Purification and characterization of salicylate hydroxylase from Pseudomonas putida PpG7.
The salicylate hydroxylase from P. putida PpG7 was purified and characterized. The enzyme appears to be monomeric, and it showed one major band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis with an apparent Mr of 45 kDa. The sequence of the first 25 amino acids of salicylate hydroxylase (PpG7) was determined. Also, the total amino acid composition of salicylate hydroxylase (PpG7) was obtained and compared with that of the known salicylate hydroxylase from P. putida.
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Department of Biochemistry, University of Illinois, Urbana 61801.
Murray
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Jollie
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Gunsalus
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D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D006899:Mixed Function Oxygenases / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011549:Pseudomonas / Q000201:enzymology*; D012459:Salicylates / Q000378:metabolism
D000596:Amino Acids; D012459:Salicylates; D006899:Mixed Function Oxygenases; C022619:salicylate 1-monooxygenase