Elucidating the role of metal ions in carbonic anhydrase catalysis

Kim, Jin Kyun; Lee, Cheol; Lim, Sujeong; Adhikari, Aniruddha; Andring, Jacob T.; McKenna, Robert; Ghim, Cheol-Min; Kim, Chae Un

doi:10.1038/s41467-020-18425-5

Cited by 94 publications

(62 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Histidine residues are found in the active sites of many hydrolases, mainly in the form of histidine triads (including CA) [36,37]. Therefore, using histidine in the design of catalytic amyloids peptides can potentially uncover other types of hydrolytic activities.…”

Section: Catalytic Activity Emerging From Peptides Self-assembled Into Amyloidsmentioning

confidence: 99%

Catalytic Amyloids as Novel Synthetic Hydrolases

Duran-Meza

Díaz-Espinoza

2021

IJMS

View full text Add to dashboard Cite

Amyloids are supramolecular assemblies composed of polypeptides stabilized by an intermolecular beta-sheet core. These misfolded conformations have been traditionally associated with pathological conditions such as Alzheimer’s and Parkinson´s diseases. However, this classical paradigm has changed in the last decade since the discovery that the amyloid state represents a universal alternative fold accessible to virtually any polypeptide chain. Moreover, recent findings have demonstrated that the amyloid fold can serve as catalytic scaffolds, creating new opportunities for the design of novel active bionanomaterials. Here, we review the latest advances in this area, with particular emphasis on the design and development of catalytic amyloids that exhibit hydrolytic activities. To date, three different types of activities have been demonstrated: esterase, phosphoesterase and di-phosphohydrolase. These artificial hydrolases emerge upon the self-assembly of small peptides into amyloids, giving rise to catalytically active surfaces. The highly stable nature of the amyloid fold can provide an attractive alternative for the design of future synthetic hydrolases with diverse applications in the industry, such as the in situ decontamination of xenobiotics.

show abstract

Section: Catalytic Activity Emerging From Peptides Self-assembled Into Amyloidsmentioning

confidence: 99%

Catalytic Amyloids as Novel Synthetic Hydrolases

Duran-Meza

Díaz-Espinoza

2021

IJMS

View full text Add to dashboard Cite

show abstract

“…Water molecules present in the vicinity of biological systems are often characterized by unique interactions that grant them significantly different properties from those of bulk water. Despite the diverse profiles of biological entities, ranging from the surfaces of lipid bilayers, [10] channel proteins, [11] and grooves of DNA [12] to deeply buried active sites within enzymes, [13,14] there are certain common features and unique characteristics that distinguish water molecules in such environments. These characteristics typically stem from the fact that the extended hydrogen (H)‐bond network in bulk water is severely curtailed at biological interfaces, and it is often insightful to treat the relevant water molecules as a distinct category under the term “biological water” [15–33] …”

Section: Biological Watermentioning

confidence: 99%

“…For instance, single‐point mutation in native human carbonic anhydrase II can lead to the restructuring of water replenishment pathways that influence the electrostatic environment around the relevant reaction centers [13] . Such reorganization of the water network also occurs when the coordination geometries of the active‐site metal ions are altered in response to the substitution of native metal ions by their non‐native analogues [14] …”

Section: Biological Watermentioning

confidence: 99%

See 1 more Smart Citation

Hydrogen‐Bond Dynamics and Energetics of Biological Water

2020

Self Cite

View full text Add to dashboard Cite

Water molecules in the immediate vicinity of biomacromolecules and biomimetic organized assemblies often exhibit a markedly distinct behavior from that of their bulk counterparts. The overall sluggish behavior of biological water substantially affects the stability and integrity of biomolecules, as well as the successful execution of various crucial water‐mediated biochemical phenomena. In this Minireview, insights are provided into the features of truncated hydrogen‐bond networks that grant biological water its unique characteristics. In particular, experimental results and theoretical investigations, based on chemical kinetics, are presented that have shed light on the dynamics and energetics governing such characteristics. It is emphasized how such details help us to understand the energetics of biological water, an aspect relatively less explored than its dynamics. For instance, when biological water at hydrophilic or charged protein surfaces was explored, the free energy of H‐bond breakage was found to be of the order of 0.4 kcal mol−1 higher than that of bulk water.

show abstract

“…CAs are zinc-binding enzymes that catalyze the reversible conversion of carbon dioxide and water to bicarbonate and one proton (Tripp et al, 2001). The zinc-binding is mediated by three histidine residues essential for the protein's catalytic function (Aspatwar et al, 2014;Kim et al, 2020). CAs are involved in many physiological processes requiring ion regulation or carbon transport (Supuran, 2016), both of which are crucial for the controlled precipitation of carbonate biominerals.…”

Section: Introductionmentioning

confidence: 99%

Carbonic Anhydrases: An Ancient Tool in Calcareous Sponge Biomineralization

et al. 2021

View full text Add to dashboard Cite

Enzymes of the α-carbonic anhydrase gene family (CAs) are essential for the deposition of calcium carbonate biominerals. In calcareous sponges (phylum Porifera, class Calcarea), specific CAs are involved in the formation of calcite spicules, a unique trait and synapomorphy of this class. However, detailed studies on the CA repertoire of calcareous sponges exist for only two species of one of the two Calcarea subclasses, the Calcaronea. The CA repertoire of the second subclass, the Calcinea, has not been investigated so far, leaving a considerable gap in our knowledge about this gene family in Calcarea. Here, using transcriptomic analysis, phylogenetics, and in situ hybridization, we study the CA repertoire of four additional species of calcareous sponges, including three from the previously unsampled subclass Calcinea. Our data indicate that the last common ancestor of Calcarea had four ancestral CAs with defined subcellular localizations and functions (mitochondrial/cytosolic, membrane-bound, and secreted non-catalytic). The evolution of membrane-bound and secreted CAs involved gene duplications and losses, whereas mitochondrial/cytosolic and non-catalytic CAs are evidently orthologous genes. Mitochondrial/cytosolic CAs are biomineralization-specific genes recruited for biomineralization in the last common ancestor of calcareous sponges. The spatial–temporal expression of these CAs differs between species, which may reflect differences between subclasses or be related to the secondary thickening of spicules during biomineralization that does not occur in all species. With this study, we extend the understanding of the role and the evolution of a key biomineralization gene in calcareous sponges.

show abstract

Elucidating the role of metal ions in carbonic anhydrase catalysis

Cited by 94 publications

References 51 publications

Catalytic Amyloids as Novel Synthetic Hydrolases

Catalytic Amyloids as Novel Synthetic Hydrolases

Hydrogen‐Bond Dynamics and Energetics of Biological Water

Carbonic Anhydrases: An Ancient Tool in Calcareous Sponge Biomineralization

Contact Info

Product

Resources

About