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. 1981 Apr;146(1):233–238. doi: 10.1128/jb.146.1.233-238.1981

Evolutionary relationships among gamma-carboxymuconolactone decarboxylases.

W K Yeh, D R Durham, P Fletcher, L N Ornston
PMCID: PMC217074  PMID: 6783616

Abstract

gamma-Carboxymuconolactone decarboxylase (EC 4.1.1.44) from Azotobacter vinelandii resembled the isofunctional enzymes from Acinetobacter calcoaceticus and Pseudomonas putida. All three decarboxylases appeared to be hexamers formed by association of identical subunits of about 13,300 daltons. The A. vinelandii and P. putida decarboxylases cross-reacted immunologically with each other, and the NH2-terminal amino acid sequences of the enzymes differed in no more than 7 of the first 36 residues. In contrast, the A. calcoaceticus decarboxylase did not cross-react with the decarboxylase from A. vinelandii or P. putida; the NH2-terminal amino acid sequences of these enzymes diverged about 50% from the NH2-terminal amino acid sequence of the A. calcoaceticus decarboxylase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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