Structure and assembly of protocatechuate 3,4-dioxygenase

Research output: Contribution to journalArticle

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Abstract

Dioxygenases catalyse the cleavage of molecular oxygen with subsequent incorporation of both oxygen atoms into organic substrates. Some of the best-studied dioxygenases have been isolated from bacteria where they catalyse the critical ring-opening step in the biodegradation of aromatic compounds. These bacterial enzymes generally contain nonheme ferric iron as the sole cofactor. Protocatechuate 3,4-dioxygenase (3,4-PCD) was one of the first such enzymes recognized1 and catalyses the intradiol cleavage of protocatechuic acid by oxygen to produce β- car boxy- cis,cis-muconic acid. Previous studies have shown that the 3,4-PCD found in Pseudomonas aeruginosa is an oligomer with a relative molecular mass (Mr) of 587,000 (587K) containing 12 copies each of α (22.3K) and β (26.6K) subunits2-6. The X-ray structure determination of 3,4-PCD reveals the catalytic iron environment required for oxygenolytic cleavage of aromatic rings and also provides a novel holoenzyme assembly with cubic 23(T) symmetry and first examples of mixed β-barrel domains.

Original languageEnglish (US)
Pages (from-to)403-405
Number of pages3
JournalNature
Volume336
Issue number6197
DOIs
StatePublished - Jan 1 1988

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Protocatechuate-3,4-Dioxygenase
Dioxygenases
NSC 153174
Oxygen
Iron
Holoenzymes
Enzymes
Pseudomonas aeruginosa
X-Rays
Bacteria

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Structure and assembly of protocatechuate 3,4-dioxygenase. / Ohlendorf, D. H.; Lipscomb, J. D.; Weber, P. C.

In: Nature, Vol. 336, No. 6197, 01.01.1988, p. 403-405.

Research output: Contribution to journalArticle

Ohlendorf, D. H. ; Lipscomb, J. D. ; Weber, P. C. / Structure and assembly of protocatechuate 3,4-dioxygenase. In: Nature. 1988 ; Vol. 336, No. 6197. pp. 403-405.
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