Reductase gene sequences and protein structures: p-cymene methyl hydroxylase.
Oxygenases are critical to cycling carbon in the biosphere and dependent on reductase action, principally from flavoprotein enzymes. Oxygenase diversity among organisms and strains carries a common theme of protein sequence and folding. p-Cymene (para-isopropyl toluene) was chosen as a point of convergence in terpene-aromatic mineralization to characterize a methyl hydroxylase electron transport system with the aerobe Pseudomonas aureofaciens. The cymA hydroxylase reductase gene was isolated and sequenced and the protein primary structure deduced. Optimized amino acid sequence alignments of flavoprotein reductases revealed major similarities over protein length, in the binding domains for NAD(P)H, and the flavine centers of pro- and eukaryote systems.
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NHEERL, Gulf Ecology Division, U.S. EPA, Gulf Breeze, Florida 32561-5299, USA.
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D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D001483:Base Sequence; D000081007:Cymenes; D015342:DNA Probes; D008969:Molecular Sequence Data; D039821:Monoterpenes; D010088:Oxidoreductases / Q000737:chemistry / Q000235:genetics*; D016133:Polymerase Chain Reaction; D011487:Protein Conformation; D011549:Pseudomonas / Q000201:enzymology*; D016415:Sequence Alignment; D012984:Software; D013729:Terpenes / Q000378:metabolism*
D001426:Bacterial Proteins; D000081007:Cymenes; D015342:DNA Probes; D039821:Monoterpenes; D013729:Terpenes; C007210:4-cymene; C105942:CymA protein, Pseudomonas aureofaciens; D010088:Oxidoreductases