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Environmental Microbiology Reports Jun 2022The alpha/beta-fold superfamily of hydrolases is rapidly becoming one of the largest groups of structurally related enzymes with diverse catalytic functions. In this... (Review)
Review
The alpha/beta-fold superfamily of hydrolases is rapidly becoming one of the largest groups of structurally related enzymes with diverse catalytic functions. In this superfamily of enzymes, esterase deserves special attention because of their wide distribution in biological systems and importance towards environmental and industrial applications. Among various esterases, phthalate hydrolases are the key alpha/beta enzymes involved in the metabolism of structurally diverse estrogenic phthalic acid esters, ubiquitously distributed synthetic chemicals, used as plasticizer in plastic manufacturing processes. Although they vary both at the sequence and functional levels, these hydrolases use a similar acid-base-nucleophile catalytic mechanism to catalyse reactions on structurally different substrates. The current review attempts to present insights on phthalate hydrolases, describing their sources, structural diversities, phylogenetic affiliations and catalytically different types or classes of enzymes, categorized as diesterase, monoesterase and diesterase-monoesterase, capable of hydrolysing phthalate diester, phthalate monoester and both respectively. Furthermore, available information on in silico analyses and site-directed mutagenesis studies revealing structure-function integrity and altered enzyme kinetics have been highlighted along with the possible scenario of their evolution at the molecular level.
Topics: Esterases; Evolution, Molecular; Hydrolases; Phthalic Acids; Phylogeny
PubMed: 34816599
DOI: 10.1111/1758-2229.13028 -
Glycobiology Sep 2022The substitution and de-substitution of carbohydrate materials are important steps in the biosynthesis and/or breakdown of a wide variety of biologically important... (Review)
Review
The substitution and de-substitution of carbohydrate materials are important steps in the biosynthesis and/or breakdown of a wide variety of biologically important polymers. The SGNH hydrolase superfamily is a group of related and well-studied proteins with a highly conserved catalytic fold and mechanism composed of 16 member families. SGNH hydrolases can be found in vertebrates, plants, fungi, bacteria, and archaea, and play a variety of important biological roles related to biomass conversion, pathogenesis, and cell signaling. The SGNH hydrolase superfamily is chiefly composed of a diverse range of carbohydrate-modifying enzymes, including but not limited to the carbohydrate esterase families 2, 3, 6, 12 and 17 under the carbohydrate-active enzyme classification system and database (CAZy.org). In this review, we summarize the structural and functional features that delineate these subfamilies of SGNH hydrolases, and which generate the wide variety of substrate preferences and enzymatic activities observed of these proteins to date.
Topics: Biopolymers; Carbohydrates; Esterases; Hydrolases; Protein Conformation
PubMed: 35871440
DOI: 10.1093/glycob/cwac045 -
Prostaglandins & Other Lipid Mediators Nov 2017Soluble epoxide hydrolase (sEH) is a bifunctional enzyme that exhibits lipid epoxide hydrolase (sEH-H) and lipid phosphatase activity (sEH-P), with each being located in... (Review)
Review
Soluble epoxide hydrolase (sEH) is a bifunctional enzyme that exhibits lipid epoxide hydrolase (sEH-H) and lipid phosphatase activity (sEH-P), with each being located in its own distinct domain. While the epoxide hydrolase activity is well-investigated, the role of the phosphatase domain remains unclear. This article briefly summarizes the evolution, structure and SNPs of the human sEH, with a special focus on the function and postulated role of the N-terminal domain of sEH. Furthermore, the article provides an overview of tools to study sEH-P.
Topics: Animals; Epoxide Hydrolases; Humans; Phosphoric Monoester Hydrolases; Polymorphism, Single Nucleotide; Solubility
PubMed: 28729091
DOI: 10.1016/j.prostaglandins.2017.07.002 -
Biotechnology Advances 2021Xylan is the most abundant hemicellulose in nature and as such it is a huge source of renewable carbon. Its bioconversion requires a battery of xylanolytic enzymes. Of... (Review)
Review
Xylan is the most abundant hemicellulose in nature and as such it is a huge source of renewable carbon. Its bioconversion requires a battery of xylanolytic enzymes. Of them the most important are the endo-β-1,4-xylanases which depolymerize the polysaccharide into smaller fragments. Most of the xylanases are members of glycoside hydrolase (GH) families 10 and 11, although they are classified in some other GH families. The relatively new xylanases of GH30 are of special interest. Initially, they appeared to be specific glucuronoxylanases, however, other specificities were found later among prokaryotic and in particular eukaryotic enzymes. This review gives an overview of the substrate and product specificities observed for the GH30 xylanases characterized to date. An emphasis is given to the structure-activity relationship in order to explain how minor differences in catalytic centre and its vicinity can alter catalytic properties from the endoxylanase into the reducing end xylose releasing exoxylanase or into the non-reducing end xylobiohydrolase. Biotechnological potential of the GH30 xylanases is also considered.
Topics: Endo-1,4-beta Xylanases; Glycoside Hydrolases; Substrate Specificity; Xylans; Xylose
PubMed: 33548454
DOI: 10.1016/j.biotechadv.2021.107704 -
Prostaglandins & Other Lipid Mediators Aug 2002The leukotrienes (LTs) are a family of lipid mediators involved in inflammation and allergy. Leukotriene B4 is a classical chemoattractant, which triggers adherence and... (Review)
Review
The leukotrienes (LTs) are a family of lipid mediators involved in inflammation and allergy. Leukotriene B4 is a classical chemoattractant, which triggers adherence and aggregation of leukocytes to the endothelium at only nanomolar concentrations. In addition, leukotriene B4 modulates immune responses, participates in the host-defense against infections, and is a key mediator of PAF-induced lethal shock. Because of these powerful biological effects, leukotriene B4 is implicated in a variety of acute and chronic inflammatory diseases, e.g. nephritis, arthritis, dermatitis, and chronic obstructive pulmonary disease. The final step in the biosynthesis of leukotriene B4 is catalyzed by leukotriene A4 hydrolase, a unique bi-functional zinc metalloenzyme with an anion-dependent aminopeptidase activity. Here we describe the most recent developments regarding our understanding of the structure, function, and catalytic mechanisms of leukotriene A4 hydrolase.
Topics: Amino Acids; Animals; Catalytic Domain; Enzyme Inhibitors; Epoxide Hydrolases; Humans; Leukotrienes; Ligands; Molecular Structure; Phylogeny; Protein Binding; Protein Structure, Tertiary
PubMed: 12432939
DOI: 10.1016/s0090-6980(02)00051-5 -
ChemSusChem Oct 2021The research on polyethylene terephthalate (PET) hydrolyzing enzymes started in 2005; several studies are now nearing the objective of their application in biorecycling... (Review)
Review
The research on polyethylene terephthalate (PET) hydrolyzing enzymes started in 2005; several studies are now nearing the objective of their application in biorecycling of PET, which is an urgent environmental issue. The thermostability of PET hydrolases must be higher than 70 °C, which has already been established by several thermophilic cutinases, as higher thermostability results in higher activity. Additionally, pretreatment of waste PET to more enzyme-attackable forms is necessary for PET biorecycling. This Minireview summarizes research on enzymatic PET hydrolysis from two viewpoints: 1) improvement of PET hydrolases by focusing on their thermostabilities by mutation of enzyme genes, their expression in several hosts, and their modifications; and 2) processing of waste PET to readily biodegradable forms. Finally, the outlook of PET biorecycling is described.
Topics: Animals; Bacteria; Binding Sites; Carboxylic Ester Hydrolases; Gene Expression Regulation; Humans; Hydrolases; Hydrolysis; Models, Molecular; Mutation; Nanoparticles; Polyethylene Terephthalates; Protein Binding; Protein Conformation; Protein Stability; Structure-Activity Relationship
PubMed: 33949146
DOI: 10.1002/cssc.202100740 -
Current Protein & Peptide Science 2017The α/β hydrolase fold superfamily is an ancient and widely diversified group of primarily hydrolytic enzymes. In this review, the adaptations of these proteins to the... (Review)
Review
The α/β hydrolase fold superfamily is an ancient and widely diversified group of primarily hydrolytic enzymes. In this review, the adaptations of these proteins to the pathogenic lifestyle of Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis, are examined. Of the 105 α/β hydrolases identified in Mtb, many are associated with lipid metabolism, particularly in the biosynthesis and maintenance of the Mtb's unique cell envelope, as well in the large number of extracellular lipases that are likely responsible for degradation of host lipid material. α/β hydrolase fold proteins are also involved in the evasion and modulation of the immune response, detoxification and metabolic adaptations, including growth, response to acidification of the intracellular environment and dormancy. A striking feature of Mtb's α/β hydrolases is their diversification into virulence-associated niches. It is clear that the α/β hydrolase fold family has made a significant contribution to Mtb's remarkable success as a pathogen.
Topics: Bacterial Adhesion; Bacterial Proteins; Host-Parasite Interactions; Humans; Hydrolases; Models, Molecular; Mycobacterium tuberculosis; Protein Folding
PubMed: 27480283
DOI: 10.2174/1389203717666160729093515 -
Protein and Peptide Letters 2009The alpha/beta hydrolase superfamily has rapidly expanded in recent years and continues to do so at an expeditious pace. According to the ESTHER database... (Review)
Review
The alpha/beta hydrolase superfamily has rapidly expanded in recent years and continues to do so at an expeditious pace. According to the ESTHER database (http://bioweb.ensam.inra.fr/ESTHER) 29000 papers have been published cataloguing 89 family groups, comprising a total of 15438 gene loci and 666 structures. This paper presents a snapshot of the current family taxonomy, catalytic chemistries, structural topologies and useful technologies emerging from the knowledge base at the current time.
Topics: Animals; Catalytic Domain; Humans; Hydrolases; Models, Molecular; Multigene Family; Protein Folding; Protein Structure, Tertiary; Structure-Activity Relationship; Substrate Specificity
PubMed: 19508187
DOI: 10.2174/092986609789071298 -
Biochimica Et Biophysica Acta Jul 2014Peptidyl-tRNA hydrolase is an essential enzyme which acts as one of the rescue factors of the stalled ribosomes. It is an esterase that hydrolyzes the ester bond in the... (Review)
Review
Peptidyl-tRNA hydrolase is an essential enzyme which acts as one of the rescue factors of the stalled ribosomes. It is an esterase that hydrolyzes the ester bond in the peptidyl-tRNA molecules, which are products of ribosome stalling. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death. Over the recent years, it has been heralded as an attractive drug target for antimicrobial therapeutics. Two distinct classes of peptidyl-tRNA hydrolase, Pth and Pth2, have been identified in nature. This review gives an overview of the structural and functional aspects of Pth, along with its sequence and structural comparison among various species of bacteria. While the mode of binding of the substrate to Pth and the mechanism of hydrolysis are still speculated upon, the structure-based drug design using this protein as the target is still largely unexplored. This review focuses on the structural features of Pth, giving a direction to structure-based drug design on this protein.
Topics: Bacteria; Carboxylic Ester Hydrolases; Hydrolysis; Substrate Specificity
PubMed: 24768774
DOI: 10.1016/j.bbapap.2014.04.012 -
Chembiochem : a European Journal of... Jul 2011The superfamily of α/β-hydrolase fold enzymes is one of the largest known protein families, including a broad range of synthetically useful enzymes such as lipases,... (Review)
Review
The superfamily of α/β-hydrolase fold enzymes is one of the largest known protein families, including a broad range of synthetically useful enzymes such as lipases, esterases, amidases, hydroxynitrile lyases, epoxide hydrolases and dehalogenases. This minireview covers methods developed for efficient protein engineering of these enzymes. Special emphasis is placed on the alteration of enzyme properties such as substrate range, thermostability and enantioselectivity for their application in biocatalysis. In addition, concepts for the investigation of the evolutionary relationship between the different members of this protein superfamily are covered, together with successful examples.
Topics: Amino Acid Sequence; Bacteria; Directed Molecular Evolution; Fungi; Hydrolases; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Engineering; Sequence Alignment
PubMed: 21506229
DOI: 10.1002/cbic.201000771