Alteration of cofactor specificity of the acrylyl-CoA reductase from Escherichia coli

2021 ◽  
Author(s):  
Aleksander S. Reshetnikov ◽  
Sergey Y. But ◽  
Olga N. Rozova ◽  
Ildar I. Mustakhimov ◽  
Valentina N. Khmelenina
Keyword(s):  
Escherichia Coli ◽  
Cofactor Specificity ◽  
Coa Reductase

Selection of an Escherichia coli host that expresses mutant forms of Mycobacterium tuberculosis 2-trans enoyl-ACP(CoA) reductase and 3-ketoacyl-ACP(CoA) reductase enzymes

2004 ◽  
Vol 34 (1) ◽  
pp. 118-125 ◽  
Author(s):  
Simone S Poletto ◽  
Isabel O da Fonseca ◽  
Luiz P.S de Carvalho ◽  
Luiz A Basso ◽  
Diógenes S Santos
Keyword(s):  
Escherichia Coli ◽  
Mycobacterium Tuberculosis ◽  
Coa Reductase ◽  
Mutant Forms ◽  
Selection Of

Studies on the Metabolism of Unsaturated Fatty Acids. VIII. Induction of 2,4-Dienoyl-CoA Reductase in Escherichia coli on the Addition of Unsaturated Fatty Acids1

1982 ◽  
Vol 91 (4) ◽  
pp. 1453-1456 ◽  
Author(s):  
Michinao MIZUGAKI ◽  
Tomoko NISHIMAKI ◽  
Hirotaka YAMAMOTO ◽  
Sumiko NISHIMURA ◽  
Mataichi SAGI ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Unsaturated Fatty Acids ◽  
Coa Reductase

scholarly journals Crystal Structure of Lactaldehyde Dehydrogenase from Escherichia coli and Inferences Regarding Substrate and Cofactor Specificity

2007 ◽  
Vol 366 (2) ◽  
pp. 481-493 ◽  
Author(s):  
Luigi Di Costanzo ◽  
German A. Gomez ◽  
David W. Christianson
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Cofactor Specificity

scholarly journals Cloning of a Novel Aldo-Keto Reductase Gene from Klebsiella sp. Strain F51-1-2 and Its Functional Expression in Escherichia coli

2007 ◽  
Vol 73 (15) ◽  
pp. 4959-4965 ◽  
Author(s):  
Hong Jiang ◽  
Chao Yang ◽  
Hong Qu ◽  
Zheng Liu ◽  
Q. S. Fu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Organophosphorus Compounds ◽  
Functional Expression ◽  
Nitrilotriacetic Acid ◽  
Coding Region ◽  
Reductive Transformation ◽  
Cofactor Specificity ◽  
Expression In Escherichia Coli ◽  
Reductase Gene ◽  
One Step

ABSTRACT A soil bacterium capable of metabolizing organophosphorus compounds by reducing the P═S group in the molecules was taxonomically identified as Klebsiella sp. strain F51-1-2. The gene involved in the reduction of organophosphorus compounds was cloned from this strain by the shotgun technique, and the deduced protein (named AKR5F1) showed homology to members of the aldo-keto reductase (AKR) superfamily. The intact coding region for AKR5F1 was subcloned into vector pET28a and overexpressed in Escherichia coli BL21(DE3). Recombinant His6-tagged AKR5F1 was purified in one step using Ni-nitrilotriacetic acid affinity chromatography. Assays for cofactor specificity indicated that reductive transformation of organophosphorus compounds by the recombinant AKR5F1 specifically required NADH. The kinetic constants of the purified recombinant AKR5F1 toward six thion organophosphorus compounds were determined. For example, the Km and k cat values of reductive transformation of malathion by the purified recombinant AKR5F1 are 269.5 ± 47.0 μΜ and 25.7 ± 1.7 min−1, respectively. Furthermore, the reductive transformation of organophosphorus compounds can be largely explained by structural modeling.

scholarly journals Coproduction of Acetaldehyde and Hydrogen during Glucose Fermentation by Escherichia coli

2011 ◽  
Vol 77 (18) ◽  
pp. 6441-6450 ◽  
Author(s):  
Huilin Zhu ◽  
Ramon Gonzalez ◽  
Thomas A. Bobik
Keyword(s):  
Escherichia Coli ◽  
Alcohol Dehydrogenase ◽  
Production Rate ◽  
Dehydrogenase Activity ◽  
Allyl Alcohol ◽  
Glucose Fermentation ◽  
Acetyl Coa ◽  
Acetaldehyde Dehydrogenase ◽  
Content Type ◽  
Coa Reductase

ABSTRACTEscherichia coliK-12 strain MG1655 was engineered to coproduce acetaldehyde and hydrogen during glucose fermentation by the use of exogenous acetyl-coenzyme A (acetyl-CoA) reductase (for the conversion of acetyl-CoA to acetaldehyde) and the native formate hydrogen lyase. A putative acetaldehyde dehydrogenase/acetyl-CoA reductase fromSalmonella enterica(SeEutE) was cloned, produced at high levels, and purified by nickel affinity chromatography.In vitroassays showed that this enzyme had both acetaldehyde dehydrogenase activity (68.07 ± 1.63 μmol min−1mg−1) and the desired acetyl-CoA reductase activity (49.23 ± 2.88 μmol min−1mg−1). TheeutEgene was engineered into anE. colimutant lacking native glucose fermentation pathways (ΔadhE, ΔackA-pta, ΔldhA, and ΔfrdC). The engineered strain (ZH88) produced 4.91 ± 0.29 mM acetaldehyde while consuming 11.05 mM glucose but also produced 6.44 ± 0.26 mM ethanol. Studies showed that ethanol was produced by an unknown alcohol dehydrogenase(s) that converted the acetaldehyde produced by SeEutE to ethanol. Allyl alcohol was used to select for mutants with reduced alcohol dehydrogenase activity. Three allyl alcohol-resistant mutants were isolated; all produced more acetaldehyde and less ethanol than ZH88. It was also found that modifying the growth medium by adding 1 g of yeast extract/liter and lowering the pH to 6.0 further increased the coproduction of acetaldehyde and hydrogen. Under optimal conditions, strain ZH136 converted glucose to acetaldehyde and hydrogen in a 1:1 ratio with a specific acetaldehyde production rate of 0.68 ± 0.20 g h−1g−1dry cell weight and at 86% of the maximum theoretical yield. This specific production rate is the highest reported thus far and is promising for industrial application. The possibility of a more efficient “no-distill” ethanol fermentation procedure based on the coproduction of acetaldehyde and hydrogen is discussed.

Studies on the Metabolism of Unsaturated Fatty Acids. XII.1 Reaction Catalyzed by 2,4-Dienoyl-CoA Reductase of Escherichia coli

1983 ◽  
Vol 94 (2) ◽  
pp. 409-413 ◽  
Author(s):  
Michinao MIZUGAKI ◽  
Chiharu KIMURA ◽  
Tomoko NISHIMAKI ◽  
Akihiko KAWAGUCHI ◽  
Shigenobu OKUDA ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Unsaturated Fatty Acids ◽  
Coa Reductase
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