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Literature summary extracted from

  • Matsumoto, K.; Yamada, M.; Leong, C.; Jo, S.; Kuzuyama, T.; Taguchi, S.
    A new pathway for poly(3-hydroxybutyrate) production in Escherichia coli and Corynebacterium glutamicum by functional expression of a new acetoacetyl-coenzyme A synthase (2011), Biosci. Biotechnol. Biochem., 75, 364-366.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.3.1.194 synthesis usage of the enzyme for recombinant high-level production of poly(3-hydroxybutyrate), P(3HB), in Escherichia coli and Corynebacterium glutamicum. P(3HB) is the natural aliphatic polyester that can be processed into a wide variety of consumer products, including plastics, films and fibers Streptomyces sp.
2.3.1.304 synthesis usage of the enzyme for recombinant high-level production of poly(3-hydroxybutyrate), P(3HB), in Escherichia coli and Corynebacterium glutamicum. P(3HB) is the natural aliphatic polyester that can be processed into a wide variety of consumer products, including plastics, films and fibers Cupriavidus necator

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.194 co-expression of polyhydroxyalkanoate synthase, PhaC, from Ralstonia eutropha with acetoacetyl-CoA synthetase in Escherichia coli and Corynebacterium glutamicum leading to enhanced production of polyhydroxybutanoates, by cloning the AACS gene into the phaABC operon of Ralstonia eutropha. Overexpression of AACS leads to a great enhancement of the malonyl-CoA pool in Escherichia coli Streptomyces sp.
2.3.1.194 recombinant expression of AACS in Corynebacterium glutamicum and Escherichia coli leads to aquired ability to form poly(3-hydroxybutyrate) in the transformed organisms by 19.7 wt% and 10.5 wt%, respectively, biosynthetic pathway, overview Streptomyces sp.
2.3.1.304 co-expression of PhaC with acetoacetyl-CoA synthetase, AACS, from Streptomyces sp. CL190 in Escherichia coli and Corynebacterium glutamicum leading to enhanced production of polyhydroxybutanoates, by cloning the AACS gene into the phaABC operon of Ralstonia eutropha Cupriavidus necator

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.194 acetyl-CoA + malonyl-CoA Streptomyces sp.
-
 acetoacetyl-CoA + CoA + CO2
-
 ?
2.3.1.194 acetyl-CoA + malonyl-CoA Streptomyces sp.
-
 CoA + acetoacetyl-CoA + CO2
-
 ir
2.3.1.304 3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n Cupriavidus necator
-
 [(R)-3-hydroxybutanoate]n+1 + CoA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.194 Streptomyces sp.
-
-
-
2.3.1.194 Streptomyces sp.
-
 gene nphT7
-
2.3.1.304 Cupriavidus necator
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.194 acetyl-CoA + malonyl-CoA
-
 Streptomyces sp. acetoacetyl-CoA + CoA + CO2
-
 ?
2.3.1.194 acetyl-CoA + malonyl-CoA
-
 Streptomyces sp. CoA + acetoacetyl-CoA + CO2
-
 ir
2.3.1.304 3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
-
 Cupriavidus necator [(R)-3-hydroxybutanoate]n+1 + CoA
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.194 AACS
-
 Streptomyces sp.
2.3.1.194 Acetoacetyl-CoA synthase
-
 Streptomyces sp.
2.3.1.194 Acetoacetyl-CoA synthetase
-
 Streptomyces sp.
2.3.1.194 acetoacetyl-coenzyme A synthase
-
 Streptomyces sp.
2.3.1.194 More the enzyme belongs to the thiolase superfamily of enzymes Streptomyces sp.
2.3.1.194 NphT7
-
 Streptomyces sp.
2.3.1.304 PhaC
-
 Cupriavidus necator
2.3.1.304 polyhydroxyalkanoate synthase
-
 Cupriavidus necator

General Information

EC Number General Information Comment Organism
2.3.1.194 metabolism polyhydroxyalkanoate synthase, PhaC, catalyzes generation of (R)-3-hydroxybutyrate monomers from two acetyl-CoA molecules, and further of short-chain length polyhydroxyalkanoates, PHAs. The malonyl-CoA availability is a limiting factor to synthesis of poly(3-hydroxybutyrate), P(3HB), thus acetoacetyl-CoA synthetase, which is controlling the malonyl-CoA pool, is an important enzyme for increasing the P(3HB) production Streptomyces sp.
2.3.1.194 additional information alterations in acety-CoA carboxylase activity to optimize the acetyl-CoA/malonyl-CoA ratio might be an effective way to increase poly(3-hydroxybutyrate) production via the AACS-catalyzed paythway Streptomyces sp.
2.3.1.304 metabolism PhaC is involved in the biosynthetic pathway for generation of (R)-3-hydroxybutyrate monomers from two acetyl-CoA molecules, and further of short-chain length polyhydroxyalkanoates, PHAs. The malonyl-CoA availability is a limiting factor to synthesis of poly(3-hydroxybutyrate), P(3HB), thus acetoacetyl-CoA synthetase, which is controlling the malonyl-CoA pool, is an important enzyme for increasing the P(3HB) production Cupriavidus necator