A new member of the aldo–keto reductase family from the plant pathogen Xylella fastidiosa

Rosselli, Luciana Kauer; Oliveira, C. L. P.; Azzoni, Adriano Rodrigues; Tada, Susely F.S.; Catani, Cleide Ferreira; Saraiva, Antonio Marcos; Soares, José Sérgio; Medrano, Francisco J.; Torriani, Íris L.; Souza, Anete Pereira de

doi:10.1016/j.abb.2006.07.005

Cited by 9 publications

(7 citation statements)

References 23 publications

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“…Together, there is a wealth of new knowledge of X. fastidiosa and its interactions with plants and insect vectors. The availability of genomic information on X. fastidiosa has led to numerous reports of proteins and other biochemical processes in this species (30,35,36,45,70,84,89,103,120), but these studies are not emphasized in this review. We also do not address the many studies of detection methods and strain variation (26,39,56,58,81).…”

Section: Introductionmentioning

confidence: 99%

Living in two Worlds: The Plant and Insect Lifestyles ofXylella fastidiosa

Chatterjee

Almeida

Lindow

2008

Annu. Rev. Phytopathol.

366

394

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Diseases caused by Xylella fastidiosa have attained great importance worldwide as the pathogen and its insect vectors have been disseminated. Since this is the first plant pathogenic bacterium for which a complete genome sequence was determined, much progress has been made in understanding the process by which it spreads within the xylem vessels of susceptible plants as well as the traits that contribute to its acquisition and transmission by sharpshooter vectors. Although this pathogen shares many similarities with Xanthomonas species, such as its use of a small fatty acid signal molecule to coordinate virulence gene expression, the traits that it utilizes to cause disease and the manner in which they are regulated differ substantially from those of related plant pathogens. Its complex lifestyle as both a plant and insect colonist involves traits that are in conflict with these stages, thus apparently necessitating the use of a gene regulatory scheme that allows cells expressing different traits to co-occur in the plant.

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Section: Introductionmentioning

confidence: 99%

Living in two Worlds: The Plant and Insect Lifestyles ofXylella fastidiosa

Chatterjee

Almeida

Lindow

2008

Annu. Rev. Phytopathol.

366

394

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“…Among the identified AKRs, BdsA shared 53% identity with XF1729 from Xylella fastidiosa 9a5c, which is a pathogen associated with crop disease. XF1729 catalyzes the reduction of (Ϯ)-glyceraldehyde and 2-nitrobenzaldehyde in the presence of NADPH (18). Sequence alignment of BdsA with AKRs revealed that the catalytic tetrad (Asp62, Tyr67, Lys92, and His142) was conserved in BdsA (Fig.…”

Section: Resultsmentioning

confidence: 99%

Bacterial Enzymes Catalyzing the Synthesis of 1,8-Dihydroxynaphthalene, a Key Precursor of Dihydroxynaphthalene Melanin, from Sorangium cellulosum

Sone

Nakamura

Sasaki

et al. 2018

Appl Environ Microbiol

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1,8-Dihydroxynaphthalene (1,8-DHN) is a key intermediate in the biosynthesis of DHN melanin, which is specific to fungi. In this study, we characterized the enzymatic properties of the gene products of an operon consisting of ,, and from the gram-negative bacterium, Heterologous expression of ,, and in caused secretion of a dark-brown pigment into the broth. High-performance liquid chromatography analysis of the broth revealed that the recombinant strain produced 1,8-DHN, indicating that the operon encoded a novel enzymatic system for the synthesis of 1,8-DHN. Simultaneous incubation of the recombinant SoceCHS1, BdsA, and BdsB with malonyl-CoA and NADPH resulted in the synthesis of 1,8-DHN. SoceCHS1, a type III polyketide synthase (PKS), catalyzed the synthesis of 1,3,6,8-tetrahydroxynaphthalene (THN) THN was in turn converted to 1,8-DHN by successive steps of reduction and dehydration, which were catalyzed by BdsA and BdsB. BdsA, which is a member of the aldo-keto reductase (AKR) superfamily, catalyzed the reduction of THN and 1,3,8-tetrahydroxynaphthalene (THN) to scytalone and vermelone, respectively. The stereoselectivity of THN reduction by BdsA occurred on the -face to give ()-scytalone with more than 99% optical purity. BdsB, a SnoaL2-like protein, catalyzed the dehydration of scytalone and vermelone to THN and 1,8-DHN, respectively. The fungal pathway for the synthesis of 1,8-DHN is comprised of a type I PKS, naphthol reductases of the short-chain dehydrogenase/reductase (SDR) superfamily, and scytalone dehydratase (SD). These findings demonstrated 1,8-DHN synthesis by novel enzymes of bacterial origin. Although the DHN biosynthetic pathway was thought to be specific to fungi, we discovered novel DHN synthesis enzymes of bacterial origin. The biosynthesis of bacterial DHN utilized a type III PKS for polyketide synthesis, an AKR superfamily for reduction, and a SnoaL2-like NTF2 superfamily for dehydration, whereas the biosynthesis of fungal DHN utilized a type I PKS, SDR superfamily enzyme, and SD-like NTF2 superfamily. Surprisingly, the enzyme systems comprising the pathway were significantly different from each other, suggesting independent, parallel evolution leading to the same biosynthesis. DHN melanin plays roles in host invasion and adaptation to stress in pathogenic fungi and is therefore important to study. However, it is unclear whether DHN biosynthesis occurs in bacteria. Importantly, we did find that bacterial DHN biosynthetic enzymes were conserved among pathogenic bacteria.

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“…AKR13A1 demonstrated activity towards pyridine 2‐aldehyde [15], but the catalytic efficiency ( k cat /K m ) of HpAKR for pyridine 2‐aldehyde was six‐fold higher than that of AKR13A1. The characterization of the second family member, AKR13B1, again was quite limited, as Michaelis constants were estimated for just two aldehyde substrates, glyceraldehyde and 2‐nitrobenzaldehyde [16]. However, it is noted that AKR13B1 demonstrates activity towards glyceraldehyde, unlike the other two family members.…”

Section: Discussionmentioning

confidence: 99%

“…The sequence was submitted to the AKR superfamily database (http://www.med.upenn.edu/akr) for nomenclature assignment and was classified as AKR13C1. There are only two other members in this family, the AKR13A1 YacK protein from Schizosaccaromyces pombe [15] and the AKR13B1 phenylacetaldehyde dehydrogenase enzyme from Xylella fastidiosa [16].…”

Section: Sequence Analysis Of Hpakrmentioning

confidence: 99%

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Aldo‐keto reductase from Helicobacter pylori– role in adaptation to growth at acid pH

Cornally¹,

Mee²,

MacDonaill³

et al. 2008

The FEBS Journal

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Pyridine‐linked oxidoreductase enzymes of Helicobacter pylori have been implicated in the pathogenesis of gastric disease. Previous studies in this laboratory examined a cinnamyl alcohol dehydrogenase that was capable of detoxifying a range of aromatic aldehydes. In the present work, we have extended these studies to identify and characterize an aldoketo reductase (AKR) enzyme present in H. pylori. The gene encoding this AKR was identified in the sequenced strain of H. pylori, 26695. The gene, referred to as HpAKR, was cloned and expressed in Escherichia coli as a His‐tag fusion protein, and purified using nickel chelate chromatography. The gene product (HpAKR) has been assigned to the AKR13C1 family, although it differs in specificity from the two other known members of this family. The enzyme is a monomer with a molecular mass of approximately 39 kDa on SDS/PAGE. It reduces a range of aromatic aldehyde substrates with high catalytic efficiency, and exhibits dual cofactor specificity for both NADPH and NADH. HpAKR can function over a broad pH range (pH 4–9), and has a pH optimum of 5.5. It is inhibited by sodium valproate. Its substrate specificity complements that of the cinnamyl alcohol dehydrogenase activity in H. pylori, giving the organism the capacity to reduce a wide range of aldehydes. Generation of an HpAKR isogenic mutant of H. pylori demonstrated that HpAKR is required for growth under acidic conditions, suggesting an important role for this enzyme in adaptation to growth in the gastric mucosa. This AKR is a member of a hitherto little‐studied class.

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A new member of the aldo–keto reductase family from the plant pathogen Xylella fastidiosa

Cited by 9 publications

References 23 publications

Living in two Worlds: The Plant and Insect Lifestyles ofXylella fastidiosa

Living in two Worlds: The Plant and Insect Lifestyles ofXylella fastidiosa

Bacterial Enzymes Catalyzing the Synthesis of 1,8-Dihydroxynaphthalene, a Key Precursor of Dihydroxynaphthalene Melanin, from Sorangium cellulosum

Aldo‐keto reductase from Helicobacter pylori– role in adaptation to growth at acid pH

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