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J. Biol. Chem., Vol. 261, Issue 3, 1158-1163, Jan, 1986
BP Unger, IC Gunsalus and SG Sligar
Cytochrome P-450cam catalyzes the stereospecific methylene hydroxylation of
camphor to form 5-exohydroxycamphor and is encoded by the camC gene on the
CAM plasmid of Pseudomonas putida, ATCC 17453. The cytochrome P-450cam
structural gene has been cloned by mutant complementation in P. putida
(Koga, H., Rauchfuss, B., and Gunsalus, I. C. (1985) Biochem. Biophys. Res.
Commun. 130, 412-417). We report the complete nucleotide sequence of the
camC gene along with 155 base pairs of 5' and 175 base pairs of 3' flanking
sequence. Upon comparison of the amino acid sequence derived from the gene
sequence to the one obtained from the purified protein (Haniu, M., Armes,
L. G., Yasunobu, K. T., Shastry, B. A., and Gunsalus, I. C. (1982) J. Biol.
Chem. 257, 12664-12671), five differences were found. The most significant
was the addition of a Trp and a Thr residue between Val-54 and Arg-55,
thereby increasing the amino acid numbering scheme by 2 after Val-54,
bringing the total number of amino acids to 414. Other differences were:
Gln-274- ---Glu-276, Ser-359----His-361, and Asn-405----Asp-407. N-terminal
amino acid sequence analysis of the cloned cytochrome P-450cam enzyme
expressed in Escherichia coli under the lac promoter showed a faithful
translation of the hemo-protein, with the N-terminal Met removed by
processing as found in P. putida. Purification to homogeneity of the cloned
protein was accomplished by the method used for the CAM plasmid- encoded
enzyme of P. putida. The G + C content of the camC gene was found to be
59.0%, caused by a preferred usage of G and C terminated codons. The gene
encoding putidaredoxin reductase, camA, was located 22 nucleotides
downstream from the cytochrome P-450cam gene. The camA gene initiated with
a novel GUG codon, the first such initiator documented in Pseudomonas.
Nucleotide sequence of the Pseudomonas putida cytochrome P-450cam gene and its expression in Escherichia coli
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