scholarly journals The Fifth WS/DGAT Enzyme of the Bacterium Marinobacter aquaeolei  VT8

Lipids ◽  
2020 ◽  
Vol 55 (5) ◽  
pp. 479-494
Author(s):  
Katharina Vollheyde ◽  
Dan Yu ◽  
Ellen Hornung ◽  
Cornelia Herrfurth ◽  
Ivo Feussner
Keyword(s):  
Marinobacter Aquaeolei

scholarly journals Fatty Alcohols for Wax Esters in Marinobacter aquaeolei VT8: Two Optional Routes in the Wax Biosynthesis Pathway

2013 ◽  
Vol 79 (22) ◽  
pp. 7055-7062 ◽  
Author(s):  
Eric M. Lenneman ◽  
Janet M. Ohlert ◽  
Nagendra P. Palani ◽  
Brett M. Barney
Keyword(s):  
Fatty Alcohol ◽  
Fatty Acyl ◽  
Wax Esters ◽  
Transcriptional Analysis ◽  
Wax Ester ◽  
Fatty Aldehyde ◽  
Marinobacter Aquaeolei

ABSTRACTThe biosynthesis of wax esters in bacteria is accomplished by a unique pathway that combines a fatty alcohol and a fatty acyl coenzyme A substrate. Previousin vitroenzymatic studies indicated that two different enzymes could be involved in the synthesis of the required fatty alcohol inMarinobacter aquaeoleiVT8. In this study, we demonstrate through a series of gene deletions and transcriptional analysis that either enzyme is capable of fulfilling the role of providing the fatty alcohol required for wax ester biosynthesisin vivo, but evolution has clearly selected one of these, a previously characterized fatty aldehyde reductase, as the preferred enzyme to perform this reaction under typical wax ester-accumulating conditions. These results complement previousin vitrostudies and provide the first glimpse into the role of each enzymein vivoin the native organism.

scholarly journals Genomic Potential of Marinobacter aquaeolei, a Biogeochemical “Opportunitroph”

2011 ◽  
Vol 77 (8) ◽  
pp. 2763-2771 ◽  
Author(s):  
Esther Singer ◽  
Eric A. Webb ◽  
William C. Nelson ◽  
John F. Heidelberg ◽  
Natalia Ivanova ◽  
...  
Keyword(s):  
Defense Mechanisms ◽  
Genome Structure ◽  
Heavy Metal Resistance ◽  
Metal Resistance ◽  
Polluted Water ◽  
Metabolic Potential ◽  
Genetic Characteristics ◽  
Content Type ◽  
Marinobacter Aquaeolei ◽  
The Many

ABSTRACTThe genus ofMarinobacteris one of the most ubiquitous in the global oceans and assumed to significantly impact various biogeochemical cycles. The genome structure and content ofMarinobacter aquaeoleiVT8 was analyzed and compared with those from other organisms with diverse adaptive strategies. Here, we report the many “opportunitrophic” genetic characteristics and strategies thatM. aquaeoleihas adopted to promote survival under various environmental conditions. Genome analysis revealed its metabolic potential to utilize oxygen and nitrate as terminal electron acceptors, iron as an electron donor, and urea, phosphonate, and various hydrocarbons as alternative N, P, and C sources, respectively. Miscellaneous sensory and defense mechanisms, apparently acquired via horizontal gene transfer, are involved in the perception of environmental fluctuations and antibiotic, phage, toxin, and heavy metal resistance, enabling survival under adverse conditions, such as oil-polluted water. Multiple putative integrases, transposases, and plasmids appear to have introduced additional metabolic potential, such as phosphonate degradation. The genomic potential ofM. aquaeoleiand its similarity to other opportunitrophs are consistent with its cosmopolitan occurrence in diverse environments and highly variable lifestyles.

scholarly journals Purification, Characterization, and Potential Bacterial Wax Production Role of an NADPH-Dependent Fatty Aldehyde Reductase from Marinobacter aquaeolei VT8

2009 ◽  
Vol 75 (9) ◽  
pp. 2758-2764 ◽  
Author(s):  
Bradley D. Wahlen ◽  
Whitney S. Oswald ◽  
Lance C. Seefeldt ◽  
Brett M. Barney
Keyword(s):  
Fatty Acids ◽  
Specific Activity ◽  
Aromatic Aldehydes ◽  
Wax Esters ◽  
Wax Ester ◽  
Fatty Aldehyde ◽  
Aldehyde Reductase ◽  
Specific Chemical ◽  
Marinobacter Aquaeolei ◽  
Long Chain

ABSTRACT Wax esters, ester-linked fatty acids and long-chain alcohols, are important energy storage compounds in select bacteria. The synthesis of wax esters from fatty acids is proposed to require the action of a four-enzyme pathway. An essential step in the pathway is the reduction of a fatty aldehyde to the corresponding fatty alcohol, although the enzyme responsible for catalyzing this reaction has yet to be identified in bacteria. We report here the purification and characterization of an enzyme from the wax ester-accumulating bacterium Marinobacter aquaeolei VT8, which is a proposed fatty aldehyde reductase in this pathway. The enzyme, a 57-kDa monomer, was expressed in Escherichia coli as a fusion protein with the maltose binding protein on the N terminus and was purified to near homogeneity by using amylose affinity chromatography. The purified enzyme was found to reduce a number of long-chain aldehydes to the corresponding alcohols coupled to the oxidation of NADPH. The highest specific activity was observed for the reduction of decanal (85 nmol decanal reduced/min/mg). Short-chain and aromatic aldehydes were not substrates. The enzyme showed no detectable catalysis of the reverse reaction, the oxidation of decanol by NADP+. The mechanism of the enzyme was probed with several site-specific chemical probes. The possible uses of this enzyme in the production of wax esters are discussed.

scholarly journals Marinobacter aquaeolei sp. nov., a halophilic bacterium isolated from a Vietnamese oil-producing well

1999 ◽  
Vol 49 (2) ◽  
pp. 367-375 ◽  
Author(s):  
Nguyen B. Huu ◽  
Ewald B. M. Denner ◽  
Dang T. C. Ha ◽  
Gerhard Wanner ◽  
Helga Stan-Lotter
Keyword(s):  
Halophilic Bacterium ◽  
Marinobacter Aquaeolei

scholarly journals Engineering of CYP153A33 With Enhanced Ratio of Hydroxylation to Overoxidation Activity in Whole-Cell Biotransformation of Medium-Chain 1-Alkanols

2022 ◽  
Vol 9 ◽  
Author(s):  
Hyuna Park ◽  
Doyeong Bak ◽  
Wooyoung Jeon ◽  
Minjung Jang ◽  
Jung-Oh Ahn ◽  
...  
Keyword(s):  
Site Directed Mutagenesis ◽  
Dodecanoic Acid ◽  
P450 Monooxygenase ◽  
Oxidation Activity ◽  
Whole Cell ◽  
Structure Activity ◽  
Marinobacter Aquaeolei ◽  
Whole Cell Biotransformation ◽  
Dodecanedioic Acid ◽  
Hydroxylation Activity

α,ω-Dodecanediol is a versatile material that has been widely used not only as an adhesive and crosslinking reagent, but also as a building block in the pharmaceutical and polymer industries. The biosynthesis of α,ω-dodecanediol from fatty derivatives, such as dodecane and dodecanol, requires an ω-specific hydroxylation step using monooxygenase enzymes. An issue with the whole-cell biotransformation of 1-dodecanol using cytochrome P450 monooxygenase (CYP) with ω-specific hydroxylation activity was the low conversion and production of the over-oxidized product of dodecanoic acid. In this study, CYP153A33 from Marinobacter aquaeolei was engineered to obtain higher ω-specific hydroxylation activity through site-directed mutagenesis. The target residue was mutated to increase flux toward α,ω-dodecanediol synthesis, while reducing the generation of the overoxidation product of dodecanoic acid and α,ω-dodecanedioic acid. Among the evaluated variants, CYP153A33 P136A showed a significant increase in 1-dodecanol conversion, i.e., 71.2% (7.12 mM from 10 mM 1-dodecanol), with an increased hydroxylation to over-oxidation activity ratio, i.e., 32.4. Finally, the applicability of this engineered enzyme for ω-specific hydroxylation against several 1-alkanols, i.e., from C6 to C16, was investigated and discussed based on the structure-activity relationship.

Exemplar Abstract for Marinobacter aquaeolei Nguyen et al. 1999.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Kara Mannor ◽  
George M Garrity
Keyword(s):  
Marinobacter Aquaeolei

Nomenclature Abstract for Marinobacter aquaeolei Nguyen et al. 1999.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Sarah Wigley ◽  
George M Garrity
Keyword(s):  
Marinobacter Aquaeolei
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