Aromatic-Alcohol Dehydrogenases from <i>Pseudomonas putida</i> N.C.I.B. 9869

Keat, Malcolm J.; Hopper, David J.

doi:10.1042/bst0040494

Cited by 4 publications

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“…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. This second reaction is not necessarily of physiological importance, since cells also contain NAD+-linked alcohol dehydrogenases (Keat & Hopper, 1976).…”

Section: Discussionmentioning

confidence: 99%

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: 99%

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

Keat¹,

Hopper²

1978

Biochemical Journal

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Degradation of diarylethane structures by Pseudomonas fluorescens biovar I

et al. 1988

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Pseudomonas fluorescens biovar I was isolated from a pulp mill effluent based on its ability to grow on synthetic media containing 1,2-diarylethane structures as the sole carbon and energy source. Analysis of samples taken from cultures of this strain in benzoin or 4,4'-dimethoxybenzoin (anisoin), showed that cleavage between the two aliphatic carbons takes place prior to ring fission. Intermonomeric cleavage was also obtained with crude extracts. Substrates of this reaction were only those 1,2-diarylethane compounds that supported growth of the bacterium. The purification and partial characterization of an enzyme that catalyzes the NADH-dependent reduction of the carbonyl group of benzoin and anisoin is also reported.

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Purification and characterization of benzyl alcohol- and benzaldehyde- dehydrogenase from Pseudomonas putida CSV86

2011

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Pseudomonas putida CSV86 utilizes benzyl alcohol via catechol and methylnaphthalenes through detoxification pathway via hydroxymethylnaphthalenes and naphthaldehydes. Based on metabolic studies, benzyl alcohol dehydrogenase (BADH) and benzaldehyde dehydrogenase (BZDH) were hypothesized to be involved in the detoxification pathway. BADH and BZDH were purified to apparent homogeneity and were (1) homodimers with subunit molecular mass of 38 and 57 kDa, respectively, (2) NAD(+) dependent, (3) broad substrate specific accepting mono- and di-aromatic alcohols and aldehydes but not aliphatic compounds, and (4) BADH contained iron and magnesium, while BZDH contained magnesium. BADH in the forward reaction converted alcohol to aldehyde and required NAD(+), while in the reverse reaction it reduced aldehyde to alcohol in NADH-dependent manner. BZDH showed low K (m) value for benzaldehyde as compared to BADH reverse reaction. Chemical cross-linking studies revealed that BADH and BZDH do not form multi-enzyme complex. Thus, the conversion of aromatic alcohol to acid is due to low K (m) and high catalytic efficiency of BZDH. Phylogenetic analysis revealed that BADH is a novel enzyme and diverged during the evolution to gain the ability to utilize mono- and di-aromatic compounds. The wide substrate specificity of these enzymes enables strain to detoxify methylnaphthalenes to naphthoic acids efficiently.

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Aromatic-Alcohol Dehydrogenases from Pseudomonas putida N.C.I.B. 9869

Cited by 4 publications

References 0 publications

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

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

Degradation of diarylethane structures by Pseudomonas fluorescens biovar I

Purification and characterization of benzyl alcohol- and benzaldehyde- dehydrogenase from Pseudomonas putida CSV86

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