Evolution of carbonic anhydrases in fungi

Elleuche, Skander; Pöggeler, Stefanie

doi:10.1007/s00294-009-0238-x

Cited by 57 publications

(77 citation statements)

References 42 publications

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“…Here, we report the first activation study of CaNce103 and Can2 with a series of amines and amino acids (of types 1-18), investigated earlier [10][11][12][13][14] for their interaction with mammalian a-CAs as well as very recently 15 with the b-and c-class enzymes from the Archaea domain and the common yeast. Such a study may help a better understanding of the b-CA catalytic/activation mechanism (the natural proton shuttling residue in this class of enzymes has not been yet identified), as well as the design of CAAs targeting b-CAs from these or other pathogenic fungi.…”

Section: Introductionmentioning

confidence: 98%

“…8 These are the only data available in the literature regarding the activation of b-and c-CAs, even though these enzymes are widespread in the phylogenetic tree. 9,10 The recent characterization of CAs in fungi [11][12][13][14] led us to initiate a systematic search of modulators of these enzymes activity, that is, inhibitors and activators, which might show therapeutic potential. 15,16 Cryptococcus neoformans contains two b-CAs, Can1 and Can2, which share homology to the S. cerevisiae gene NCE103.…”

Section: Introductionmentioning

confidence: 99%

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Carbonic anhydrase activators: Activation of the β-carbonic anhydrases from the pathogenic fungi Candida albicans and Cryptococcus neoformans with amines and amino acids

Innocenti¹,

Hall²,

Scozzafava³

et al. 2010

Bioorganic & Medicinal Chemistry

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Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Carbonic anhydrase activators: Activation of the β-carbonic anhydrases from the pathogenic fungi Candida albicans and Cryptococcus neoformans with amines and amino acids

Innocenti¹,

Hall²,

Scozzafava³

et al. 2010

Bioorganic & Medicinal Chemistry

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“…CAs occur in all three domains of life (Eubacteria, Archaea and Eukaryota), and play roles in diverse metabolic pathways. The CA superfamily is subdivided into five families: α-CA, β-CA, γ-CA, δ-CA and ζ-CA [23,24]. Interestingly, large-scale phylogenetic analyses reveal no homology between these five families [25], and they are therefore thought to be the result of convergent evolution, i.e.…”

Section: The Carbonic Anhydrase Super-familymentioning

confidence: 99%

The evolution of metazoan α-carbonic anhydrases and their roles in calcium carbonate biomineralization

et al. 2014

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The carbonic anhydrase (CA; EC 4.2.1.1) superfamily is a class of ubiquitous metallo-enzymes that catalyse the reversible hydration of carbon dioxide. The α-CA family, present in all metazoan clades, is a key enzyme involved in a wide range of physiological functions including pH regulation, respiration, photosynthesis, and biocalcification. This paper reviews the evolution of the α-CA family, with an emphasis on metazoan α-CA members involved in biocalcification. Phylogenetic analyses reveal a complex evolutionary history of α-CAs, and suggest α-CA was independently co-opted into a variety of skeleton forming roles (e.g. as a provider of HCO 3 − ions, a structural protein, a nucleation activator, etc.) in multiple metazoan lineages. This evolutionary history is most likely the result of multiple gene duplications coupled with the insertion of repetitive or non-repetitive low-complexity domains (RLCDs/LCDs). These domains, of largely unknown function, appear to be lineage-specific, and provide further support for the hypothesis of independent recruitment of α-CAs to diverse metazoan biocalcification processes. An analysis of α-CA sequences associated with biocalcification processes indicates that the domains involved in the activity and conformation of the active site are extremely conserved among metazoans.

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“…γ-CAs have been reported in plants, archaea, and some bacteria. 38,39 The last two CA classes: δ-and ζ-CAs are structurally similar to the β-CAs.…”

Section: Discussionmentioning

confidence: 99%

Serum Carbonic Anhydrase 1 is a Biomarker for Diagnosis of Human Schistosoma mansoni Infection

Kardoush

Ward

Ndao

2017

The American Journal of Tropical Medicine and Hygiene

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Abstract. Schistosoma mansoni is a major public health threat in many parts of the world. The current diagnostic tests for schistosomiasis are suboptimal, particularly early in infection, when the parasite burden is low and with reinfection after treatment. We sought to identify novel biomarkers of active infection by studying serum proteins in a mouse model of schistosomiasis followed by confirmation in chronically infected patients. Acute (6 weeks) and chronic (12 weeks) sera from S. mansoni-infected C57Bl/6 mice as well as sera from chronically infected patients were assessed using two proteomic platforms: surface-enhanced, laser desorption and ionization, time-of-flight mass spectrometry and Velos Orbitrap mass spectrometry. Several candidate biomarkers were further evaluated by Western blot and/or enzyme-linked immunosorbent assay (ELISA). Among the most promising was carbonic anhydrase 1 (CA1), a host protein found primarily in red blood cells and enterocytes that proved to be a negative biomarker for schistosomiasis in both mouse and human samples. Reduced serum CA-1 levels were confirmed by both Western blot (murine and human: both P < 0.001) and ELISA (human: P < 0.01). Western blots of serial mouse sera revealed a progressive reduction in serum CA1 levels over the 12-week infection period. CA1 is a promising negative serum biomarker for the diagnosis of S. mansoni infection.

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Evolution of carbonic anhydrases in fungi

Abstract: The ubiquitous metalloenzyme carbonic anhy-

Cited by 57 publications

References 42 publications

Carbonic anhydrase activators: Activation of the β-carbonic anhydrases from the pathogenic fungi Candida albicans and Cryptococcus neoformans with amines and amino acids

Carbonic anhydrase activators: Activation of the β-carbonic anhydrases from the pathogenic fungi Candida albicans and Cryptococcus neoformans with amines and amino acids

The evolution of metazoan α-carbonic anhydrases and their roles in calcium carbonate biomineralization

Serum Carbonic Anhydrase 1 is a Biomarker for Diagnosis of Human Schistosoma mansoni Infection

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