Characterization of acetoacetyl-CoA reductase (3-oxoreductase) from Streptomyces coelicolor: Its possible role in polyhydroxybutyrate biosynthesis

1983 ◽  
Vol 11 (5) ◽  
pp. 598-599 ◽  
Author(s):  
NEVILLE M. PACKTER ◽  
STEPHEN FLATMAN
Keyword(s):  
Streptomyces Coelicolor ◽  
Coa Reductase ◽  
Acetoacetyl Coa Reductase

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.

scholarly journals The purification and characterization of acetoacetyl-coenzyme A reductase from Azotobacter beijerinckii

1971 ◽  
Vol 121 (2) ◽  
pp. 309-316 ◽  
Author(s):  
G. A. F. Ritchie ◽  
P. J. Senior ◽  
E. A. Dawes
Keyword(s):  
Substrate Specificity ◽  
Reaction Rate ◽  
Acyl Carrier Protein ◽  
Thiol Group ◽  
Carrier Protein ◽  
Purification And Characterization ◽  
Michaelis Constants ◽  
Coa Reductase ◽  
Acetoacetyl Coa Reductase

A soluble acetoacetyl-CoA reductase (EC 1.1.1.36) was purified 54-fold from Azotobacter beijerinckii N.C.I.B. 9067 and the reaction product identified as d(−)-β-hydroxybutyryl-CoA. The Michaelis constants for acetoacetyl-CoA, NADPH and NADH were determined and the reaction rate was found to be some fivefold greater with NADPH than with NADH. At neutral pH the equilibrium greatly favours the formation of the reduced product. Substrate specificity was in the order: acetoacetyl-CoA>acetoacetylpantetheine>acetoacetyl-(acyl-carrier protein). The enzyme possesses a functional thiol group, suffers inactivation by oxygen and is inhibited by thiol-blocking reagents. Inhibition by p-chloromercuribenzoate is reversed by excess of dithiothreitol, which also protects the enzyme from inactivation by oxygen.

Cloning and characterization of the histidine biosynthetic gene cluster of Streptomyces coelicolor A3(2)

Gene ◽  
1990 ◽  
Vol 90 (1) ◽  
pp. 31-41 ◽  
Author(s):  
Danila Limauro ◽  
Alessandra Avitabile ◽  
Carmela Cappellano ◽  
Anna Maria Puglia ◽  
Carmelo B. Bruni
Keyword(s):  
Gene Cluster ◽  
Streptomyces Coelicolor ◽  
Biosynthetic Gene Cluster ◽  
Biosynthetic Gene

scholarly journals Molecular Characterization of a Poly-β-Hydroxybutyrate-Producing Microbacterium Isolate

2015 ◽  
Vol 3 (2) ◽  
pp. 143-150 ◽  
Author(s):  
Yehia A. Osman ◽  
Ahmed Abd Elrazak ◽  
Wesam Khater ◽  
EL-Shahat Nashy ◽  
Attia Mohamadeen
Keyword(s):  
Biosynthetic Pathway ◽  
Nitrogen Deficiency ◽  
Rrna Gene ◽  
Excess Carbon ◽  
Controlling Elements ◽  
Tree Data ◽  
Microbacterium Paraoxydans ◽  
Coa Reductase ◽  
Beta Hydroxybutyrate

Bacterial poly-β-hydroxybutyrate (PHB) is a natural, biodegradable polymer, which is accumulated in the cells as an energy reserve materialdue to depletion of nitrogen or phosphorous in the presence of excess carbon source. This polymer is foreseen to possess high industrialpotentiality and excellent alternative to the non-degradable petroleum-based plastics. In this study, we isolated and characterized a localbacterial strain WA81 which accumulated 18mg/L PHB after 72 h growth in mineral salt medium under nitrogen deficiency. The PHB granuleswere detected in the cells using TEM and the genes encode for this polymer were detected by oligonucleotide primers using PCR technology.The 16S rRNA gene nucleotide sequence for this isolate was used to construct a phylogentic tree against all available sequences in the GenBank.The phylogenetic tree data suggested that the closest type strain to the local bacterium is the Microbacterium paraoxydans CF36T and hencewe named it Microbacterium sp. strain WA81. Moreover, the set of enzymes responsible for the PHB biosynthetic pathway and their controllingelements were detected in this local isolate using PCR. The genes encode for the biosynthesis enzymes are phbA (β-ketothiolase), phbB(acetoacetly CoA reductase), phbC (PHB polymerase), while the genes encode for the controlling elements are phbP (phasin), phbZ (PHBdepolymerase). The novelty of this local bacterium lies in its ability to accumulate huge amounts of PHB in its cytoplasm and the presence ofa whole set of genes encode for the PHB biosynthetic and catabolic pathways of this polymer.Int J Appl Sci Biotechnol, Vol 3(2): 143-150 DOI: http://dx.doi.org/10.3126/ijasbt.v3i2.12277 

Tricorn Protease in Bacteria: Characterization of the Enzyme from Streptomyces coelicolor

2001 ◽  
Vol 382 (3) ◽  
Author(s):  
Noriko Tamura ◽  
Günther Pfeifer ◽  
Wolfgang Baumeister ◽  
Tomohiro Tamura
Keyword(s):  
Streptomyces Coelicolor
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