scholarly journals A synthetic enzymatic pathway for extremely thermophilic acetone production based on the unexpectedly thermostable acetoacetate decarboxylase fromClostridium acetobutylicum

2018 ◽  
Vol 115 (12) ◽  
pp. 2951-2961 ◽  
Author(s):  
Benjamin M. Zeldes ◽  
Christopher T. Straub ◽  
Jonathan K. Otten ◽  
Michael W. W. Adams ◽  
Robert M. Kelly
Keyword(s):  
Acetoacetate Decarboxylase

scholarly journals Engineered Synthetic Pathway for Isopropanol Production in Escherichia coli

2007 ◽  
Vol 73 (24) ◽  
pp. 7814-7818 ◽  
Author(s):  
T. Hanai ◽  
S. Atsumi ◽  
J. C. Liao
Keyword(s):  
Escherichia Coli ◽  
Secondary Alcohol ◽  
Clostridium Beijerinckii ◽  
Synthetic Pathway ◽  
E Coli ◽  
Coa Transferase ◽  
Secondary Alcohol Dehydrogenase ◽  
Acetoacetate Decarboxylase ◽  
Shake Flasks ◽  
K 12

ABSTRACT A synthetic pathway was engineered in Escherichia coli to produce isopropanol by expressing various combinations of genes from Clostridium acetobutylicum ATCC 824, E. coli K-12 MG1655, Clostridium beijerinckii NRRL B593, and Thermoanaerobacter brockii HTD4. The strain with the combination of C. acetobutylicum thl (acetyl-coenzyme A [CoA] acetyltransferase), E. coli atoAD (acetoacetyl-CoA transferase), C. acetobutylicum adc (acetoacetate decarboxylase), and C. beijerinckii adh (secondary alcohol dehydrogenase) achieved the highest titer. This strain produced 81.6 mM isopropanol in shake flasks with a yield of 43.5% (mol/mol) in the production phase. To our knowledge, this work is the first to produce isopropanol in E. coli, and the titer exceeded that from the native producers.

Head-space gas-chromatographic determination of 3-hydroxybutyrate in plasma after enzymic reactions, and the relationship among the three ketone bodies.

1985 ◽  
Vol 31 (4) ◽  
pp. 596-598 ◽  
Author(s):  
M Kimura ◽  
K Kobayashi ◽  
A Matsuoka ◽  
K Hayashi ◽  
Y Kimura
Keyword(s):  
Ketone Bodies ◽  
Normal Subjects ◽  
Chromatographic Determination ◽  
Diabetic Patients ◽  
Head Space ◽  
Analytical Recovery ◽  
Acetoacetate Decarboxylase ◽  
Reproducible Method ◽  
The Relationship

Abstract In this sensitive, reproducible method for determination of D-3-hydroxybutyrate (3-OHB) in plasma, it is converted to acetone by use of 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30)/lactate dehydrogenase (EC 1.1.1.27) coupled with acetoacetate decarboxylase (EC 4.1.1.4). The resulting acetone is detected by head-space gas chromatography. The lowest concentration of 3-OHB detectable in plasma was 2 mumol/L. The calibration curve showed a linear relationship for 3-OHB concentration from 0 to 5 mmol/L (r = 0.999). Analytical recovery of 3-OHB (50 mumol/L) was 97.9 (SD 3.8)%. The method was developed for determination of the three ketone bodies in plasma. The ratio of acetone to acetoacetate was not significantly different (p greater than 0.2) between normals (n = 31) and diabetics (n = 86). In normal subjects, the ratio of 3-OHB to acetoacetate was 1.20 (SD 0.44). In diabetic patients, the ratio correlated with the logarithm of the total ketone body concentration (r = 0.828).

Acetoacetate Decarboxylase. Subunits and Properties*

Biochemistry ◽  
1966 ◽  
Vol 5 (3) ◽  
pp. 823-833 ◽  
Author(s):  
Florence Lederer ◽  
Stephen M. Coutts ◽  
Richard A. Laursen ◽  
F. H. Westheimer
Keyword(s):  
Acetoacetate Decarboxylase

Conversion of levulinic acid to 2-butanone by acetoacetate decarboxylase from Clostridium acetobutylicum

2013 ◽  
Vol 97 (12) ◽  
pp. 5627-5634 ◽  
Author(s):  
Kyoungseon Min ◽  
Seil Kim ◽  
Taewoo Yum ◽  
Yunje Kim ◽  
Byoung-In Sang ◽  
...  
Keyword(s):  
Clostridium Acetobutylicum ◽  
Levulinic Acid ◽  
Acetoacetate Decarboxylase

scholarly journals Acetoacetate decarboxylase and a peptide with similar activity produced by Bacillus polymyxa A-57.

1986 ◽  
Vol 50 (10) ◽  
pp. 2509-2516 ◽  
Author(s):  
Yukio KIMURA ◽  
Noriko YASUDA ◽  
Hiroko TANIGAKI-NAGAE ◽  
Toshikatsu NAKABAYASHI ◽  
Hisami MATSUNAGA ◽  
...  
Keyword(s):  
Bacillus Polymyxa ◽  
Similar Activity ◽  
Acetoacetate Decarboxylase
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