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The complete amino acid sequence of the beta-subunit of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa.
The complete amono aicd sequence of the beta-subunit of protocatechuate 3,4-dioxygenase is presented. The beta-subunit contained 237 amino acid residues, 4 of which were methionines. Accordingly, cyanogen bromide cleavage of the S-carboxymethylated beta-subunit produced five peptides. The sequences of these peptides were determined by analyses of the peptides obtained by tryptic, staphyloccal protease and thermolysin digestions. The alignment of the cyanogen bromide peptides was deduced by the use of overlapping peptides containing methionine which were obtained by tryptic digestion of the S-carboxymethylated beta-subunit. The calculated molecular weight was 26,588, which is close to the value estimated by acrylamide gel electrophoresis in the presence of sodium dodecyl sulfate.
PMID: 115853 [PubMed - indexed for MEDLINE]
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Cited by 6 PubMed Central articles
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Purification and Characterization of Hydroxyquinol 1,2-Dioxygenase from Azotobacter sp. Strain GP1.
Latus M, Seitz H, Eberspacher J, Lingens F.
Appl Environ Microbiol. 1995 Jul; 61(7):2453-2460.
[Appl Environ Microbiol. 1995]
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Cloning, sequencing, and expression of the Pseudomonas putida protocatechuate 3,4-dioxygenase genes.
Frazee RW, Livingston DM, LaPorte DC, Lipscomb JD.
J Bacteriol. 1993 Oct; 175(19):6194-202.
[J Bacteriol. 1993]
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Spontaneous mutations in pcaH and -G, structural genes for protocatechuate 3,4-dioxygenase in Acinetobacter calcoaceticus.
Gerischer U, Ornston LN.
J Bacteriol. 1995 Mar; 177(5):1336-47.
[J Bacteriol. 1995]
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