Literature summary for 1.1.1.36 extracted from

Yokoo, T.; Matsumoto, K.; Ooba, T.; Morimoto, K.; Taguchi, S.
Enhanced poly(3-hydroxybutyrate) production in transgenic tobacco BY-2 cells using engineered acetoacetyl-CoA reductase (2015), Biosci. Biotechnol. Biochem., 79, 986-988.

Application

Application	Comment	Organism
synthesis	the engineered enzyme mutant T173S can be used for increased production of poly(3-hydroxybutyrate) in a Corynebacterium glutamicum expression system	Cupriavidus necator

Cloned(Commentary)

Cloned (Comment)	Organism
gene phaB, recombinant expression of a PhaB mutant T173s enzyme from Ralstonia eutropha in Nicotiana tabacum cv. Bright Yellow-2 cells, the mutated PhaB increases the poly(3-hydroxybutyrate) (P(3HB)) content by threefold compared to control. Plasmids pRIphaC-phaB(WT) and pRIphaCphaB(TS) are introduced into BY-2 cells using the Agrobacterium-mediated transfection method. The PhaB-catalyzed reaction is suggested to be a rate-limiting step of P(3HB) biosynthesis in tobacco BY-2 cells	Cupriavidus necator

Cloned (Comment)

Organism

gene phaB, recombinant expression of a PhaB mutant T173s enzyme from Ralstonia eutropha in Nicotiana tabacum cv. Bright Yellow-2 cells, the mutated PhaB increases the poly(3-hydroxybutyrate) (P(3HB)) content by threefold compared to control. Plasmids pRIphaC-phaB(WT) and pRIphaCphaB(TS) are introduced into BY-2 cells using the Agrobacterium-mediated transfection method. The PhaB-catalyzed reaction is suggested to be a rate-limiting step of P(3HB) biosynthesis in tobacco BY-2 cells

Cupriavidus necator

Protein Variants

Protein Variants	Comment	Organism
T173S	by random mutagenesis and high-throughput screening, enzyme mutant engineering for increased production of poly(3-hydroxybutyrate) in a Corynebacterium glutamicum expression system	Cupriavidus necator

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
(R)-3-hydroxyacyl-CoA + NADP+	Cupriavidus necator	-	3-oxoacyl-CoA + NADPH + H+	-	r
(R)-3-hydroxyacyl-CoA + NADP+	Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1	-	3-oxoacyl-CoA + NADPH + H+	-	r

Organism

Organism	UniProt	Comment	Textmining
Cupriavidus necator	P14697	-	-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1	P14697	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(R)-3-hydroxyacyl-CoA + NADP+	-	Cupriavidus necator	3-oxoacyl-CoA + NADPH + H+	-	r
(R)-3-hydroxyacyl-CoA + NADP+	-	Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1	3-oxoacyl-CoA + NADPH + H+	-	r

Synonyms

Synonyms	Comment	Organism
NADPH-dependent acetoacetyl-CoA reductase	-	Cupriavidus necator
PhaB	-	Cupriavidus necator

Cofactor

Cofactor	Comment	Organism	Structure
NADP+	-	Cupriavidus necator
NADPH	-	Cupriavidus necator

General Information

General Information	Comment	Organism
metabolism	the enzyme is rate-limiting in poly(3-hydroxybutyrate) biosynthesis. Poly(3-hydroxybutyrate) (P(3HB)) is synthesized from acetyl-CoA via three successive reactions. Two molecules of acetyl-CoA are condensed into acetoacetyl-CoA by a beta-ketothiolase (PhaA). Then NADPH-dependent acetoacetyl-CoA reductase (PhaB) converts acetoacetyl-CoA into (R)-3-hydroxybutyryl-CoA (3HB-CoA), which is finally polymerized into P(3HB) by polyhydroxyalkanoate synthase (PhaC)	Cupriavidus necator