogenase (GabD). The recombinant Escherichia coli coexpressing all five genes produces 0.3 g/l glutarate from glucose. To further improve the titers, 2-oxoglutarate is rechanneled into carbon chain extension pathway via the clustered regularly interspersed palindromic repeats system mediated interference (CRISPRi) of essential genes sucA and sucB in tricarboxylic acid cycle. The final strain can produce 0.42 g/l glutarate, which is increased by 40% compared with the parental strain. Glutarate is one of the most potential building blocks for bioplastics Saccharomyces cerevisiae
4.2.1.36 synthesis glutarate biosynthetic pathway by incorporation of a +1 carbon chain extension pathway from 2-oxoglutarate in combination with 2-oxo acid decarboxylation pathway in Escherichia coli. Introduction of homocitrate synthase, homoaconitase and homoisocitrate dehydrogenase from Saccharomyces cerevisiae into Escherichia coli enables +1 carbon extension from 2-oxoglutarate to 2-oxoadipate, which is subsequently converted into glutarate by a promiscuous 2-oxo acid decarboxylase (KivD) and a succinate semialdehyde dehydrogenase (GabD). The recombinant Escherichia coli coexpressing all five genes produces 0.3 g/l glutarate from glucose. To further improve the titers, 2-oxoglutarate is rechanneled into carbon chain extension pathway via the clustered regularly interspersed palindromic repeats system mediated interference (CRISPRi) of essential genes sucA and sucB in tricarboxylic acid cycle. The final strain can produce 0.42 g/l glutarate, which is increased by 40% compared with the parental strain. Glutarate is one of the most potential building blocks for bioplastics Saccharomyces cerevisiae

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.87 expression in Escherichia coli. Introduction of homocitrate synthase, homoaconitase and homoisocitrate dehydrogenase from Saccharomyces cerevisiae into Escherichia coli enables +1 carbon extension from 2-oxoglutarate to 2-oxoadipate, which is subsequently converted into glutarate by a promiscuous 2-oxo acid decarboxylase (KivD) and a succinate semialdehyde dehydrogenase (GabD) Saccharomyces cerevisiae
2.3.3.14 expression in Escherichia coli. Introduction of homocitrate synthase, homoaconitase and homoisocitrate dehydrogenase from Saccharomyces cerevisiae into Escherichia coli enables +1 carbon extension from 2-oxoglutarate to 2-oxoadipate, which is subsequently converted into glutarate by a promiscuous 2-oxo acid decarboxylase (KivD) and a succinate semialdehyde dehydrogenase (GabD) Saccharomyces cerevisiae
4.2.1.36 expression in Escherichia coli. Introduction of homocitrate synthase, homoaconitase and homoisocitrate dehydrogenase from Saccharomyces cerevisiae into Escherichia coli enables +1 carbon extension from 2-oxoglutarate to 2-oxoadipate, which is subsequently converted into glutarate by a promiscuous 2-oxo acid decarboxylase (KivD) and a succinate semialdehyde dehydrogenase (GabD) Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.87 Saccharomyces cerevisiae P40495
-
-
1.1.1.87 Saccharomyces cerevisiae ATCC 204508 P40495
-
-
2.3.3.14 Saccharomyces cerevisiae P48570
-
-
2.3.3.14 Saccharomyces cerevisiae ATCC 204508 P48570
-
-
4.2.1.36 Saccharomyces cerevisiae P49367
-
-
4.2.1.36 Saccharomyces cerevisiae ATCC 204508 P49367
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.87 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
-
Saccharomyces cerevisiae 2-oxoadipate + CO2 + NADH + H+
-
?
1.1.1.87 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
-
Saccharomyces cerevisiae ATCC 204508 2-oxoadipate + CO2 + NADH + H+
-
?
2.3.3.14 acetyl-CoA + H2O + 2-oxoglutarate
-
Saccharomyces cerevisiae (2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
?
2.3.3.14 acetyl-CoA + H2O + 2-oxoglutarate
-
Saccharomyces cerevisiae ATCC 204508 (2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
-
?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.87 HICDH
-
Saccharomyces cerevisiae
1.1.1.87 LYS12
-
Saccharomyces cerevisiae
2.3.3.14 HCS
-
Saccharomyces cerevisiae
2.3.3.14 LYS20
-
Saccharomyces cerevisiae
4.2.1.36 Homoaconitase
-
Saccharomyces cerevisiae
4.2.1.36 LYS4
-
Saccharomyces cerevisiae