A critical review on marine serine protease and its inhibitors: A new wave of drugs?

Barzkar, Noora; Khan, Zaheer; Jahromi, Saeid Tamadoni; Pourmozaffar, Sajjad; Gozari, Mohsen; Nahavandi, Reza

doi:10.1016/j.ijbiomac.2020.12.134

Cited by 27 publications

(15 citation statements)

References 188 publications

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“…Even though these enzymes have been characterized from a wide range of different sources, microbial fibrinolytic enzymes are considered attractive tools due to their features, such as enhanced specificity [8], low production cost [8], comparatively high yield [28] and the possibility to be genetically modified by recombinant DNA technology and protein engineering approaches [29]. Marine ecosystems serve as a reservoir of microorganisms producing important therapeutic metabolites, especially enzymes [30][31][32][33][34][35][36][37][38][39], but they remain largely unexplored to date. Due to the wide biodiversity of the marine environment, marine microorganisms can provide a diverse array of enzymes for biotechnological development, with possible improved pharmacological properties and lesser side effects [40].…”

Section: Introductionmentioning

confidence: 99%

Marine Microbial Fibrinolytic Enzymes: An Overview of Source, Production, Biochemical Properties and Thrombolytic Activity

2022

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Cardiovascular diseases (CVDs) have emerged as a major threat to global health resulting in a decrease in life expectancy with respect to humans. Thrombosis is one of the foremost causes of CVDs, and it is characterized by the unwanted formation of fibrin clots. Recently, microbial fibrinolytic enzymes due to their specific features have gained much more attention than conventional thrombolytic agents for the treatment of thrombosis. Marine microorganisms including bacteria and microalgae have the significant ability to produce fibrinolytic enzymes with improved pharmacological properties and lesser side effects and, hence, are considered as prospective candidates for large scale production of these enzymes. The current review presents an outline regarding isolation sources, production, features, and thrombolytic potential of fibrinolytic biocatalysts from marine microorganisms identified so far.

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Section: Introductionmentioning

confidence: 99%

Marine Microbial Fibrinolytic Enzymes: An Overview of Source, Production, Biochemical Properties and Thrombolytic Activity

2022

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“…Serine is often phosphorylated, glycosylated or N-acetylated. These post-translational modifications are crucial for organic life ( Barzkar et al., 2021 ), and is a precursor in the biosynthesis of other amino acids like glycine, cysteine, and D-serine ( Murtas et al., 2020 ). SER is also essential in the production of phosphoglycerides, glycerides, sphingolipids and phosphatidylserine ( Hirabayashi and Furuya, 2008 ; Kent, 1995 ).…”

Section: Introductionmentioning

confidence: 99%

3D interaction homology: Hydropathic interaction environments of serine and cysteine are strikingly different and their roles adapt in membrane proteins

Catalano

Mughram

Guo

et al. 2021

Current Research in Structural Biology

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Atomic-resolution protein structural models are prerequisites for many downstream activities like structure-function studies or structure-based drug discovery. Unfortunately, this data is often unavailable for some of the most interesting and therapeutically important proteins. Thus, computational tools for building native-like structural models from less-than-ideal experimental data are needed. To this end, interaction homology exploits the character, strength and loci of the sets of interactions that define a structure. Each residue type has its own limited set of backbone angle-dependent interaction motifs, as defined by their environments. In this work, we characterize the interactions of serine, cysteine and S-bridged cysteine in terms of 3D hydropathic environment maps. As a result, we explore several intriguing questions. Are the environments different between the isosteric serine and cysteine residues? Do some environments promote the formation of cystine S–S bonds? With the increasing availability of structural data for water-insoluble membrane proteins, are there environmental differences for these residues between soluble and membrane proteins? The environments surrounding serine and cysteine residues are dramatically different: serine residues are about 50% solvent exposed, while cysteines are only 10% exposed; the latter are more involved in hydrophobic interactions although there are backbone angle-dependent differences. Our analysis suggests that one driving force for –S–S– bond formation is a rather substantial increase in burial and hydrophobic interactions in cystines. Serine and cysteine become less and more, respectively, solvent-exposed in membrane proteins. 3D hydropathic environment maps are an evolving structure analysis tool showing promise as elements in a new protein structure prediction paradigm.

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“…The marine ecosystem is considered the largest ecosystem, covering ~70% of this planet [ 1 , 2 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 ] and giving it a unique feature in the known universe. Reportedly, marine ecosystems make up the habitat of >80% of the living beings found on earth [ 11 , 12 , 13 , 14 ].…”

Section: Introductionmentioning

confidence: 99%

Alginate Lyases from Marine Bacteria: An Enzyme Ocean for Sustainable Future

et al. 2022

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The cell wall of brown algae contains alginate as a major constituent. This anionic polymer is a composite of β-d-mannuronate (M) and α-l-guluronate (G). Alginate can be degraded into oligosaccharides; both the polymer and its products exhibit antioxidative, antimicrobial, and immunomodulatory activities and, hence, find many commercial applications. Alginate is attacked by various enzymes, collectively termed alginate lyases, that degrade glycosidic bonds through β-elimination. Considering the abundance of brown algae in marine ecosystems, alginate is an important source of nutrients for marine organisms, and therefore, alginate lyases play a significant role in marine carbon recycling. Various marine microorganisms, particularly those that thrive in association with brown algae, have been reported as producers of alginate lyases. Conceivably, the marine-derived alginate lyases demonstrate salt tolerance, and many are activated in the presence of salts and, therefore, find applications in the food industry. Therefore, this review summarizes the structural and biochemical features of marine bacterial alginate lyases along with their applications. This comprehensive information can aid in the expansion of future prospects of alginate lyases.

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A critical review on marine serine protease and its inhibitors: A new wave of drugs?

Cited by 27 publications

References 188 publications

Marine Microbial Fibrinolytic Enzymes: An Overview of Source, Production, Biochemical Properties and Thrombolytic Activity

Marine Microbial Fibrinolytic Enzymes: An Overview of Source, Production, Biochemical Properties and Thrombolytic Activity

3D interaction homology: Hydropathic interaction environments of serine and cysteine are strikingly different and their roles adapt in membrane proteins

Alginate Lyases from Marine Bacteria: An Enzyme Ocean for Sustainable Future

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