Genetics of ferulic acid bioconversion to protocatechuic acid in plant-growth-promoting Pseudomonas putida WCS358
Article Abstract:
The degradation of ferulic acid in the Pseudomonas putida is under the control of several genes in the bacterial genome. The genes were identified in a Tn5 genomic mutant bank. Four genes were identified to be determinants in the bioconversion of ferulic acid to protocatechuic acid. These are fca, vdh, vanA and vanB. The first two genes codes for proteins responsible for the synthesis of vanillic acid from ferulic acid while the last two genes codes for proteins that demethylate vanillic acid to yield protocatechuic acid.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
User Contributions:
Comment about this article or add new information about this topic:
Purification and characterization of ferulate and p-coumarate decarboxylase from Bacillus pumilus
Article Abstract:
Standard techniques help purify an enzyme from Bacillus pumilus PS213, which is responsible for the nonoxidative decarboxylation of ferulic acid and p-coumaric acid producing 4-vinylguaiacol and 4-vinylphenol, respectively. Purified enzyme exhibits a single band of 23 kDa and size exclusion chromatography reveals the molecular mass of the enzyme as 45 kDa. Addition of cation exerts no influence on the enzyme activity, which is maximum at 37 degrees Celsius and pH 5.5.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
User Contributions:
Comment about this article or add new information about this topic:
Cloning, sequencing, and expression in Escherichia coli of the Bacillus pumilus gene for ferulic acid decarboxylase
Article Abstract:
A Bacillus pumilus 3,690-bp HindIII fragment containing the gene encoding ferulic acid decarboxylase (fdc) stimulates ferulic acid decarboxylation when expressed in Escherichia coli. The DNA fragment contains a Shine-Dalgarno sequence and a promoter sequence. The fdc has an apparent molecular mass of 42 kDa and is a homodimer. The B. pumilus fdc is structurally similar to the E. coli enzyme and 66.7% identical to yeast phenylacrylic decarboxylases.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
User Contributions:
Comment about this article or add new information about this topic:
- Abstracts: Assignment of hitherto unidentified 16S rDNA species to a main line of descent within the domain Bacteria. Phylogenetic analysis of the genera Rhodococcus and Nocardia and evidence for the evolutionary origin of the genus Nocardia from within the radiation of Rhodococcus species
- Abstracts: Chromosome extraction and revision of linkage group 2 in Tribolium castaneum. A hybrid incompatibility factor in Tribolium castaneum
- Abstracts: Heteropolysaccharide formation by Arthrobacter viscosus grown on xylose and xylose oligosaccharides. Production and characterization of laccase from Botrytis cinerea 61-34
- Abstracts: Engineering of a cold-adapted protease by sequential random mutagenesis and a screening system. Molecular characterization of a gene encoding extracellular serine protease isolated from a subtilisin inhibitor-deficient mutant of Streptomyces albogriseolus S-3253
- Abstracts: Characterization and environmental regulation of outer membrane proteins in Xenorhabdus nematophilus. Purification and characterization of Xenorhabdicin, a phage tail-like bacteriocin, from the lysogenic strain F1 of Xenorhabdus nematophilus