Early intermediates in the degradation of α-conidendrin by a Pseudomonas multivorans

Toms, Anne; Wood, John M.

doi:10.1021/bi00806a005

Cited by 12 publications

(1 citation statement)

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“…Such a mechanism requires the appropriate groups para to each other and all of the substrates for the enzyme have this orientation (Table 3). A similar scheme has been postulated for hydroxylation of a-conidendrin in its metabolism by Pseudomonas multivorans, although no enzymes have been demonstrated (Toms & Wood, 1970). p-Hydroxybenzyl alcohol was identified as a product, but a second dehydrogenation by the enzyme can convert this into p-hydroxybenzaldehyde, which was the major product under the conditions used.…”

Section: Discussionmentioning

confidence: 76%

P-cresol and 3,5-xylenol methylhydroxylases in Pseudomonas putida N.C.I.B. 9896

Keat¹,

Hopper²

1978

Biochemical Journal

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Pseudomonas putida N.C.I.B. 9869, when grown on 3,5-xylenol, hydroxylates the methyl groups on 3,5-xylenol and on p-cresol by two different enzymes. 3,5-Xylenol methylhydroxylase, studied only in relatively crude extracts, requires NADH, is not active with p-cresol and is inhibited by cyanide, but not by CO. The p-cresol methylhydroxylase requires an electron acceptor and will act under anaerobic conditions. It was purified and is a flavocytochrome c of mol.wt. approx. 114,000 consisting of two subunits of equal size. The enzyme catalyses the hydroxylation of p-cresol (Km 16 micron) and the further oxidation of product, p-hydroxybenzyl alcohol (Km 27 micron) to p-hydroxybenzaldehyde. A different p-cresol methylhydroxylase of the flavocytochrome c type is induced by growth on p-cresol. It too was purified and has mol.wt. approx. 100,000, and again consisted of two equal-size subunits. The Km for p=cresol 3.6 micron and for p=hydroxybenzyl alcohol, 15 micron.

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Section: Discussionmentioning

confidence: 76%