ArticleJournal of bacteriology2005
Identification of an amino acid position that determines the substrate range of integral membrane alkane hydroxylases.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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42 citing papers in PubMed, 135 citations in OpenAlex.
- Engineering membrane-bound alkane monooxygenase from Marinobacter sp. for increased activity in the selective ω-hy-droxylation of linear and branched aliphatic esters.Protein science : a publication of the Protein Society · 2026Article
- Engineering of Transmembrane Alkane Monooxygenases to Improve a Key Reaction Step in the Synthesis of Polymer Precursor Tulipalin A.Angewandte Chemie (International ed. in English) · 2025Article
- Metabolic characterization of alkane monooxygenases and the growth phenotypes ofJournal of bacteriology · 2025Article
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- Generalization of Classification of AlkB Family Alkane Monooxygenases fromInternational journal of molecular sciences · 2025Article
- Biodegradation of a complex hydrocarbon mixture and biosurfactant production by Burkholderia thailandensis E264 and an adapted microbial consortium.Biodegradation · 2024Article
- Structure and Function of Alkane Monooxygenase (AlkB).Accounts of chemical research · 2023Review
- Structure and mechanism of the alkane-oxidizing enzyme AlkB.Nature communications · 2023Article
- Structural basis for enzymatic terminal C-H bond functionalization of alkanes.Nature structural & molecular biology · 2023Article
- Potential of Indigenous Strains Isolated from the Wastewater Treatment Plant of a Crude Oil Refinery.Microorganisms · 2023Article
- Rational design of enzyme activity and enantioselectivity.Frontiers in bioengineering and biotechnology · 2023Review
- An alkane monooxygenase (AlkB) family in which all electron transfer partners are covalently bound to the oxygen-activating hydroxylase.Journal of inorganic biochemistry · 2022Article
- An Overview of the Electron-Transfer Proteins That Activate Alkane Monooxygenase (AlkB).Frontiers in microbiology · 2022Review
- Biotechnological applications of marine bacteria in bioremediation of environments polluted with hydrocarbons and plastics.Applied microbiology and biotechnology · 2021Review
- Investigation of the prevalence and catalytic activity of rubredoxin-fused alkane monooxygenases (AlkBs).Journal of inorganic biochemistry · 2021Article
- Whole-genome sequence-based analysis of the Paenibacillus aquistagni strain DK1, a polyethylene-degrading bacterium isolated from landfill.World journal of microbiology & biotechnology · 2021Article
- Directed evolution methods for overcoming trade-offs between protein activity and stability.AIChE journal. American Institute of Chemical Engineers · 2020Article
- Characterization and Transcriptional Regulation ofMicroorganisms · 2019Article
- Biosynthesis of Medium-Chain ω-Hydroxy Fatty Acids by AlkBGT ofFrontiers in bioengineering and biotechnology · 2019Article
- CrgA Protein Represses AlkB2 Monooxygenase and Regulates the Degradation of Medium-to-Long-ChainFrontiers in microbiology · 2019Article
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7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Selection experiments and protein engineering were used to identify an amino acid position in integral membrane alkane hydroxylases (AHs) that determines whether long-chain-length alkanes can be hydroxylated by these enzymes. First, substrate range mutants of the Pseudomonas putida GPo1 and Alcanivorax borkumensis AP1 medium-chain-length AHs were obtained by selection experiments with a specially constructed host. In all mutants able to oxidize alkanes longer than C13, W55 (in the case of P. putida AlkB) or W58 (in the case of A. borkumensis AlkB1) had changed to a much less bulky amino acid, usually serine or cysteine. The corresponding position in AHs from other bacteria that oxidize alkanes longer than C13 is occupied by a less bulky hydrophobic residue (A, V, L, or I). Site-directed mutagenesis of this position in the Mycobacterium tuberculosis H37Rv AH, which oxidizes C10 to C16 alkanes, to introduce more bulky amino acids changed the substrate range in the opposite direction; L69F and L69W mutants oxidized only C10 and C11 alkanes. Subsequent selection for growth on longer alkanes restored the leucine codon. A structure model of AHs based on these results is discussed.
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