Crystalline quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus

Geiger, Otto; Goerisch, Helmut

doi:10.1021/bi00368a031

Cited by 49 publications

(26 citation statements)

References 25 publications

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“…In contrast, an atypical soluble glucose dehydrogenase found only in Acinetobacter calcoaceticus (63,64) can oxidize both mono-and disaccharides. Interestingly, this periplasmic enzyme is rather different from the membrane-bound glucose dehydrogenases, not only with regard to its sugar substrate specificity but also in its preference for electron acceptors.…”

Section: Discussionmentioning

confidence: 92%

An Outer Membrane Enzyme That Generates the 2-Amino-2- deoxy-gluconate Moiety of Rhizobium leguminosarum Lipid A

Que-Gewirth

Lin

Cotter

et al. 2003

Journal of Biological Chemistry

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The structures of Rhizobium leguminosarum and Rhizobium etli lipid A are distinct from those found in other Gram-negative bacteria. Whereas the more typical Escherichia coli lipid A is a hexa-acylated disaccharide of glucosamine that is phosphorylated at positions 1 and 4, R. etli and R. leguminosarum lipid A consists of a mixture of structurally related species (designated A-E) that lack phosphate. A conserved distal unit, comprised of a diacylated glucosamine moiety with galacturonic acid residue at position 4 and a secondary 27-hydroxyoctacosanoyl (27-OH-C28) as part of a 2 acyloxyacyl moiety, is present in all five components. The proximal end is heterogeneous, differing in the number and lengths of acyl chains and in the identity of the sugar itself. A proximal glucosamine unit is present in B and C, but an unusual 2-amino-2-deoxy-gluconate moiety is found in D-1 and E. We now demonstrate that membranes of R. leguminosarum and R. etli can convert B to D-1 in a reaction that requires added detergent and is inhibited by EDTA. Membranes of Sinorhizobium meliloti and E. coli lack this activity. Mass spectrometry demonstrates that B is oxidized in vitro to a substance that is 16 atomic mass units larger, consistent with the formation of D-1. The oxidation of the lipid A proximal unit is also demonstrated by matrix-assisted laser desorption ionization time-of-flight mass spectrometry in the positive and negative modes using the model substrate, 1-dephospho-lipid IV A . With this material, an additional intermediate (or by product) is detected that is tentatively identified as a lactone derivative of 1-dephospho-lipid IV A . The enzyme, presumed to be an oxidase, is located exclusively in the outer membrane of R. leguminosarum as judged by sucrose gradient analysis. To our knowledge, an oxidase associated with the outer membranes of Gram-negative bacteria has not been reported previously.

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Section: Discussionmentioning

confidence: 92%

An Outer Membrane Enzyme That Generates the 2-Amino-2- deoxy-gluconate Moiety of Rhizobium leguminosarum Lipid A

Que-Gewirth

Lin

Cotter

et al. 2003

Journal of Biological Chemistry

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“…This clone is able to complement GDH-mutants in .4. calcoaceticus, E. coli and Pseudomonas aeruginosa. Dokter et al (1986) and Geiger and Grrisch (1986) reported the isolation of a PQQ dependent GDH protein from A. calcoaceticus consisting of two identical subunits. The amino acid sequence of the Mr 86956 GDH from A. calcoaceticus shows a 140 residue N-terminal region with high hydrophobicity.…”

Section: Introductionmentioning

confidence: 99%

Cloning, characterization and DNA sequencing of the gene encoding the Mr50000 quinoprotein glucose dehydrogenase fromAcinetobacter calcoaceticus

et al. 1989

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Recently we described the cloning of the gene coding for a Mr 87,000 glucose dehydrogenase (GDH-A) from Acinetobacter calcoaceticus. In this report we describe the cloning of a gene coding for a second GDH (GDH-B) with a Mr of 50,000 from the same organism. This gene was isolated using a 20-mer synthetic oligonucleotide, derived from the N-terminal amino acid sequence of purified GDH-B as a probe to screen a genomic bank. From the DNA sequence of the gdhB gene, a protein can be derived of Mr 52,772 with a 24 amino acid signal peptide which is removed, resulting in the mature protein with a Mr 50,231. In vitro transcription-translation of the gdhB clone shows the mature and the precursor protein. The derived amino acid sequence has no obvious homology with GDH-A of A. calcoaceticus. We show that disaccharides are specific GDH-B substrates and that 2-deoxyglucose is specific for GDH-A.

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“…s-GDH has been purified (Dokter et aI., 1986;Geiger and Gorisch, 1986) and most of its properties are shown in Table 1. It is a dimeric, strongly basic protein with a broad substrate specificity.…”

Section: General Propertiesmentioning

confidence: 99%

The Biology of Acinetobacter

Towner¹,

Bergogne-Bérézin²,

Fewson³

1991

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All rights reservedNo part of this book may be reproduced, stored in a retrieval system, or transmitted in any form or by any means, electronic, mechanical, photocopying, microfilming, recording, or otherwise, without written permission from the Publisher PREFACEThe 1st International Workshop on Acinetobacter was held on 6th September, 1986, in Manchester, England, in association with the 14th International Congress of Microbiology. That occasion was so well attended and productive that there were soon discussions about how, when and where the next meeting should be held. This time, however, there was sufficient confidence to think of a more substantial meeting and to plan for the proceedings to be published. It emerged that there was wide agreement that the time was ripe to take stock of the entire biology of Acinetobacter: its occurrence and taxonomy; its molecular biology, biochemistry and physiology; its clinical importance and its industrial and commercial applications. The 2nd International Workshop on Acinetobacter took place from 6th to 7th September, 1990, at the Institut Pasteur, Paris, and was sponsored by the Federation of European Microbiological Societies. There were about 100 participants from 19 countries. The backbone of the meeting consisted of 23 plenary lectures. There were 28 posters and the meeting closed with a general discussion which went on long after the official finishing time despite all the counter-attractions of a sunny Parisian Friday afternoon. Indeed discussions continued while cruising along the Seine and while dining at the top of the Tour Montparnasse. However, the vitality and usefulness of even the most successful meeting is difficult to transmit by the printed word. The editors decided, therefore, not simply to publish the proceedings of the Workshop, but rather to commission a set of review articles with the aim of giving an up-to-date and rounded picture of our current knowledge of the genus Acinetobacter. These reviews, together with a

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Crystalline quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus

Cited by 49 publications

References 25 publications

An Outer Membrane Enzyme That Generates the 2-Amino-2- deoxy-gluconate Moiety of Rhizobium leguminosarum Lipid A

An Outer Membrane Enzyme That Generates the 2-Amino-2- deoxy-gluconate Moiety of Rhizobium leguminosarum Lipid A

Cloning, characterization and DNA sequencing of the gene encoding the Mr50000 quinoprotein glucose dehydrogenase fromAcinetobacter calcoaceticus

The Biology of Acinetobacter

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