An NADP-linked acetoacetyl CoA reductase from Zoogloea ramigera

1977 ◽  
Vol 114 (3) ◽  
pp. 211-217 ◽  
Author(s):  
Terumi Saito ◽  
Tetsuya Fukui ◽  
Fumiaki Ikeda ◽  
Yoshimasa Tanaka ◽  
Kenkichi Tomita
Keyword(s):  
Coa Reductase ◽  
Acetoacetyl Coa Reductase ◽  
Zoogloea Ramigera

An NAD-Linked Acetoacetyl-CoA Reductase from Zoogloea ramigera I-16-M

1981 ◽  
Vol 118 (1) ◽  
pp. 53-59 ◽  
Author(s):  
Hidetoshi SHUTO ◽  
Tetsuya FUKUL ◽  
Terumi SAITO ◽  
Yuri SHIRAKURA ◽  
Kenkichi TOMITA
Keyword(s):  
Coa Reductase ◽  
Acetoacetyl Coa Reductase ◽  
Zoogloea Ramigera

scholarly journals Acetoacetyl Coenzyme A Reductase and Polyhydroxybutyrate Synthesis in Rhizobium(Cicer) sp. Strain CC 1192

1998 ◽  
Vol 64 (8) ◽  
pp. 2859-2863 ◽  
Author(s):  
Shahid N. Chohan ◽  
Les Copeland
Keyword(s):  
Coenzyme A ◽  
Citrate Synthase ◽  
Living Cells ◽  
High Ratio ◽  
Free Living ◽  
Insoluble Material ◽  
Living State ◽  
Biochemical Level ◽  
Coa Reductase ◽  
Acetoacetyl Coa Reductase

ABSTRACT Biochemical controls that regulate the biosynthesis of poly-3-hydroxybutyrate (PHB) were investigated in Rhizobium(Cicer) sp. strain CC 1192. This species is of interest for studying PHB synthesis because the polymer accumulates to a large extent in free-living cells but not in bacteroids during nitrogen-fixing symbiosis with chickpea (Cicer arietinumL.) plants. Evidence is presented that indicates that CC 1192 cells retain the enzymic capacity to synthesize PHB when they differentiate from the free-living state to the bacteroid state. This evidence includes the incorporation by CC 1192 bacteroids of radiolabel from [14C]malate into 3-hydroxybutyrate which was derived by chemically degrading insoluble material from bacteroid pellets. Furthermore, the presence of an NADPH-dependent acetoacetyl coenzyme A (CoA) reductase, which was specific forR-(−)-3-hydroxybutyryl-CoA and NADP+ in the oxidative direction, was demonstrated in extracts from free-living and bacteroid cells of CC 1192. Activity of this enzyme in the reductive direction appeared to be regulated at the biochemical level mainly by the availability of substrates. The CC 1192 cells also contained an NADH-specific acetoacetyl-CoA reductase which oxidizedS-(+)-3-hydroxybutyryl-CoA. A membrane preparation from CC 1192 bacteroids readily oxidized NADH but not NADPH, which is suggested to be a major source of reductant for nitrogenase. Thus, a high ratio of NADPH to NADP+, which could enhance delivery of reductant to nitrogenase, could also favor the reduction of acetoacetyl-CoA for PHB synthesis. This would mean that fine controls that regulate the partitioning of acetyl-CoA between citrate synthase and 3-ketothiolase are important in determining whether PHB accumulates.

Isolation and partial characterization of Bacillus megaterium mutants deficient in poly(3-hydroxybutyrate) synthesis

1995 ◽  
Vol 41 (13) ◽  
pp. 77-79 ◽  
Author(s):  
Mirtha E. Floccari ◽  
Nancy I. López ◽  
Beatriz S. Méndez ◽  
Ursula Pieper Fürst ◽  
Alexander Steinbüchel
Keyword(s):  
Bacillus Megaterium ◽  
Allyl Alcohol ◽  
Chromatographic Analysis ◽  
Partial Characterization ◽  
Enzymatic Characterization ◽  
Gas Chromatographic Analysis ◽  
Selection For ◽  
Coa Reductase ◽  
Acetoacetyl Coa Reductase

Poly(3-hydroxybutyrate) (PHB)-negative mutants of Bacillus megaterium were isolated following mutagenesis with N-methyl-N′-nitro-N-nitrosoguanidine. Different strategies were used for isolation, including ultracentrifugation through sucrose gradients and selection for resistance to allyl alcohol. The mutants were detected on agar plates by staining the colonies with Sudan Black. Four mutants did not synthesize any PHB as revealed by gas chromatographic analysis. The enzymatic characterization showed no or extremely low synthase activity for all of the mutants. In contrast, no significant alterations were observed in the β-ketothiolase and the NADPH-dependent acetoacetyl-CoA reductase activities. All mutants sporulated in complete and minimal media.Key words: poly(3-hydroxybutyrate), synthase, mutants, Bacillus megaterium.

scholarly journals Crystal structure of acetoacetyl-CoA reductase from Rickettsia felis

2021 ◽  
Vol 77 (2) ◽  
pp. 54-60
Author(s):  
Justas V. Rodarte ◽  
Jan Abendroth ◽  
Thomas E. Edwards ◽  
Donald D. Lorimer ◽  
Bart L. Staker ◽  
...  
Keyword(s):  
Spotted Fever ◽  
Effective Means ◽  
Infectious Agent ◽  
Unknown Origin ◽  
Acid Synthesis ◽  
Rickettsia Felis ◽  
Wide Range ◽  
Coa Reductase ◽  
Acetoacetyl Coa Reductase

Rickettsia felis, a Gram-negative bacterium that causes spotted fever, is of increasing interest as an emerging human pathogen. R. felis and several other Rickettsia strains are classed as National Institute of Allergy and Infectious Diseases priority pathogens. In recent years, R. felis has been shown to be adaptable to a wide range of hosts, and many fevers of unknown origin are now being attributed to this infectious agent. Here, the structure of acetoacetyl-CoA reductase from R. felis is reported at a resolution of 2.0 Å. While R. felis acetoacetyl-CoA reductase shares less than 50% sequence identity with its closest homologs, it adopts a fold common to other short-chain dehydrogenase/reductase (SDR) family members, such as the fatty-acid synthesis II enzyme FabG from the prominent pathogens Staphylococcus aureus and Bacillus anthracis. Continued characterization of the Rickettsia proteome may prove to be an effective means of finding new avenues of treatment through comparative structural studies.

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