The oxidation of <scp>d</scp>-quinate and related acids by <i>Acetomonas oxydans</i>

“…doi:10.1016/j.femsle.2004. 10.014 has been reported, by the action of an NAD-dependent quinate dehydrogenase (NAD-QDH), in fungi [2], Aerobacter aerogenes [3], and Pseudomonas aeruginosa [4], and also by an NAD(P)-independent QDH (EC 1.1.99.25) in Acinetobacter calcoaceticus [5], and acetic acid bacteria [6]. van Kleef and Duine [7] indicated the involvement of PQQ as a cofactor in NAD(P)-independent QDH of A. calcoaceticus LMD 79.41, although the purification of the enzyme was unsuccessful.…”

Section: Introductionmentioning

confidence: 99%

Quinate oxidation inGluconobacter oxydansIFO3244: purification and characterization of quinoprotein quinate dehydrogenase

Vangnai

Toyama

De-Eknamkul

et al. 2004

FEMS Microbiology Letters

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Quinoprotein quinate dehydrogenase (QDH) is a membrane-bound enzyme containing pyrroloquinoline quinone (PQQ) as the prosthetic group. QDH in Gluconobacter oxydans IFO3244 was found to be inducible by quinate and it is not constitutively expressed in the absence of quinate. The purification of holo-form of QDH to nearly homogeneity was achieved. The purified QDH appears to have two subunits of approximately 65 and 21 kDa, which could be the result of proteolysis of single polypeptide. Kinetic analysis indicated that the purified enzyme is much more specific to quinate than QDH from Acinetobacter calcoaceticus. The efficiency of the artificial electron acceptor was also determined.

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“…A particulate quinate dehydrogenase which does not require pyridine nucleotides has been also found in Acetomonas oxydans, but in contrast with the enzyme of A . calco-aceticus, its synthesis is apparently constitutive [14]. This article deals with the regulation of quinate oxidation in A .…”

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confidence: 99%

Regulation of the Enzymes of the β‐Ketoadipate Pathway in Moraxella

Tresguerres¹,

Torrontegui²,

Ccánovas³

et al. 1970

European Journal of Biochemistry

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1. The ability to oxidize quinate is elicited in Acinetobacter calco-aceticus not only by growth on quinate but also by growth on protocatechuate or its precursors such as shikimate and p-hydroxybenzoate. Accordingly the synthesis of a quinate dependent dehydrogenase was found to be induced by protocatechuate. Moreover, this enzyme seems to belong to the same coordinate block of enzymes responsible for the conversion of shikimate to /3-ketoadipyl-CoA.2. Analogies between quinate and shikimate oxidation in A . calco-aceticus have been substantiated by showing that both quinate dehydrogenase and shikimate dehydrogenase activities rely on a single enzyme.3. Several auxotrophs that have lost the ability to utilize both quinate and shikimate as sole source of carbon and energy have been isolated. Particularly relevant for this study are two of these mutants in which the dehydrogenase is severely impaired and correspondingly their ability t o oxidize the mentioned hydroaromatic compounds is substantially reduced. The properties of these auxotrophs and their revertants confirm the key role of the dehydrogenase in the dissimilation of both quinate and shikimate. The rationale of the control of this enzyme by protocatechuate is discussed.

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The oxidation of d-quinate and related acids by Acetomonas oxydans

Cited by 24 publications

References 20 publications

Purification and Characterization of Membrane-bound Quinoprotein Quinate Dehydrogenase

Purification and Characterization of Membrane-bound Quinoprotein Quinate Dehydrogenase

Quinate oxidation inGluconobacter oxydansIFO3244: purification and characterization of quinoprotein quinate dehydrogenase

Regulation of the Enzymes of the β‐Ketoadipate Pathway in Moraxella

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