Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.3.99.3 (acyl-CoA dehydrogenase)
 1,425 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In honeybees, queens synthesize the "queen pheromone," whereas workers synthesize fatty acid components of "royal jelly" in their mandibular glands (MGs). To identify candidate proteins involved in the caste-selective MG function, we performed a proteomic analysis and identified three proteins that were expressed selectively in queen MGs (aldehyde dehydrogenase 1 [ALDH1], medium-chain acyl-CoA dehydrogenase [MCAD], and electron transfer flavoprotein alpha [ETFalpha)]), and a protein that was expressed selectively in worker MGs (fatty acid synthase [FAS)]). The quantitative reversed transcription-polymerase chain reaction demonstrated that the level of aldh1 transcription in MGs was significantly higher, whereas that of fas transcription was lower in queens than in workers. Among the eight genes encoding proteins similar to ALDH1 that are registered in the honeybee genome database, aldh6, aldh7, and aldh1 were expressed at significantly higher levels in queen MGs than in worker MGs. In situ hybridization showed that in the queen head, aldh1 was expressed in MG cells, whereas aldh6 and aldh7 were expressed in fat cells attached to the MGs. These results suggest caste- and cell type-selective aldehyde/fatty acid metabolism in honeybee MGs.
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PMID:Differential gene expression in the mandibular glands of queen and worker honeybees, Apis mellifera L.: implications for caste-selective aldehyde and fatty acid metabolism. 1966 65

Pseudomonas putida BIRD-1 has the potential to be used for the industrial production of butanol due to its solvent tolerance and ability to metabolize low-cost compounds. However, the strain has two major limitations: it assimilates butanol as sole carbon source and butanol concentrations above 1% (v/v) are toxic. With the aim of facilitating BIRD-1 strain design for industrial use, a genome-wide mini-Tn5 transposon mutant library was screened for clones exhibiting increased butanol sensitivity or deficiency in butanol assimilation. Twenty-one mutants were selected that were affected in one or both of the processes. These mutants exhibited insertions in various genes, including those involved in the TCA cycle, fatty acid metabolism, transcription, cofactor synthesis and membrane integrity. An omics-based analysis revealed key genes involved in the butanol response. Transcriptomic and proteomic studies were carried out to compare short and long-term tolerance and assimilation traits. Pseudomonas putida initiates various butanol assimilation pathways via alcohol and aldehyde dehydrogenases that channel the compound to central metabolism through the glyoxylate shunt pathway. Accordingly, isocitrate lyase - a key enzyme of the pathway - was the most abundant protein when butanol was used as the sole carbon source. Upregulation of two genes encoding proteins PPUBIRD1_2240 and PPUBIRD1_2241 (acyl-CoA dehydrogenase and acyl-CoA synthetase respectively) linked butanol assimilation with acyl-CoA metabolism. Butanol tolerance was found to be primarily linked to classic solvent defense mechanisms, such as efflux pumps, membrane modifications and control of redox state. Our results also highlight the intensive energy requirements for butanol production and tolerance; thus, enhancing TCA cycle operation may represent a promising strategy for enhanced butanol production.
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PMID:Understanding butanol tolerance and assimilation in Pseudomonas putida BIRD-1: an integrated omics approach. 2698 5