scholarly journals Partial Purifi cation and Characterization of the Recombinant Benzaldehyde Dehydrogenase from Rhodococcus ruber UKMP-5M

2017 ◽  
Vol 15 (1) ◽  
pp. 67-73
Author(s):  
Arezoo Tavakoli ◽  
Ainon Hamzah
Keyword(s):  
Rhodococcus Ruber ◽  
Benzaldehyde Dehydrogenase

Characterization of a protocatechuate catabolic gene cluster in Rhodococcus ruber OA1 involved in naphthalene degradation

2015 ◽  
Vol 66 (1) ◽  
pp. 469-478 ◽  
Author(s):  
Chao Li ◽  
Chunyang Zhang ◽  
Guanling Song ◽  
Hong Liu ◽  
Guihua Sheng ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Rhodococcus Ruber ◽  
Catabolic Gene ◽  
Naphthalene Degradation

Morphological, Physiological, and Molecular Characterization of a Newly Isolated Steroid-Degrading Actinomycete, Identified as Rhodococcus ruber Strain Chol-4

2009 ◽  
Vol 59 (5) ◽  
pp. 548-553 ◽  
Author(s):  
Laura Fernández de las Heras ◽  
Esther García Fernández ◽  
J. María Navarro Llorens ◽  
Julián Perera ◽  
Oliver Drzyzga
Keyword(s):  
Molecular Characterization ◽  
Rhodococcus Ruber

Kinetic characterization of Rhodococcus ruber DSM 44541 alcohol dehydrogenase A

2014 ◽  
Vol 99 ◽  
pp. 68-78 ◽  
Author(s):  
Emil Hamnevik ◽  
Cecilia Blikstad ◽  
Sara Norrehed ◽  
Mikael Widersten
Keyword(s):  
Alcohol Dehydrogenase ◽  
Rhodococcus Ruber ◽  
Kinetic Characterization

scholarly journals Cloning and Characterization of a Gene Cluster for Cyclododecanone Oxidation in Rhodococcus ruber SC1

2001 ◽  
Vol 183 (21) ◽  
pp. 6478-6486 ◽  
Author(s):  
Kristy Kostichka ◽  
Stuart M. Thomas ◽  
Katharine J. Gibson ◽  
Vasantha Nagarajan ◽  
Qiong Cheng
Keyword(s):  
Gene Cluster ◽  
Dicarboxylic Acids ◽  
Rhodococcus Ruber ◽  
Cyclic Ketones ◽  
E Coli ◽  
Flavin Monooxygenase ◽  
Dodecanedioic Acid ◽  
Cyclic Compounds

ABSTRACT Biological oxidation of cyclic ketones normally results in formation of the corresponding dicarboxylic acids, which are further metabolized in the cell. Rhodococcus ruber strain SC1 was isolated from an industrial wastewater bioreactor that was able to utilize cyclododecanone as the sole carbon source. A reverse genetic approach was used to isolate a 10-kb gene cluster containing all genes required for oxidative conversion of cyclododecanone to 1,12-dodecanedioic acid (DDDA). The genes required for cyclododecanone oxidation were only marginally similar to the analogous genes for cyclohexanone oxidation. The biochemical function of the enzymes encoded on the 10-kb gene cluster, the flavin monooxygenase, the lactone hydrolase, the alcohol dehydrogenase, and the aldehyde dehydrogenase, was determined in Escherichia coli based on the ability to convert cyclododecanone. Recombinant E. colistrains grown in the presence of cyclododecanone accumulated lauryl lactone, 12-hydroxylauric acid, and/or DDDA depending on the genes cloned. The cyclododecanone monooxygenase is a type 1 Baeyer-Villiger flavin monooxygenase (FAD as cofactor) and exhibited substrate specificity towards long-chain cyclic ketones (C11 to C15), which is different from the specificity of cyclohexanone monooxygenase favoring short-chain cyclic compounds (C5 to C7).

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