Amino acid sequence of the Pseudomonas putida cytochrome P-450. I. Sequences of tryptic and clostripain peptides

In order to elucidate the complete amino acid sequence of Pseudomonas putida cytochrome P-450, tryptic digestion was performed on the S-carboxymethylated enzyme. Although cleavage did not occur at every lysyl and arginyl bond, 31 tryptic peptides ranging in size from 1 to 55 residues were isolated....

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Bibliographic Details
Published in:The Journal of biological chemistry 1982-11, Vol.257 (21), p.12657-12663
Main Authors: Haniu, M, Tanaka, M, Yasunobu, K T, Gunsalus, I C
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Carboxypeptidases
Cysteine Endopeptidases
Cytochrome P-450 Enzyme System
Endopeptidases
Peptide Fragments - analysis
Pseudomonas - metabolism
Trypsin
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Summary:In order to elucidate the complete amino acid sequence of Pseudomonas putida cytochrome P-450, tryptic digestion was performed on the S-carboxymethylated enzyme. Although cleavage did not occur at every lysyl and arginyl bond, 31 tryptic peptides ranging in size from 1 to 55 residues were isolated. These were sequenced by manual Edman degradation and carboxypeptidase digestion. Overlaps of some od these tryptic peptides were obtained by data obtained from partial Edman degradation and amino acid composition of the clostripain cleavage products. These results, together with data from the cyanogen bromide and acid cleavage peptides reported in the accompanying paper, established the complete amino acid sequence of P. putida cytochrome P-450.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)33561-0