ArticleJournal of bacteriology2000
Substrate range and genetic analysis of Acinetobacter vanillate demethylase.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 41 citations in OpenAlex.
- Ancestral Protein Reconstruction Uncovers a Thermotolerant Rieske Oxygenase with EnhancedACS synthetic biology · 2026Article
- Conversion and upgrading of syringate by Acinetobacter baylyi ADP1.Microbial cell factories · 2025Article
- Genomic insight intoHeliyon · 2024Article
- Identification of a Phylogenetically Divergent Vanillate O-Demethylase fromMicroorganisms · 2022Article
- Genomic analysis of Acinetobacter pittii CEP14 reveals its extensive biodegradation capabilities, including cometabolic degradation of cis-1,2-dichloroethene.Antonie van Leeuwenhoek · 2022Article
- Characterization of Highly Ferulate-Tolerant Acinetobacter baylyi ADP1 Isolates by a Rapid Reverse Engineering Method.Applied and environmental microbiology · 2022Article
- Enabling microbial syringol conversion through structure-guided protein engineering.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- A Protochlorophyllide (Pchlide)Frontiers in plant science · 2019Article
- A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion.Nature communications · 2018Article
- Aerobic vanillate degradation and C1 compound metabolism in Bradyrhizobium japonicum.Applied and environmental microbiology · 2009Article
- When coupled to natural transformation in Acinetobacter sp. strain ADP1, PCR mutagenesis is made less random by mismatch repair.Applied and environmental microbiology · 2005Article
- A small family of LLS1-related non-heme oxygenases in plants with an origin amongst oxygenic photosynthesizers.Plant molecular biology · 2004Article
- Genes for chlorogenate and hydroxycinnamate catabolism (hca) are linked to functionally related genes in the dca-pca-qui-pob-hca chromosomal cluster of Acinetobacter sp. strain ADP1.Applied and environmental microbiology · 2003Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An Acinetobacter sp. genetic screen was used to probe structure-function relationships in vanillate demethylase, a two-component monooxygenase. Mutants with null, leaky, and heat-sensitive phenotypes were isolated. Missense mutations tended to be clustered in specific regions, most of which make known contributions to catalytic activity. The vanillate analogs m-anisate, m-toluate, and 4-hydroxy-3,5-dimethylbenzoate are substrates of the enzyme and weakly inhibit the metabolism of vanillate by wild-type Acinetobacter bacteria. PCR mutagenesis of vanAB, followed by selection for strains unable to metabolize vanillate, yielded mutant organisms in which vanillate metabolism is more strongly inhibited by the vanillate analogs. Thus, the procedure opens for investigation amino acid residues that may contribute to the binding of either vanillate or its chemical analogs to wild-type and mutant vanillate demethylases. Selection of phenotypic revertants following PCR mutagenesis gave an indication of the extent to which amino acid substitutions can be tolerated at specified positions. In some cases, only true reversion to the original amino acid was observed. In other examples, a range of amino acid substitutions was tolerated. In one instance, phenotypic reversion failed to produce a protein with the original wild-type sequence. In this example, constraints favoring certain nucleotide substitutions appear to be imposed at the DNA level.
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